A class of enzymes that catalyze oxidation-reduction reactions of amino acids.
The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possible; as an alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor. (Enzyme Nomenclature, 1992, p9)
Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.
An enzyme that catalyzes the reduction of a protein-disulfide in the presence of glutathione, forming a protein-dithiol. Insulin is one of its substrates. EC 1.8.4.2.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
A ferredoxin-containing enzyme that catalyzes the COENZYME A-dependent oxidative decarboxylation of PYRUVATE to acetyl-COENZYME A and CARBON DIOXIDE.
A group of oxidoreductases that act on NADH or NADPH. In general, enzymes using NADH or NADPH to reduce a substrate are classified according to the reverse reaction, in which NAD+ or NADP+ is formally regarded as an acceptor. This subclass includes only those enzymes in which some other redox carrier is the acceptor. (Enzyme Nomenclature, 1992, p100) EC 1.6.
A subclass of enzymes which includes all dehydrogenases acting on primary and secondary alcohols as well as hemiacetals. They are further classified according to the acceptor which can be NAD+ or NADP+ (subclass 1.1.1), cytochrome (1.1.2), oxygen (1.1.3), quinone (1.1.5), or another acceptor (1.1.99).
The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.
Oxidoreductases that are specific for KETONES.
A family of thioltransferases that contain two active site CYSTEINE residues, which either form a disulfide (oxidized form) or a dithiol (reduced form). They function as an electron carrier in the GLUTHIONE-dependent synthesis of deoxyribonucleotides by RIBONUCLEOTIDE REDUCTASES and may play a role in the deglutathionylation of protein thiols. The oxidized forms of glutaredoxins are directly reduced by the GLUTATHIONE.
The naturally occurring or experimentally induced replacement of one or more AMINO ACIDS in a protein with another. If a functionally equivalent amino acid is substituted, the protein may retain wild-type activity. Substitution may also diminish, enhance, or eliminate protein function. Experimentally induced substitution is often used to study enzyme activities and binding site properties.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.
Sulfur-sulfur bond isomerases that catalyze the rearrangement of disulfide bonds within proteins during folding. Specific protein disulfide-isomerase isoenzymes also occur as subunits of PROCOLLAGEN-PROLINE DIOXYGENASE.
A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
Oxidoreductases with specificity for oxidation or reduction of SULFUR COMPOUNDS.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
Hydrogen-donating proteins that participates in a variety of biochemical reactions including ribonucleotide reduction and reduction of PEROXIREDOXINS. Thioredoxin is oxidized from a dithiol to a disulfide when acting as a reducing cofactor. The disulfide form is then reduced by NADPH in a reaction catalyzed by THIOREDOXIN REDUCTASE.
Amino acids that are not synthesized by the human body in amounts sufficient to carry out physiological functions. They are obtained from dietary foodstuffs.
Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.
Cellular proteins and protein complexes that transport amino acids across biological membranes.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
NAD(P)H:(quinone acceptor) oxidoreductases. A family that includes three enzymes which are distinguished by their sensitivity to various inhibitors. EC 1.6.99.2 (NAD(P)H DEHYDROGENASE (QUINONE);) is a flavoprotein which reduces various quinones in the presence of NADH or NADPH and is inhibited by dicoumarol. EC 1.6.99.5 (NADH dehydrogenase (quinone)) requires NADH, is inhibited by AMP and 2,4-dinitrophenol but not by dicoumarol or folic acid derivatives. EC 1.6.99.6 (NADPH dehydrogenase (quinone)) requires NADPH and is inhibited by dicoumarol and folic acid derivatives but not by 2,4-dinitrophenol.
A broad category of oxidoreductases that either reduce double bonds or oxidize single bonds between OXYGEN and CARBON in organic compounds.
Proteins found in any species of bacterium.
The rate dynamics in chemical or physical systems.
A flavoprotein oxidase complex that contains iron-sulfur centers. It catalyzes the oxidation of SUCCINATE to fumarate and couples the reaction to the reduction of UBIQUINONE to ubiquinol.
Chemical groups containing the covalent disulfide bonds -S-S-. The sulfur atoms can be bound to inorganic or organic moieties.
Proteins prepared by recombinant DNA technology.
A kingdom of hyperthermophilic ARCHAEA found in diverse environments.
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
The sequential correspondence of nucleotides in one nucleic acid molecule with those of another nucleic acid molecule. Sequence homology is an indication of the genetic relatedness of different organisms and gene function.
A genus of gram-negative, anaerobic, rod-shaped bacteria isolated from the bovine RUMEN, the human gingival sulcus, and dental PULPITIS infections.
Commonly observed structural components of proteins formed by simple combinations of adjacent secondary structures. A commonly observed structure may be composed of a CONSERVED SEQUENCE which can be represented by a CONSENSUS SEQUENCE.
The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.
A thiol-containing non-essential amino acid that is oxidized to form CYSTINE.
A FLAVOPROTEIN enzyme that catalyzes the oxidation of THIOREDOXINS to thioredoxin disulfide in the presence of NADP+. It was formerly listed as EC 1.6.4.5
A flavoprotein containing oxidoreductase that catalyzes the dehydrogenation of SUCCINATE to fumarate. In most eukaryotic organisms this enzyme is a component of mitochondrial electron transport complex II.
The functional hereditary units of BACTERIA.
The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.
The relationships of groups of organisms as reflected by their genetic makeup.
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.
Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.
Single-stranded complementary DNA synthesized from an RNA template by the action of RNA-dependent DNA polymerase. cDNA (i.e., complementary DNA, not circular DNA, not C-DNA) is used in a variety of molecular cloning experiments as well as serving as a specific hybridization probe.
The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups.
Amino acids containing an aromatic side chain.
The process by which ELECTRONS are transported from a reduced substrate to molecular OXYGEN. (From Bennington, Saunders Dictionary and Encyclopedia of Laboratory Medicine and Technology, 1984, p270)
A subclass of enzymes which includes all dehydrogenases acting on carbon-carbon bonds. This enzyme group includes all the enzymes that introduce double bonds into substrates by direct dehydrogenation of carbon-carbon single bonds.
The sum of the weight of all the atoms in a molecule.
Amino acids which have a branched carbon chain.
The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to alpha helices, beta strands (which align to form beta sheets) or other types of coils. This is the first folding level of protein conformation.
Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.
Ecosystem and environmental activities, functions, or events.
An enzyme of the oxidoreductase class that catalyzes the conversion of beta-D-glucose and oxygen to D-glucono-1,5-lactone and peroxide. It is a flavoprotein, highly specific for beta-D-glucose. The enzyme is produced by Penicillium notatum and other fungi and has antibacterial activity in the presence of glucose and oxygen. It is used to estimate glucose concentration in blood or urine samples through the formation of colored dyes by the hydrogen peroxide produced in the reaction. (From Enzyme Nomenclature, 1992) EC 1.1.3.4.
A sequence of amino acids in a polypeptide or of nucleotides in DNA or RNA that is similar across multiple species. A known set of conserved sequences is represented by a CONSENSUS SEQUENCE. AMINO ACID MOTIFS are often composed of conserved sequences.
An essential branched-chain amino acid important for hemoglobin formation.
Nicotinamide adenine dinucleotide phosphate. A coenzyme composed of ribosylnicotinamide 5'-phosphate (NMN) coupled by pyrophosphate linkage to the 5'-phosphate adenosine 2',5'-bisphosphate. It serves as an electron carrier in a number of reactions, being alternately oxidized (NADP+) and reduced (NADPH). (Dorland, 27th ed)
An enzyme that catalyzes the oxidation and reduction of FERREDOXIN or ADRENODOXIN in the presence of NADP. EC 1.18.1.2 was formerly listed as EC 1.6.7.1 and EC 1.6.99.4.
Oxidoreductases that are specific for ALDEHYDES.
A multistage process that includes cloning, physical mapping, subcloning, determination of the DNA SEQUENCE, and information analysis.
A condensation product of riboflavin and adenosine diphosphate. The coenzyme of various aerobic dehydrogenases, e.g., D-amino acid oxidase and L-amino acid oxidase. (Lehninger, Principles of Biochemistry, 1982, p972)
A coenzyme composed of ribosylnicotinamide 5'-diphosphate coupled to adenosine 5'-phosphate by pyrophosphate linkage. It is found widely in nature and is involved in numerous enzymatic reactions in which it serves as an electron carrier by being alternately oxidized (NAD+) and reduced (NADH). (Dorland, 27th ed)
Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
A flavoprotein and iron sulfur-containing oxidoreductase complex that catalyzes the conversion of UBIQUINONE to ubiquinol. In MITOCHONDRIA the complex also couples its reaction to the transport of PROTONS across the internal mitochondrial membrane. The NADH DEHYDROGENASE component of the complex can be isolated and is listed as EC 1.6.99.3.
A flavoprotein that reversibly catalyzes the oxidation of NADH or NADPH by various quinones and oxidation-reduction dyes. The enzyme is inhibited by dicoumarol, capsaicin, and caffeine.
Extrachromosomal, usually CIRCULAR DNA molecules that are self-replicating and transferable from one organism to another. They are found in a variety of bacterial, archaeal, fungal, algal, and plant species. They are used in GENETIC ENGINEERING as CLONING VECTORS.
Small molecules that are required for the catalytic function of ENZYMES. Many VITAMINS are coenzymes.
Processes involved in the formation of TERTIARY PROTEIN STRUCTURE.
A genus of basidiomycetous fungi, family POLYPORACEAE, order POLYPORALES, that grows on logs or tree stumps in shelflike layers. The species P. ostreatus, the oyster mushroom, is a choice edible species and is the most frequently encountered member of the genus in eastern North America. (Alexopoulos et al., Introductory Mycology, 4th ed, p531)
(5Z)-(15S)-11 alpha-Hydroxy-9,15-dioxoprostanoate:NAD(P)+ delta(13)-oxidoreductase. An enzyme active in prostaglandin E and F catabolism. It catalyzes the reduction of the double bond at the 13-14 position of the 15-ketoprostaglandins and uses NADPH as cofactor. EC 1.3.1.48.
A multistage process that includes the determination of a sequence (protein, carbohydrate, etc.), its fragmentation and analysis, and the interpretation of the resulting sequence information.
A group of proteins possessing only the iron-sulfur complex as the prosthetic group. These proteins participate in all major pathways of electron transport: photosynthesis, respiration, hydroxylation and bacterial hydrogen and nitrogen fixation.
A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine).
Systems of enzymes which function sequentially by catalyzing consecutive reactions linked by common metabolic intermediates. They may involve simply a transfer of water molecules or hydrogen atoms and may be associated with large supramolecular structures such as MITOCHONDRIA or RIBOSOMES.
Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are linear polypeptides that are normally synthesized on RIBOSOMES.
Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.
Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.
Derivatives of the dimethylisoalloxazine (7,8-dimethylbenzo[g]pteridine-2,4(3H,10H)-dione) skeleton. Flavin derivatives serve an electron transfer function as ENZYME COFACTORS in FLAVOPROTEINS.
Cells lacking a nuclear membrane so that the nuclear material is either scattered in the cytoplasm or collected in a nucleoid region.
Use of restriction endonucleases to analyze and generate a physical map of genomes, genes, or other segments of DNA.
A set of genes descended by duplication and variation from some ancestral gene. Such genes may be clustered together on the same chromosome or dispersed on different chromosomes. Examples of multigene families include those that encode the hemoglobins, immunoglobulins, histocompatibility antigens, actins, tubulins, keratins, collagens, heat shock proteins, salivary glue proteins, chorion proteins, cuticle proteins, yolk proteins, and phaseolins, as well as histones, ribosomal RNA, and transfer RNA genes. The latter three are examples of reiterated genes, where hundreds of identical genes are present in a tandem array. (King & Stanfield, A Dictionary of Genetics, 4th ed)
A sequence of successive nucleotide triplets that are read as CODONS specifying AMINO ACIDS and begin with an INITIATOR CODON and end with a stop codon (CODON, TERMINATOR).
A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement.
A class of enzymes that catalyze geometric or structural changes within a molecule to form a single product. The reactions do not involve a net change in the concentrations of compounds other than the substrate and the product.(from Dorland, 28th ed) EC 5.
Established cell cultures that have the potential to propagate indefinitely.
A non-essential amino acid that occurs in high levels in its free state in plasma. It is produced from pyruvate by transamination. It is involved in sugar and acid metabolism, increases IMMUNITY, and provides energy for muscle tissue, BRAIN, and the CENTRAL NERVOUS SYSTEM.
Enzymes catalyzing the dehydrogenation of or oxidation of compounds containing primary amines.
Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes.
The degree of similarity between sequences. Studies of AMINO ACID SEQUENCE HOMOLOGY and NUCLEIC ACID SEQUENCE HOMOLOGY provide useful information about the genetic relatedness of genes, gene products, and species.
Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.
A photo-active pigment localized in prolamellar bodies occurring within the proplastids of dark-grown bean leaves. In the process of photoconversion, the highly fluorescent protochlorophyllide is converted to chlorophyll.
The process of cumulative change at the level of DNA; RNA; and PROTEINS, over successive generations.
Stable elementary particles having the smallest known negative charge, present in all elements; also called negatrons. Positively charged electrons are called positrons. The numbers, energies and arrangement of electrons around atomic nuclei determine the chemical identities of elements. Beams of electrons are called CATHODE RAYS.
The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.
The extent to which an enzyme retains its structural conformation or its activity when subjected to storage, isolation, and purification or various other physical or chemical manipulations, including proteolytic enzymes and heat.
Proteins obtained from ESCHERICHIA COLI.
Compounds containing the -SH radical.
RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.
Amino acid transporter systems capable of transporting basic amino acids (AMINO ACIDS, BASIC).
An enzyme that utilizes NADH or NADPH to reduce FLAVINS. It is involved in a number of biological processes that require reduced flavin for their functions such as bacterial bioluminescence. Formerly listed as EC 1.6.8.1 and EC 1.5.1.29.
The space between the inner and outer membranes of a cell that is shared with the cell wall.
The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
An essential branched-chain aliphatic amino acid found in many proteins. It is an isomer of LEUCINE. It is important in hemoglobin synthesis and regulation of blood sugar and energy levels.
A glucose dehydrogenase that catalyzes the oxidation of beta-D-glucose to form D-glucono-1,5-lactone, using NAD as well as NADP as a coenzyme.
Non-pathogenic ovoid to rod-shaped bacteria that are widely distributed and found in fresh water as well as marine and hypersaline habitats.
A low-molecular-weight (16,000) iron-free flavoprotein containing one molecule of flavin mononucleotide (FMN) and isolated from bacteria grown on an iron-deficient medium. It can replace ferredoxin in all the electron-transfer functions in which the latter is known to serve in bacterial cells.
Amino acids with side chains that are positively charged at physiological pH.
Proteins found in any species of fungus.
An essential amino acid. It is often added to animal feed.
Theoretical representations that simulate the behavior or activity of chemical processes or phenomena; includes the use of mathematical equations, computers, and other electronic equipment.
A test used to determine whether or not complementation (compensation in the form of dominance) will occur in a cell with a given mutant phenotype when another mutant genome, encoding the same mutant phenotype, is introduced into that cell.
The restriction of a characteristic behavior, anatomical structure or physical system, such as immune response; metabolic response, or gene or gene variant to the members of one species. It refers to that property which differentiates one species from another but it is also used for phylogenetic levels higher or lower than the species.
Short sequences (generally about 10 base pairs) of DNA that are complementary to sequences of messenger RNA and allow reverse transcriptases to start copying the adjacent sequences of mRNA. Primers are used extensively in genetic and molecular biology techniques.
Transport proteins that carry specific substances in the blood or across cell membranes.
Deoxyribonucleic acid that makes up the genetic material of bacteria.
An analytical method used in determining the identity of a chemical based on its mass using mass analyzers/mass spectrometers.
A set of three nucleotides in a protein coding sequence that specifies individual amino acids or a termination signal (CODON, TERMINATOR). Most codons are universal, but some organisms do not produce the transfer RNAs (RNA, TRANSFER) complementary to all codons. These codons are referred to as unassigned codons (CODONS, NONSENSE).
Multicellular, eukaryotic life forms of kingdom Plantae (sensu lato), comprising the VIRIDIPLANTAE; RHODOPHYTA; and GLAUCOPHYTA; all of which acquired chloroplasts by direct endosymbiosis of CYANOBACTERIA. They are characterized by a mainly photosynthetic mode of nutrition; essentially unlimited growth at localized regions of cell divisions (MERISTEMS); cellulose within cells providing rigidity; the absence of organs of locomotion; absence of nervous and sensory systems; and an alternation of haploid and diploid generations.
Catalyzes the oxidation of GLUTATHIONE to GLUTATHIONE DISULFIDE in the presence of NADP+. Deficiency in the enzyme is associated with HEMOLYTIC ANEMIA. Formerly listed as EC 1.6.4.2.
One of the three domains of life (the others being BACTERIA and Eukarya), formerly called Archaebacteria under the taxon Bacteria, but now considered separate and distinct. They are characterized by: (1) the presence of characteristic tRNAs and ribosomal RNAs; (2) the absence of peptidoglycan cell walls; (3) the presence of ether-linked lipids built from branched-chain subunits; and (4) their occurrence in unusual habitats. While archaea resemble bacteria in morphology and genomic organization, they resemble eukarya in their method of genomic replication. The domain contains at least four kingdoms: CRENARCHAEOTA; EURYARCHAEOTA; NANOARCHAEOTA; and KORARCHAEOTA.
The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
A pyrrolo-quinoline having two adjacent keto-groups at the 4 and 5 positions and three acidic carboxyl groups. It is a coenzyme of some DEHYDROGENASES.
A species of gram-positive bacteria that is a common soil and water saprophyte.
The phenomenon whereby compounds whose molecules have the same number and kind of atoms and the same atomic arrangement, but differ in their spatial relationships. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)
The phenotypic manifestation of a gene or genes by the processes of GENETIC TRANSCRIPTION and GENETIC TRANSLATION.
Enzymes of the oxidoreductase class that catalyze the dehydrogenation of hydroxysteroids. (From Enzyme Nomenclature, 1992) EC 1.1.-.
Cyanogen bromide (CNBr). A compound used in molecular biology to digest some proteins and as a coupling reagent for phosphoroamidate or pyrophosphate internucleotide bonds in DNA duplexes.
A serine endopeptidase that is formed from TRYPSINOGEN in the pancreas. It is converted into its active form by ENTEROPEPTIDASE in the small intestine. It catalyzes hydrolysis of the carboxyl group of either arginine or lysine. EC 3.4.21.4.
Iron-containing proteins that transfer electrons, usually at a low potential, to flavoproteins; the iron is not present as in heme. (McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)
Proteins found in the PERIPLASM of organisms with cell walls.
A non-essential amino acid. It is found primarily in gelatin and silk fibroin and used therapeutically as a nutrient. It is also a fast inhibitory neurotransmitter.
The movement of materials (including biochemical substances and drugs) through a biological system at the cellular level. The transport can be across cell membranes and epithelial layers. It also can occur within intracellular compartments and extracellular compartments.
A non-essential amino acid present abundantly throughout the body and is involved in many metabolic processes. It is synthesized from GLUTAMIC ACID and AMMONIA. It is the principal carrier of NITROGEN in the body and is an important energy source for many cells.
One of the three domains of life (the others being Eukarya and ARCHAEA), also called Eubacteria. They are unicellular prokaryotic microorganisms which generally possess rigid cell walls, multiply by cell division, and exhibit three principal forms: round or coccal, rodlike or bacillary, and spiral or spirochetal. Bacteria can be classified by their response to OXYGEN: aerobic, anaerobic, or facultatively anaerobic; by the mode by which they obtain their energy: chemotrophy (via chemical reaction) or PHOTOTROPHY (via light reaction); for chemotrophs by their source of chemical energy: CHEMOLITHOTROPHY (from inorganic compounds) or chemoorganotrophy (from organic compounds); and by their source for CARBON; NITROGEN; etc.; HETEROTROPHY (from organic sources) or AUTOTROPHY (from CARBON DIOXIDE). They can also be classified by whether or not they stain (based on the structure of their CELL WALLS) with CRYSTAL VIOLET dye: gram-negative or gram-positive.
A category of nucleic acid sequences that function as units of heredity and which code for the basic instructions for the development, reproduction, and maintenance of organisms.
Any of the processes by which cytoplasmic or intercellular factors influence the differential control of gene action in bacteria.
A branched-chain essential amino acid that has stimulant activity. It promotes muscle growth and tissue repair. It is a precursor in the penicillin biosynthetic pathway.
The biosynthesis of PEPTIDES and PROTEINS on RIBOSOMES, directed by MESSENGER RNA, via TRANSFER RNA that is charged with standard proteinogenic AMINO ACIDS.
A change from planar to elliptic polarization when an initially plane-polarized light wave traverses an optically active medium. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
The property of objects that determines the direction of heat flow when they are placed in direct thermal contact. The temperature is the energy of microscopic motions (vibrational and translational) of the particles of atoms.
Endogenous amino acids released by neurons as excitatory neurotransmitters. Glutamic acid is the most common excitatory neurotransmitter in the brain. Aspartic acid has been regarded as an excitatory transmitter for many years, but the extent of its role as a transmitter is unclear.
A sulfur-containing essential L-amino acid that is important in many body functions.
An essential amino acid that is physiologically active in the L-form.
The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.
One of the non-essential amino acids commonly occurring in the L-form. It is found in animals and plants, especially in sugar cane and sugar beets. It may be a neurotransmitter.
A large collection of DNA fragments cloned (CLONING, MOLECULAR) from a given organism, tissue, organ, or cell type. It may contain complete genomic sequences (GENOMIC LIBRARY) or complementary DNA sequences, the latter being formed from messenger RNA and lacking intron sequences.
Deletion of sequences of nucleic acids from the genetic material of an individual.
In vitro method for producing large amounts of specific DNA or RNA fragments of defined length and sequence from small amounts of short oligonucleotide flanking sequences (primers). The essential steps include thermal denaturation of the double-stranded target molecules, annealing of the primers to their complementary sequences, and extension of the annealed primers by enzymatic synthesis with DNA polymerase. The reaction is efficient, specific, and extremely sensitive. Uses for the reaction include disease diagnosis, detection of difficult-to-isolate pathogens, mutation analysis, genetic testing, DNA sequencing, and analyzing evolutionary relationships.
An enzyme that catalyzes the oxidation of XANTHINE in the presence of NAD+ to form URIC ACID and NADH. It acts also on a variety of other purines and aldehydes.
An element with the atomic symbol N, atomic number 7, and atomic weight [14.00643; 14.00728]. Nitrogen exists as a diatomic gas and makes up about 78% of the earth's atmosphere by volume. It is a constituent of proteins and nucleic acids and found in all living cells.
Drug metabolizing enzymes which oxidize methyl ethers. Usually found in liver microsomes.
The location of the atoms, groups or ions relative to one another in a molecule, as well as the number, type and location of covalent bonds.
An enzyme that catalyzes the conversion of (S)-malate and NAD+ to oxaloacetate and NADH. EC 1.1.1.37.
A non-essential amino acid that is synthesized from GLUTAMIC ACID. It is an essential component of COLLAGEN and is important for proper functioning of joints and tendons.
A water-soluble, colorless crystal with an acid taste that is used as a chemical intermediate, in medicine, the manufacture of lacquers, and to make perfume esters. It is also used in foods as a sequestrant, buffer, and a neutralizing agent. (Hawley's Condensed Chemical Dictionary, 12th ed, p1099; McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed, p1851)
Spectroscopic method of measuring the magnetic moment of elementary particles such as atomic nuclei, protons or electrons. It is employed in clinical applications such as NMR Tomography (MAGNETIC RESONANCE IMAGING).
An essential aromatic amino acid that is a precursor of MELANIN; DOPAMINE; noradrenalin (NOREPINEPHRINE), and THYROXINE.
A mutation caused by the substitution of one nucleotide for another. This results in the DNA molecule having a change in a single base pair.
Process of generating a genetic MUTATION. It may occur spontaneously or be induced by MUTAGENS.
A sodium-dependent neutral amino acid transporter that accounts for most of the sodium-dependent neutral amino acid uptake by mammalian cells. The preferred substrates for this transporter system include ALANINE; SERINE; and GLUTAMINE.
Amino acids with uncharged R groups or side chains.
Reversibly catalyzes the oxidation of a hydroxyl group of sugar alcohols to form a keto sugar, aldehyde or lactone. Any acceptor except molecular oxygen is permitted. Includes EC 1.1.1.; EC 1.1.2. and EC 1.1.99.
Proteins obtained from the species SACCHAROMYCES CEREVISIAE. The function of specific proteins from this organism are the subject of intense scientific interest and have been used to derive basic understanding of the functioning similar proteins in higher eukaryotes.
A naturally occurring amino acid in both eukaryotic and prokaryotic organisms. It is found in tRNAs and in the catalytic site of some enzymes. The genes for glutathione peroxidase and formate dehydrogenase contain the TGA codon, which codes for this amino acid.
An essential amino acid that is necessary for normal growth in infants and for NITROGEN balance in adults. It is a precursor of INDOLE ALKALOIDS in plants. It is a precursor of SEROTONIN (hence its use as an antidepressant and sleep aid). It can be a precursor to NIACIN, albeit inefficiently, in mammals.
A tripeptide with many roles in cells. It conjugates to drugs to make them more soluble for excretion, is a cofactor for some enzymes, is involved in protein disulfide bond rearrangement and reduces peroxides.
The uptake of naked or purified DNA by CELLS, usually meaning the process as it occurs in eukaryotic cells. It is analogous to bacterial transformation (TRANSFORMATION, BACTERIAL) and both are routinely employed in GENE TRANSFER TECHNIQUES.
The biosynthesis of RNA carried out on a template of DNA. The biosynthesis of DNA from an RNA template is called REVERSE TRANSCRIPTION.
Compounds based on fumaric acid.
Mutagenesis where the mutation is caused by the introduction of foreign DNA sequences into a gene or extragenic sequence. This may occur spontaneously in vivo or be experimentally induced in vivo or in vitro. Proviral DNA insertions into or adjacent to a cellular proto-oncogene can interrupt GENETIC TRANSLATION of the coding sequences or interfere with recognition of regulatory elements and cause unregulated expression of the proto-oncogene resulting in tumor formation.
A genus of motile or nonmotile gram-positive bacteria of the family Clostridiaceae. Many species have been identified with some being pathogenic. They occur in water, soil, and in the intestinal tract of humans and lower animals.
A flavoprotein containing oxidoreductase that catalyzes the reduction of lipoamide by NADH to yield dihydrolipoamide and NAD+. The enzyme is a component of several MULTIENZYME COMPLEXES.
In bacteria, a group of metabolically related genes, with a common promoter, whose transcription into a single polycistronic MESSENGER RNA is under the control of an OPERATOR REGION.
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in enzyme synthesis.
Selenoproteins are proteins that specifically incorporate SELENOCYSTEINE into their amino acid chain. Most selenoproteins are enzymes with the selenocysteine residues being responsible for their catalytic functions.
The complete absence, or (loosely) the paucity, of gaseous or dissolved elemental oxygen in a given place or environment. (From Singleton & Sainsbury, Dictionary of Microbiology and Molecular Biology, 2d ed)
Detection of RNA that has been electrophoretically separated and immobilized by blotting on nitrocellulose or other type of paper or nylon membrane followed by hybridization with labeled NUCLEIC ACID PROBES.
Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure.
Proteins that have one or more tightly bound metal ions forming part of their structure. (Dorland, 28th ed)
A process that includes the determination of AMINO ACID SEQUENCE of a protein (or peptide, oligopeptide or peptide fragment) and the information analysis of the sequence.
Proteins found in any species of virus.
A system of cisternae in the CYTOPLASM of many cells. In places the endoplasmic reticulum is continuous with the plasma membrane (CELL MEMBRANE) or outer membrane of the nuclear envelope. If the outer surfaces of the endoplasmic reticulum membranes are coated with ribosomes, the endoplasmic reticulum is said to be rough-surfaced (ENDOPLASMIC RETICULUM, ROUGH); otherwise it is said to be smooth-surfaced (ENDOPLASMIC RETICULUM, SMOOTH). (King & Stansfield, A Dictionary of Genetics, 4th ed)
Proteins found in plants (flowers, herbs, shrubs, trees, etc.). The concept does not include proteins found in vegetables for which VEGETABLE PROTEINS is available.
A multisubunit enzyme complex that contains CYTOCHROME B GROUP; CYTOCHROME C1; and iron-sulfur centers. It catalyzes the oxidation of ubiquinol to UBIQUINONE, and transfers the electrons to CYTOCHROME C. In MITOCHONDRIA the redox reaction is coupled to the transport of PROTONS across the inner mitochondrial membrane.
An essential amino acid occurring naturally in the L-form, which is the active form. It is found in eggs, milk, gelatin, and other proteins.
Cell surface proteins that bind amino acids and trigger changes which influence the behavior of cells. Glutamate receptors are the most common receptors for fast excitatory synaptic transmission in the vertebrate central nervous system, and GAMMA-AMINOBUTYRIC ACID and glycine receptors are the most common receptors for fast inhibition.
The species Oryctolagus cuniculus, in the family Leporidae, order LAGOMORPHA. Rabbits are born in burrows, furless, and with eyes and ears closed. In contrast with HARES, rabbits have 22 chromosome pairs.
Sites on an antigen that interact with specific antibodies.
An element that is a member of the chalcogen family. It has an atomic symbol S, atomic number 16, and atomic weight [32.059; 32.076]. It is found in the amino acids cysteine and methionine.
Proteins obtained from foods. They are the main source of the ESSENTIAL AMINO ACIDS.
Hydrocarbon rings which contain two ketone moieties in any position. They can be substituted in any position except at the ketone groups.
Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.

NADH-glutamate synthase in alfalfa root nodules. Genetic regulation and cellular expression. (1/1399)

NADH-dependent glutamate synthase (NADH-GOGAT; EC 1.4.1.14) is a key enzyme in primary nitrogen assimilation in alfalfa (Medicago sativa L.) root nodules. Here we report that in alfalfa, a single gene, probably with multiple alleles, encodes for NADH-GOGAT. In situ hybridizations were performed to assess the location of NADH-GOGAT transcript in alfalfa root nodules. In wild-type cv Saranac nodules the NADH-GOGAT gene is predominantly expressed in infected cells. Nodules devoid of bacteroids (empty) induced by Sinorhizobium meliloti 7154 had no NADH-GOGAT transcript detectable by in situ hybridization, suggesting that the presence of the bacteroid may be important for NADH-GOGAT expression. The pattern of expression of NADH-GOGAT shifted during root nodule development. Until d 9 after planting, all infected cells appeared to express NADH-GOGAT. By d 19, a gradient of expression from high in the early symbiotic zone to low in the late symbiotic zone was observed. In 33-d-old nodules expression was seen in only a few cell layers in the early symbiotic zone. This pattern of expression was also observed for the nifH transcript but not for leghemoglobin. The promoter of NADH-GOGAT was evaluated in transgenic alfalfa plants carrying chimeric beta-glucuronidase promoter fusions. The results suggest that there are at least four regulatory elements. The region responsible for expression in the infected cell zone contains an 88-bp direct repeat.  (+info)

The mechanism of rhythmic ethylene production in sorghum. The role of phytochrome B and simulated shading. (2/1399)

Mutant sorghum (Sorghum bicolor [L.] Moench) deficient in functional phytochrome B exhibits reduced photoperiodic sensitivity and constitutively expresses a shade-avoidance phenotype. Under relatively bright, high red:far-red light, ethylene production by seedlings of wild-type and phytochrome B-mutant cultivars progresses through cycles in a circadian rhythm; however, the phytochrome B mutant produces ethylene peaks with approximately 10 times the amplitude of the wild type. Time-course northern blots show that the mutant's abundance of the 1-aminocyclopropane-1-carboxylic acid (ACC) oxidase mRNA SbACO2 is cyclic and is commensurate with ethylene production, and that ACC oxidase activity follows the same pattern. Both SbACO2 abundance and ACC oxidase activity in the wild-type plant are very low under this regimen. ACC levels in the two cultivars did not demonstrate fluctuations coincident with the ethylene produced. Simulated shading caused the wild-type plant to mimic the phenotype of the mutant and to produce high amplitude rhythms of ethylene evolution. The circadian feature of the ethylene cycle is conditionally present in the mutant and absent in the wild-type plant under simulated shading. SbACO2 abundance in both cultivars demonstrates a high-amplitude diurnal cycle under these conditions; however, ACC oxidase activity, although elevated, does not exhibit a clear rhythm correlated with ethylene production. ACC levels in both cultivars show fluctuations corresponding to the ethylene rhythm previously observed. It appears that at least two separate mechanisms may be involved in generating high-amplitude ethylene rhythms in sorghum, one in response to the loss of phytochrome B function and another in response to shading.  (+info)

Identification of D-proline reductase from Clostridium sticklandii as a selenoenzyme and indications for a catalytically active pyruvoyl group derived from a cysteine residue by cleavage of a proprotein. (3/1399)

Highly active D-proline reductase was obtained from Clostridium sticklandii by a modified purification scheme. The cytoplasmic enzyme had a molecular mass of about 870 kDa and was composed of three subunits with molecular masses of 23, 26, and 45 kDa. The 23-kDa subunit contained a carbonyl group at its N terminus, which could either be labeled with fluorescein thiosemicarbazide or removed by o-phenylenediamine; thus, N-terminal sequencing became feasible for this subunit. L-[14C]proline was covalently bound to the 23-kDa subunit if proline racemase and NaBH4 were added. Selenocysteine was detected in the 26-kDa subunit, which correlated with an observed selenium content of 10.6 g-atoms in D-proline reductase. No other non-proteinaceous cofactor was identified in the enzyme. A 4.8-kilobase pair (kb) EcoRI fragment was isolated and sequenced containing the two genes prdA and prdB. prdA coding for a 68-kDa protein was most likely translated as a proprotein that was posttranslationally cleaved at a threonine-cysteine site to give the 45-kDa subunit and most probably a pyruvoyl-containing 23-kDa subunit. The gene prdB encoded the 26-kDa subunit and contained an in frame UGA codon for selenocysteine insertion. prdA and prdB were transcribed together on a transcript of 4.5 kb; prdB was additionally transcribed as indicated by a 0.8-kb mRNA species.  (+info)

Substrate-specific selenoprotein B of glycine reductase from Eubacterium acidaminophilum. Biochemical and molecular analysis. (4/1399)

The substrate-specific selenoprotein B of glycine reductase (PBglycine) from Eubacterium acidaminophilum was purified and characterized. The enzyme consisted of three different subunits with molecular masses of about 22 (alpha), 25 (beta) and 47 kDa (gamma), probably in an alpha 2 beta 2 gamma 2 composition. PBglycine purified from cells grown in the presence of [75Se]selenite was labeled in the 47-kDa subunit. The 22-kDa and 47-kDa subunits both reacted with fluorescein thiosemicarbazide, indicating the presence of a carbonyl compound. This carbonyl residue prevented N-terminal sequencing of the 22-kDa (alpha) subunit, but it could be removed for Edman degradation by incubation with o-phenylenediamine. A DNA fragment was isolated and sequenced which encoded beta and alpha subunits of PBglycine (grdE), followed by a gene encoding selenoprotein A (grdA2) and the gamma subunit of PBglycine (grdB2). The cloned DNA fragment represented a second GrdB-encoding gene slightly different from a previously identified partial grdBl-containing fragment. Both grdB genes contained an in-frame UGA codon which confirmed the observed selenium content of the 47-kDa (gamma) subunit. Peptide sequence analyses suggest that grdE encodes a proprotein which is cleaved into the previously sequenced N-terminal 25-kDa (beta) subunit and a 22-kDa (alpha) subunit of PBglycine. Cleavage most probably occurred at an -Asn-Cys- site concomitantly with the generation of the blocking carbonyl moiety from cysteine at the alpha subunit.  (+info)

Oxygen depletion-induced dormancy in Mycobacterium bovis BCG. (5/1399)

Gradual depletion of oxygen causes the shift-down of aerobic growing Mycobacterium bovis BCG to an anaerobic synchronized state of nonreplicating persistence. The persistent culture shows induction of glycine dehydrogenase and alpha-crystallin-like protein and is sensitive to metronidazole.  (+info)

Structural characterization of l-aspartate oxidase and identification of an interdomain loop by limited proteolysis. (6/1399)

l-Aspartate oxidase is the first enzyme in the de novo biosynthesis of pyridinic coenzymes in facultative aerobic organisms. The enzyme is FAD dependent and it shares common features with both the oxidase and the fumarate reductase classes of flavoproteins. In this report we focused our attention on the supersecondary structure of the molecule by means of limited proteolysis studies. Moreover the polymerization state of the protein at different pH and the interactions with NAD and its analogues are described. The results suggest that l-aspartate oxidase is a monomer at pH values lower than 4.5 and a dimer at pH values higher than 6.5. The protein is organized in two major domains connected by a flexible loop located in the 120-140 region. The data obtained by limited proteolysis of the holo and the apo form in the presence and in the absence of substrates (fumarate and menadione), inhibitors (succinate) and NAD allows the proposition that both domains are involved in the binding of the flavin coenzyme. Moreover the data reported in this manuscript suggest that NAD inhibits l-aspartate oxidase activity by competing with the flavin for the binding to the enzyme.  (+info)

Control of expression of one-carbon metabolism genes of Saccharomyces cerevisiae is mediated by a tetrahydrofolate-responsive protein binding to a glycine regulatory region including a core 5'-CTTCTT-3' motif. (7/1399)

Expression of yeast genes involved in one-carbon metabolism is controlled by glycine, by L-methionine, and by nitrogen sources. Here we report a novel control element containing a core CTTCTT motif mediating the glycine response, demonstrating that a protein binds this element, that binding is modulated by tetrahydrofolate, and that folate is required for the in vivo glycine response. In an heterologous CYC1 promoter the region needed for the glycine response of GCV2 (encoding the P-subunit of glycine decarboxylase) mediated repression that was relieved by glycine. It was also responsible for L-methionine control but not nitrogen repression. GCV1 and GCV3 have an homologous region in their promoters. The GCV1 region conferred a glycine response on an heterologous promoter acting as a repressor or activator depending on promoter context. A protein was identified that bound to the glycine regulatory regions of GCV1 and GCV2 only if the CTTCTT motif was intact. This protein protected a 17-base pair CATCN7CTTCTT region of GCV2 that is conserved between GCV1 and GCV2. Protein binding was increased by tetrahydrofolate, and use of a fol1 deletion mutant indicated the involvement of a folate in the in vivo glycine response. Tetrahydrofolate or a derivative may act as a ligand for the transcription factor controlling expression of one-carbon metabolism genes.  (+info)

Purification of beef kidney D-aspartate oxidase overexpressed in Escherichia coli and characterization of its redox potentials and oxidative activity towards agonists and antagonists of excitatory amino acid receptors. (8/1399)

The flavoenzyme d-aspartate oxidase from beef kidney (DASPO, EC 1.4. 3.1) has been overexpressed in Escherichia coli. A purification procedure, faster than the one used for the enzyme from the natural source (bDASPO), has been set up yielding about 2 mg of pure recombinant protein (rDASPO) per each gram of wet E. coli paste. rDASPO has been shown to possess the same general biochemical properties of bDASPO, except that the former contains only FAD, while the latter is a mixture of two forms, one active containing FAD and one inactive containing 6-OH-FAD (9-20% depending on the preparation). This results in a slightly higher specific activity (about 15%) for rDASPO compared to bDASPO and in facilitated procedures for apoprotein preparation and reconstitution. Redox potentials of -97 mV and -157 mV were determined for free and l-(+)-tartrate complexed DASPO, respectively, in 0.1 M KPi, pH 7.0, 25 degrees C. The large positive shift in the redox potential of the coenzyme compared to free FAD (-207 mV) is in agreement with similar results obtained with other flavooxidases. rDASPO has been used to assess a possible oxidative activity of the enzyme towards a number of compounds used as agonists or antagonists of neurotransmitters, including d-aspartatic acid, d-glutamic acid, N-methyl-d-aspartic acid, d,l-cysteic acid, d-homocysteic acid, d, l-2-amino-3-phosphonopropanoic acid, d-alpha-aminoadipic acid, d-aspartic acid-beta-hydroxamate, glycyl-d-aspartic acid and cis-2, 3-piperidine dicarboxylic acid. Kinetic parameters for each substrate in 50 mM KPi, pH 7.4, 25 degrees C are reported.  (+info)

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The invention provides enzymatic methods for direct determination of percentage of glycated hemoglobin in blood samples without the need of a separated measurement of total hemoglobin content in blood samples. The methods utilizes one or two different types of oxidizing agents which selectively oxidize low-molecular weight reducing substances and high-molecular weight (mainly hemoglobin) reducing substances in blood samples, coupled with enzymatic reactions catalyzed by proteases, fructosyl amino acid oxidase, and peroxidase. The invention provides kits for performing the methods of the invention.
Reactivity: Chicken, Cow, Human and more. Compare different LOXL2 ELISA Kits & buy the right one directly at antibodies-online.com!
A new use for HMG-CoA reductase inhibitors is provided. In the instant invention, HMG-CoA reductase inhibitors are found to upregulate endothelial cell Nitric Oxide Synthase activity through a mechanism other than preventing the formation of oxidative-LDL. As a result, HMG-CoA reductase inhibitors are useful in treating or preventing conditions that result from the abnormally low expression and/or activity of endothelial cell Nitric Oxide Synthase. Such conditions include pulmonary hypertension, ischemic stroke, impotence, heart failure, hypoxia-induced conditions, insulin deficiency, progressive renal disease, gastric or esophageal motility syndrome, etc. Subjects thought to benefit mostly from such treatments include nonhyperlipidemics and nonhypercholesterolemics, but not necessarily exclude hyperlipidemics and hypercholesterolemics.
A use for rho GTPase function inhibitors is provided. In the instant invention, rho GTPase function inhibitors are found to upregulate endothelial cell Nitric Oxide Synthase activity. As a result, rho GTPase function inhibitors are useful in treating or preventing conditions that result from the abnormally low expression and/or activity of endothelial cell Nitric Oxide Synthase. Such conditions include pulmonary hypertension, ischemic stroke, impotence, heart failure, hypoxia-induced conditions, insulin deficiency, progressive renal disease, gastric or esophageal motility syndrome, etc. Subjects thought to benefit mostly from such treatments include nonhyperlipidemics and nonhypercholesterolemics, but do not necessarily exclude hyperlipidemics and hypercholesterolemics.
TY - JOUR. T1 - Identification and Purification of an L-Alanine Dehydrogenase Homolog that Catalyzes the Formation of L-Ornithine Lactam from Streptomyces incarnatus Sinefungin-Producing NRRL8089. AU - Inagaki, Kenji. PY - 2010. Y1 - 2010. M3 - Article. VL - 24. SP - 63. EP - 65. JO - Actinomycetologica. JF - Actinomycetologica. IS - 2. ER - ...
Rabbit polyclonal D Amino Acid Oxidase antibody. Tested in Mouse, Rat, Human. Independently reviewed in 1 review(s). Immunogen corresponding to recombinant full length protein.
References for Abcams Anti-D Amino Acid Oxidase antibody (ab123524). Please let us know if you have used this product in your publication
Gentaur molecular products has all kinds of products like :search , BioBasic \ L_Amino acid oxidase >4 U_mg \ ALS002764 for more molecular products just contact us
To evaluate the association profiles of the lysyl oxidase-like 1 gene polymorphisms with pseudoexfoliation syndrome in the Korean population, peripheral blood sampling will be done from the patients with pseudoexfoliation.. And genotypes of the three single nucleotide polymorphisms of lysyl oxidase-like 1 gene , rs1048661, rs3825942, rs2165241 were analyzed by direct sequencing. ...
The active site and substrate-binding mode of MD-ACO1 (Malus domestica Borkh. 1-aminocyclopropane-1-carboxylate oxidase) have been determined using site-directed mutagenesis and comparative modelling methods. The MD-ACO1 protein folds into a compact jelly-roll motif comprised of eight α-helices, 12 β-strands and several long loops. The active site is well defined as a wide cleft near the C-terminus. The co-substrate ascorbate is located in cofactor Fe2+-binding pocket, the so-called 2-His-1-carboxylate facial triad. In addition, our results reveal that Arg244 and Ser246 are involved in generating the reaction product during enzyme catalysis. The structure agrees well with the biochemical and site-directed mutagenesis results. The three-dimensional structure together with the steady-state kinetics of both the wild-type and mutant MD-ACO1 proteins reveal how the substrate specificity of MD-ACO1 is involved in the catalytic mechanism, providing insights into understanding the fruit ripening ...
LIU Y ; WHIGHAM BT ; WHEELER J ; WILLIAMS SEI ; Rautenbach RM ; Ziskind A ; Ramsay M ; CARMICHAEL TR ; Ashley-Koch AE ; Rand Allingham R ; Hauser M (2012) ...
The residues L40, A113, V291, and V294, in leucine dehydrogenase (LeuDH), predicted to be involved in recognition of the substrate side chain, have been mutated on the basis of the molecular modeling to mimic the substrate specificities of phenylalanine (PheDH), glutamate (GluDH), and lysine dehydrogenases (LysDH). The A113G and A113G/V291L mutants, imitating the PheDH active site, displayed activities toward -phenylalanine and phenylpyruvate with 1.6 and 7.8% of kcat values of the wild-type enzyme for the preferred substrates, -leucine and its keto-analog, respectively. Indeed, the residue A113, corresponding to G114 in PheDH, affects the volume of the side-chain binding pocket and has a critical role in discrimination of the bulkiness of the side chain. Another two sets of mutants, substituting L40 and V294 of LeuDH with the corresponding residues predicted in GluDH and LysDH, were also constructed and characterized. Emergence of GluDH and LysDH activities in L40K/V294S and L40D/V294S mutants,
A dual-cell device has been designed as an oxidase-like mimic with the oxidation of 3,3′,5,5′-tetramethylbenzidine as a model reaction. This dual-cell device could be also used to study oxidase-like nanozymes. It was found that only the catalytic sites for oxygen reduction are essential and necessary for oxidase-li
Video created by University of Manchester for the course Industrial Biotechnology. This module looks at the production of pharmaceuticals and fine chemicals using biocatalysis. Specifically, we will look at isolated biocatalytic ...
L-aspartate oxidase is the B protein, NadB, of the quinolinate synthetase complex. Quinolinate synthetase makes a precursor of the pyridine nucleotide portion of NAD. This model identifies proteins that cluster as L-aspartate oxidase (a flavoprotein difficult to separate from the set of closely related flavoprotein subunits of succinate dehydrogenase and fumarate reductase) by both UPGMA and neighbor-joining trees. The most distant protein accepted as an L-aspartate oxidase (NadB), that from Pyrococcus horikoshii, not only clusters with other NadB but is just one gene away from NadA ...
Abstract A simple and rapid technique for the determination of the d -amino acids which are oxidized by d -amino acid oxidase has… Expand ...
next prev parent reply index Thread overview: 91+ messages / expand[flat,nested] mbox.gz Atom feed top 2020-05-22 3:50 [PATCH 00/24] xfs: rework inode flushing to make inode reclaim fully asynchronous Dave Chinner 2020-05-22 3:50 ` [PATCH 01/24] xfs: remove logged flag from inode log item Dave Chinner 2020-05-22 7:25 ` Christoph Hellwig 2020-05-22 21:13 ` Darrick J. Wong 2020-05-22 3:50 ` [PATCH 02/24] xfs: add an inode item lock Dave Chinner 2020-05-22 6:45 ` Amir Goldstein 2020-05-22 21:24 ` Darrick J. Wong 2020-05-23 8:45 ` Christoph Hellwig 2020-05-22 3:50 ` [PATCH 03/24] xfs: mark inode buffers in cache Dave Chinner 2020-05-22 7:45 ` Amir Goldstein 2020-05-22 21:35 ` Darrick J. Wong 2020-05-24 23:41 ` Dave Chinner 2020-05-23 8:48 ` Christoph Hellwig 2020-05-25 0:06 ` Dave Chinner [this message] 2020-05-22 3:50 ` [PATCH 04/24] xfs: mark dquot Dave Chinner 2020-05-22 7:46 ` Amir Goldstein 2020-05-22 21:38 ` Darrick J. Wong 2020-05-22 3:50 ` [PATCH 05/24] xfs: mark log recovery buffers for ...
TY - JOUR. T1 - Mycobacterium smegmatis L-alanine dehydrogenase (Ald) is required for proficient utilization of alanine as a sole nitrogen source and sustained anaerobic growth. AU - Feng, Zhengyu. AU - Cáceres, Nancy E.. AU - Sarath, Gautam. AU - Barletta, Raúl G.. PY - 2002/9. Y1 - 2002/9. N2 - NAD(H)-dependent L-alanine dehydrogenase (EC 1.4.1.1) (Aid) catalyzes the oxidative deamination of L-alanine and the reductive amination of pyruvate. To assess the physiological role of Aid in Mycobacterium smegmatis, we cloned the ald gene, identified its promoter, determined the protein expression levels, and analyzed the combined effects of nutrient supplementation, oxygen availability, and growth stage on enzyme activity. High Ald activities were observed in cells grown in the presence of L- or D-alanine regardless of the oxygen availability and growth stage. In exponentially growing cells under aerobic conditions, supplementation with alanine resulted in a 25- to 50-fold increase in the enzyme ...
Purification and properties of D-aspartate oxidase from Cryptococcus humicolus UJ1.: D-Aspartate oxidase (EC 1.4.3.1), which is highly specific to D-aspartate,
Glycine Oxidase H244K, Bacillus subtilis recombinant protein, Glycine oxidase, glycine oxygen oxidoreductase (deaminating), GO validated in (PBV11404r-250), Abgent
In enzymology, a leucine dehydrogenase (EC 1.4.1.9) is an enzyme that catalyzes the chemical reaction: L-leucine + H2O + NAD+ ↔ 4-methyl-2-oxopentanoate + NH3 + NADH +
Ray, S. S., Sengupta, R., Tiso, M., Haque, M. M., Sahoo, R., Konas, D. W., Aulak, K., Regulski, M. R., Tully, T., Stuehr, D. J., Ghosh, S. (2007) Reductase Domain of Drosophila melanogaster Nitric-Oxide Synthase: Redox Transformations, Regulation, and Similarity to Mammalian Homologues. Biochemistry, 46 (42). pp. 11865-11873. ISSN 0006-2960 (Print) Ray, S. S., Tejero, J., Wang, Z. Q., Dutta, T., Bhattacharjee, A., Regulski, M. R., Tully, T., Ghosh, S., Stuehr, D. J. (2007) Oxygenase Domain of Drosophila melanogaster Nitric Oxide Synthase: Unique Kinetic Parameters Enable a More Efficient NO Release. Biochemistry, 46 (42). pp. 11857-11864. ISSN 0006-2960 (Print) Regulski, M., Stasiv, Y., Tully, T., Enikolopov, G. (2004) Essential function of nitric oxide synthase in Drosophila. Current Biology, 14 (20). R881-R882. ISSN 0960-9822 Regulski, M., Tully, T. (1995) Molecular and biochemical characterization of dNOS: a Drosophila Ca2+/calmodulin-dependent nitric oxide synthase. Proc Natl Acad Sci U S A, ...
3VPX: A psychrophilic leucine dehydrogenase from Sporosarcina psychrophila: Purification, characterization, gene sequencing and crystal structure analysis
1OMO: Structure of alanine dehydrogenase from Archaeoglobus: active site analysis and relation to bacterial cyclodeaminases and mammalian mu crystallin.
Re: [PATCH v3] xfstests: xfs mount option sanity test 2020-01-18 17:23 ` Darrick J. Wong @ 2020-01-19 7:23 ` Zorro Lang 2020-01-27 16:57 ` Darrick J. Wong 0 siblings, 1 reply; 5+ messages in thread From: Zorro Lang @ 2020-01-19 7:23 UTC (permalink / raw) To: Darrick J. Wong; +Cc: fstests, linux-xfs On Sat, Jan 18, 2020 at 09:23:30AM -0800, Darrick J. Wong wrote: , On Wed, Jan 15, 2020 at 04:11:32PM +0800, Zorro Lang wrote: , , XFS is changing to suit the new mount API, so add this case to make , , sure the changing wont bring in regression issue on xfs mount option , , parse phase, and wont change some default behaviors either. , , , , Signed-off-by: Zorro Lang ,[email protected], , , --- , , , , Hi, , , , , Thanks the suggestions from Darrick, v3 did below changes: , , 1) Add more debug info output in do_mkfs and do_test. , , 2) A new function filter_loop. , , 3) Update .out file content , , , , Ive simply run this case on RHEL-7, RHEL-8 and upstream 5.5-rc4 kernel, , , all passed. , , ...
Purified Recombinant Human LOXL2 Protein, His-tagged from Creative Biomart. Recombinant Human LOXL2 Protein, His-tagged can be used for research.
Eubacterium acidaminophilum GrdD protein: Cys359 of GrdD is the active-site thiol that catalyses the final step of acetyl phosphate formation by glycine reductase from Eubacterium acidaminophilum; GenBank L04500
Prevalence and Associations of Pseudoexfoliation Glaucoma in a Group of Tertiary Eye Care Facilities in Southwest Nigeria. . Biblioteca virtual para leer y descargar libros, documentos, trabajos y tesis universitarias en PDF. Material universiario, documentación y tareas realizadas por universitarios en nuestra biblioteca. Para descargar gratis y para leer online.
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[Purification and isolation of isoenzymes of L-amino acid oxidase from the venom of Bothrops asper].: L-amino acid oxidase (E.C. 1.4.3.2) was purified from the
An NAD-dependent enzyme that catalyzes the reversible Deamination of L-Alanine to PYRUVATE and Ammonia. The enzyme is needed for Growth when Alanine is the sole Carbon or Nitrogen source. It may also play a Role in Cell Wall synthesis because L-Alanine is an important constituent of the PEPTIDOGLYCAN layer ...
Publications Somrutai Winichayakul, Anton Pernthaner, Sam Livingston, Ruth Cookson, Richard Scott, Nick Roberts (2012) Production of active single-chain antibodies in seeds using trimeric polyoleosin fusion. Journal of Biotechnology 161: 407‑413. Scott RW, Yoo SD, Hunter DA, Gong D, Chen B, Leung S and McManus MT (2010) Regulation of 1-aminocyclopropane-1-carboxylate oxidase gene expression during leaf ontogeny in white clover. Plant Growth Regulation 62: 31‑41. Scott RW, Winichayakul S, Roldan M, Cookson R, Willingham M, Castle M, Pueschel R, Peng C-C, Tzen JTC and Roberts NJ (2010) Elevation of oil body integrity and emulsion stability by polyoleosins, multiple oleosin units joined in tandem head to tail fusions. Plant Biotechnology Journal 8: 912‑927. ...
To make this vision a reality, we attempted to transfer the plant ethylene biosynthesis pathway into E. coli. Plants produce ethylene through the Yang Cycle, which uses methionine as a base molecule to produce several different products. We studied the enzymes involved and designed a genetic circuit composed of SAM synthase, ACC synthase and ACC oxidase. E coli already possesses a gene for SAM synthase, so we added a second copy to our construct to ramp up production. ACC synthase and ACC oxidase are only found in plants, so we explored enzyme characterisation databases to find the most efficient and specific catalysts from the plant world. Our analysis pointed to apple for ACC synthase and tomato for ACC oxidase. With this in silico work done, our plan was to have all three genes synthesised by Mr. Gene after codon optimising them for E. coli. We would then add ribosome binding sites and link these three genes together in one construct for efficient ethylene production from E. coli. Naturally, ...
To make this vision a reality, we attempted to transfer the plant ethylene biosynthesis pathway into E. coli. Plants produce ethylene through the Yang Cycle, which uses methionine as a base molecule to produce several different products. We studied the enzymes involved and designed a genetic circuit composed of SAM synthase, ACC synthase and ACC oxidase. E coli already possesses a gene for SAM synthase, so we added a second copy to our construct to ramp up production. ACC synthase and ACC oxidase are only found in plants, so we explored enzyme characterisation databases to find the most efficient and specific catalysts from the plant world. Our analysis pointed to apple for ACC synthase and tomato for ACC oxidase. With this in silico work done, our plan was to have all three genes synthesised by Mr. Gene after codon optimising them for E. coli. We would then add ribosome binding sites and link these three genes together in one construct for efficient ethylene production from E. coli. Naturally, ...
Mixed transition-metal oxides (MTMOs) have attracted much research interest because of their promising applications in artificial enzymes. In this work, uniform hollow MnCo2O4 nanofibers have been fabricated via an electrospinning technique followed by a calcination process, which can be used as efficient oxidase m
retitle 336993 initramfs done by yaird with XFS severity 336993 serious thanks I use XFS on a production system and surely I am not alone in that case, so IMHO, it is a dead serious bug. It seems the initramfs implementation is sensitive to cruft at the end of the cpio.gz file. Also, it seems like yaboot might be loading extra data and appending them to the end of the image causing the kernel to fail to unpack the image. Most probably, the issue is located in the xfs_read code of yaboot. We will investigate that... Cheers, -- ((__,--,__)) Aurélien GÉRÔME .---. `--)~ ~(--` Free Software Developer / \ .-( )`-. Unix Sys & Net Admin \[email protected]@./ `~~`@) (@`~~` /`\_/`\ , , .`. // _ \\ , , : : : , \ ),_ (8___8) `. `` /`\_`, ,_/ \ `---` `- \__/---\__/ BOFH excuse #320: Youve been infected by the Telescoping Hubble virus ...
XFS filesystem is fragmented into subgroups. These groups are something like smaller partitions in a bigger one. This allows kernel to use paralellism - it can write to several parts of filesystem at the same time. Offcourse, disk head will still write data in one place after another, because disks have only one head - so this technology gives benefits before data is sent to a disk. If you have too much a. groups, your FS will be divided in many sections, and then its very likely files will get fragmented in between two or even three section. Next bad thing is that when you fill up your FS, itll start to use too much CPU. Those things slows things down dramaticly... It has been tought that at least 1 a. group is needed per 4GB, but some XFS developers denied that information, and marked it as obsolete on LKML recently. So, what to choose here? Depends on how much parallelism do you really need. This thing has its benefits in server usage, but for desktop, 2 allocation groups per one CPU seems ...
Chemical exfoliation is an indispensible step in your skincare routine, credited for absolving issues that range from acne to pore troubles. Heres a guide.
In the conceptualization and planning stages of this feature we were certain it was going to be among the best coverage we have offered in regards to exfoliation. Indeed I think the information in this feature as well as the supporting articles is very informative and well written. What I know now that I didnt know before we began the process of talking to potential writers, is how difficult it would be to find four people who were willing to contribute to this feature, primarily because of the title. I can only imagine what they would have said if they had seen the cover and opening art for this feature. Their reaction might have been similar to your own and even ours when we first looked at these images - a bit shocked and taken aback. But lets stay focused, and I will get back to the art in a minute. ...
Cell signaling transduction refers to the process in which information carried by extracellular messenger molecules is translated into changes that occur inside a cell.
Cell signaling transduction refers to the process in which information carried by extracellular messenger molecules is translated into changes that occur inside a cell.
Glycine decarboxylase is a mitochondrial enzyme complex, which is the site of photorespiratory CO2 and NH3 release. Although the proteins that constitute the complex are located within the mitochondria, because of their intimate association with photosynthesis their expression is controlled by light. Comparisons of the kinetics of mRNA accumulation between the small subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase and the H-protein of glycine decarboxylase during the greening of etiolated Arabidopsis thaliana suggest that their expression is controlled in parallel. A genomic clone for the H-protein (gdcH) was isolated from Arabidopsis and sequenced. The upstream region from -856 to +62 was fused to the β-glucuronidase (GUS) reporter gene, and this construct was transformed into tobacco. This 5′ upstream regulatory region appears to control GUS expression in a manner very similar to that of the endogenous H-protein gene. Constructs with deletions in the 5′ upstream region were ...
Purpose: To evaluate plasma total homocysteine (tHcy) and nitric oxide (NO) marker levels in patients with pseudoexfoliation syndrome (PXS), pseudoexfoliation glaucoma (PXG), primary open-angle glaucoma (POAG), and normal controls. Methods: This cross-sectional, prospective study involved 19 patients with POAG, 18 with PXS, 22 with PXG, and 20 control subjects. Fasting tHcy levels of all study participants were determined using a fluorescence polarization immunoassay method. Quantitation of total nitrate was based on the Griess reaction, in which a chromophore with a strong absorbance at 545 nm is formed by reaction of nitrite with a mixture of naphthylethylenediamine and sulphanilamide. Results: The mean plasma homocysteine level was statistically significantly elevated in the PXS (p=0.033) and the PXG (p=0.023) groups but not in the POAG group (p=0.996) when compared with the control group. Multiple logistic regression analyses comparing the various patient groups with the single control group ...
Introduction. Bothrops pirajai snake is an endemic species from the South region of Bahia state, Brazil, and it belongs nowadays to a national list of Brazilian fauna species threatened of extinction (Martins & Molina, 2008). Its venom is rich in proteins such as phospholipases A2, desintegrins, metalloproteases, serinoproteases, L-amino acid oxidases and others (Rodrigues et al., 2009). L-amino acid oxidases (LAAO, EC 1.4.3.2) are enantioselective flavoenzymes catalyzing the oxidative deamination of a wide range of L-amino acids (Stábeli et al., 2007). During the reductive half-reaction, the amino acid substrate is oxidized to the imino acid with concomitant reduction of the flavin adenine dinucleotide (FAD) cofactor. The imino acid product of oxidation undergoes a non-enzymatic hydrolysis to give the respective α-keto acid and ammonia. An oxidative half-reaction completes the catalytic cycle re-oxidizing the FAD with molecular oxygen and producing hydrogen peroxide (Moustafa et al., ...
Purpose.: We examined the association between caffeine and caffeinated beverage consumption in relation to the risk of exfoliation glaucoma or exfoliation glaucoma suspect (EG/EGS). Methods.: We followed 78,977 women from the Nurses Health Study (NHS) and 41,202 men from the Health Professionals Follow-up Study (HPFS) who were at least 40 years of age, did not have glaucoma, and reported undergoing eye examinations from 1980 (NHS) or 1986 (HPFS) to 2008. Information on consumption of caffeine-containing beverages and potential confounders were repeatedly ascertained in validated follow-up questionnaires. Confirmation with medical record review revealed 360 incident EG/EGS cases. Multivariate rate ratios (RRs) for EG/EGS were calculated in each cohort and then pooled using meta-analytic techniques. Results.: Compared with participants whose cumulatively updated total caffeine consumption was ,125 mg/day, participants who consumed ≥500 mg/day had a trend toward increased risk of EG/EGS that was ...
1.Nitric oxide is a potent vasodilator which plays a major role in the control of blood pressure. The hyperdynamic circulation of cirrhosis has been linked to nitric oxide.. 2.We measured neutrophil nitric oxide synthase activity in relation to the level of hepatic dysfunction in patients with liver disease of varying aetiology and severity.. 3.Neutrophils were isolated from 21 patients (7 Child-Pugh score A, 6 grade B and 8 grade C) aged 28-76 (median 49) years. Nitric oxide synthase activity was measured using the conversion of oxyhaemoglobin to methaemoglobin by nitric oxide and expressed in terms of cell protein. Blood pressure and biochemical indices were recorded. Data were assessed using Kruskal-Wallis one-way analysis of variance, Mann-Whitney U-test or Pearson correlation as appropriate.. 4.Systolic, mean arterial and diastolic blood pressures decreased with increasing hepatic damage (P = 0.031, P = 0.01 and P = 0.038 respectively). Nitric oxide synthase activity increased with the ...
HONG, TAN NGET (2009) Snake venom L-amino acid oxidase. In: CRC Handbook of Venoms and Toxins of Reptiles. Taylor and Francis / CRC Press, pp. 219-234. ...
91368PRTRhodococcus qingshengii 1Met Ser Ile Asp Asp Glu Leu Arg Trp Asp Gly Glu Leu Thr Val Thr1 5 10 15Arg His Asp Arg Glu Thr Gly Thr Thr Phe Val Ile Arg Ile Asp Ser 20 25 30Thr Arg Leu Gly Pro Ala Ser Gly Gly Thr Arg Ala Ala His Tyr Pro 35 40 45Ser Ile Gly His Ala Leu Ala Asp Ala Gly Lys Leu Ala Gly Ala Met 50 55 60Thr Leu Lys Met Ala Val Ser Asp Leu Pro Met Gly Gly Gly Lys Ser65 70 75 80Val Ile Ala Leu Pro Ala Pro Arg Asn Gln Ile Asp Ala Ala Thr Trp 85 90 95Ser Arg Ile Leu Gly Ile His Ala Glu Asn Ile Asp Lys Leu Glu Gly 100 105 110Asn Tyr Trp Thr Gly Pro Asp Val Asn Thr Asn Ser Ser Asp Met Asp 115 120 125Gln Leu Ser Arg Thr Thr Arg Tyr Val Phe Gly Arg Ser Val Asp Lys 130 135 140Gly Gly Ala Gly Ser Ser Ala His Ala Thr Ala Leu Gly Val Phe Glu145 150 155 160Ala Met Lys Ala Thr Ala Arg Arg Arg Gly Leu Gly Thr Leu Asp Gly 165 170 175Arg Thr Val Leu Val Gln Gly Leu Gly Ala Val Gly Gly Asp Val Val 180 185 190Arg Leu Ala Ala Gln Ala Gly Ala Arg Leu Leu Val Ala Asp Thr Asp 195 200 205Pro Gln Arg Leu ...
Abstract Background The identification of new serum biomarkers with high sensitivity and specificity is an important priority in pancreatic cancer research. Through an extensive proteomics analysis of pancreatic cancer cell lines and pancreatic juice, we previously generated a list of candidate pancreatic cancer biomarkers. The present study details further validation of four of our previously identified candidates: regenerating islet-derived 1 beta (REG1B), syncollin (SYCN), anterior gradient homolog 2 protein (AGR2), and lysyl oxidase-like 2 (LOXL2). Methods The candidate biomarkers were validated using enzyme-linked immunosorbent assays in two sample sets of serum/plasma comprising a total of 432 samples (Sample Set A: pancreatic ductal adenocarcinoma (PDAC, n = 100), healthy (n = 92); Sample Set B: PDAC (n = 82), benign (n = 41), disease-free (n = 47), other cancers (n = 70)). Biomarker performance in distinguishing PDAC from each control group was assessed individually in the two sample sets.
Description: Quantitativesandwich ELISA kit for measuring Human Lysyl oxidase homolog 3(LOXL3) in samples from serum, plasma, tissue homogenates. Now available in a cost efficient pack of 5 plates of 96 wells each, conveniently packed along with the other reagents in 5 separate kits ...
Affiliation:助手, Research Field:応用微生物学・応用生物化学, Keywords:Arthrobacter sp.,Phenylalanine dehydrogenase,Peptide,Opine dehydrogenase,Enzymatic synthesis,Bacillus sphaericus,D-Aminopeptidase,Organic solvent, # of Research Projects:2, # of Research Products:0
Is Skin Exfoliation a common side effect of Tildiem? View Skin Exfoliation Tildiem side effect risks. Female, 60 years of age, was diagnosed with lung abscess and took Tildiem 60 Mg Qd Po. Patient was hospitalized.
The transcriptional activator IFN regulatory factor 1 (IRF-1) and its antagonistic repressor IRF-2 are regulators of the IFN system. IRF-1 also manifests tumor suppressive activity, and its inactivation could contribute to the development of human hematopoietic malignancies. Here, we report the identification of the lysyl oxidase gene as a target gene of IRF-1. An IRF response element was identified in the lysyl oxidase gene promoter. We also demonstrate that the transformed phenotype of ras-expressing embryonic fibroblasts with a null mutation in the IRF-1 allele could be suppressed by the expression of the lysyl oxidase cDNA, implicating its potential role in tumor suppression. Thus, the regulation of the lysyl oxidase gene by IRF-1 could contribute to the multistep process of malignant transformation.. ...
Exfoliation delivers a tighter, firmer, smoother look and feel of skin. Because of this result, many fall into the trap of over-exfoliation: an over-zealous approach that can actually reduce skins vitality and make it more susceptible to damage from UV light.Over-exfoliation triggers the inflammatory response, leading
All Natural Facial Peels to achieve the best results of skin exfoliation and help with the skins natural anti-aging process - Jadiences Spa Collection
DAX) provides, as a Technology Preview on the ext4 and XFS file systems, a means for an application to directly map persistent memory into its address space. To use DAX, a system must have some form of persistent memory available, usually in the form of one or more Non-Volatile Dual In-line Memory Modules (NVDIMMs), and a file system that supports DAX must be created on the NVDIMM(s). Also, the file system must be mounted with the ...
Callstack: at Proteins/NESGC/1xfs at Template:Protein at template MindTouch.Deki.Script.Runtime.DekiScriptUndefinedNameException: reference to undefined name note Exception of type MindTouch.Deki.Script.Runtime.DekiScriptUndefinedNameException was thrown. at MindTouch.Deki.Script.Compiler.DekiScriptExpressionEvaluation.Visit (MindTouch.Deki.Script.Expr.DekiScriptVar expr, DekiScriptExpressionEvaluationState state) [0x00000] in ,filename unknown,:0 at MindTouch.Deki.Script.Expr.DekiScriptVar.VisitWith[DekiScriptExpressionEvaluationState,Range] (IDekiScriptExpressionVisitor`2 visitor, DekiScriptExpressionEvaluationState state) [0x00000] in ,filename unknown,:0 at MindTouch.Deki.Script.Compiler.DekiScriptExpressionEvaluation.Evaluate (MindTouch.Deki.Script.Expr.DekiScriptAccess expr, DekiScriptExpressionEvaluationState state, Boolean evaluateProperties) [0x00000] in ,filename unknown,:0 at MindTouch.Deki.Script.Compiler.DekiScriptExpressionEvaluation.Visit ...
... amino acid oxidoreductases MeSH D08.811.682.664.500.062 - alanine dehydrogenase MeSH D08.811.682.664.500.125 - d-amino-acid ... l-amino acid oxidase MeSH D08.811.682.664.500.724 - leucine dehydrogenase MeSH D08.811.682.664.500.772 - nitric oxide synthase ... amino acid isomerases MeSH D08.811.399.894.200.200 - alanine racemase MeSH D08.811.399.894.500 - carbohydrate epimerases MeSH ... aromatic-L-amino-acid decarboxylase MeSH D08.811.520.224.125.100.500 - dopa decarboxylase MeSH D08.811.520.224.125.250 - ...
"Collapse of the native structure caused by a single amino acid exchange in human NAD(P)H:quinone oxidoreductase". FEBS J. 281 ( ... is leading to an amino acid exchange on position 139 from arginine to tryptophane. Furthermore, an alternative RNA splicing ... Yang FY, Guan QK, Cui YH, Zhao ZQ, Rao W, Xi Z (Sep 2012). "NAD(P)H quinone oxidoreductase 1 (NQO1) genetic C609T polymorphism ... Ross D, Kepa JK, Winski SL, Beall HD, Anwar A, Siegel D (Dec 2000). "NAD(P)H:quinone oxidoreductase 1 (NQO1): chemoprotection, ...
... are oxidoreductases, a type of enzyme, that act upon amino acids. They constitute the majority of ... Examples include: Glutamate dehydrogenase Nitric oxide synthase Amino+Acid+Oxidoreductases at the US National Library of ...
The systematic name of this enzyme class is L-amino-acid:oxygen oxidoreductase (deaminating). This enzyme is also called ophio- ... In enzymology, an L-amino acid oxidase (LAAO) (EC 1.4.3.2) is an enzyme that catalyzes the chemical reaction an L-amino acid + ... Snake venom Oxidoreductase Oxidative deamination D-amino acid oxidase Biology portal. ... The mechanism proceeds via oxidative deamination of the L-amino acid, which affords an imino acid intermediate. Following ...
The systematic name of this enzyme class is L-amino-acid:NAD+ oxidoreductase (deaminating). Nisman B, Mager J (February 1952 ... In enzymology, a L-amino-acid dehydrogenase (EC 1.4.1.5) is an enzyme that catalyzes the chemical reaction an L-amino acid + ... H+ The 3 substrates of this enzyme are L-amino acid, H2O, and NAD+, whereas its 4 products are 2-oxo acid, NH3, NADH, and H+. ... "Diphosphopyridine nucleotide and phosphate requirement for oxidation of amino-acids by cell-free extracts of obligate anaerobes ...
... (EC 1.4.5.1, DadA) is an enzyme with systematic name D-amino acid:quinone oxidoreductase ( ... Amino Acids. 38 (1): 247-55. doi:10.1007/s00726-009-0240-0. PMID 19212808. D-amino+acid+dehydrogenase+(quinone) at the US ... Tanigawa M, Shinohara T, Saito M, Nishimura K, Hasegawa Y, Wakabayashi S, Ishizuka M, Nagata Y (January 2010). "D-Amino acid ... Olsiewski PJ, Kaczorowski GJ, Walsh C (May 1980). "Purification and properties of D-amino acid dehydrogenase, an inducible ...
... they utilize aldehyde ferredoxin oxidoreductase to metabolize the amino acid carbon source. AOR is homodimeric. Each 67kDa ... Its primary role is to oxidize aldehyde coming derived from the metabolism of amino acids and glucoses. Aldehyde Ferredoxin ... However, other proposals include its role in oxidation of amino acid metabolism aldehyde side products coming from de-aminated ... Iron atom in the cluster is additionally bound by three other Cystein ligands: . Also, another linker amino acid residue ...
The systematic name of this enzyme class is N-methyl-L-amino-acid:oxygen oxidoreductase (demethylating). Other names in common ... an L-amino acid + formaldehyde + H2O2 The 3 substrates of this enzyme are N-methyl-L-amino acid, H2O, and O2, whereas its 3 ... a N-methyl-L-amino-acid oxidase (EC 1.5.3.2) is an enzyme that catalyzes the chemical reaction an N-methyl-L-amino acid + H2O ... V. Specificity and its relation to amino acid oxidase". Hukuoka Acta Med. 43: 731-735. Moritani M, Tung TC, Fujii S, Mito H, ...
Tsugeno Y, Ito A (1997). "A key amino acid responsible for substrate selectivity of monoamine oxidase A and B". J. Biol. Chem. ... L-amino acid oxidases (LAO) and various flavin containing monoamine oxidases (MAO). The aligned region includes the flavin ... Flavin-containing amine oxidoreductases are a family of various amine oxidases, including maize polyamine oxidase (PAO), ...
... replaces the amino acid alanine with the amino acid valine at protein position 72 in the NADH-ubiquinone oxidoreductase chain 6 ... The encoded protein is 18 kDa and composed of 172 amino acids. MT-ND6 is one of seven mitochondrial genes encoding subunits of ... This mutation changes a single amino acid in the NADH dehydrogenase 6 protein at position 64, from methionine to valine. The ... MT-ND6 is a gene of the mitochondrial genome coding for the NADH-ubiquinone oxidoreductase chain 6 protein (ND6). The ND6 ...
DAO D-amino-acid dehydrogenase D-amino acid oxidase D-aspartate oxidase Glycerol-3-phosphate dehydrogenase Sarcosine oxidase ... D-amino-acid dehydrogenase EC 1.4.99.1, D-aspartate oxidase EC 1.4.3.1. D-amino acid oxidase EC 1.4.3.3 (DAMOX or DAO) is an ... FAD flavoenzyme that catalyses the oxidation of neutral and basic D-amino acids into their corresponding keto acids. DAOs have ... In molecular biology, the FAD dependent oxidoreductase family of proteins is a family of FAD dependent oxidoreductases. Members ...
CH-CH oxidoreductases) EC 1.4 includes oxidoreductases that act on the CH-NH2 group of donors (Amino acid oxidoreductases, ... EC 1.1 includes oxidoreductases that act on the CH-OH group of donors (alcohol oxidoreductases) EC 1.2 includes oxidoreductases ... Oxidoreductases are classified as EC 1 in the EC number classification of enzymes. Oxidoreductases can be further classified ... Superfamilies of single-pass transmembrane oxidoreductases in Membranome database Media related to Oxidoreductases at Wikimedia ...
... a four-amino-acid insert in the protein pyruvate flavodoxin/ferredoxin oxidoreductase, a protein which plays important roles in ... and fatty acid profiles that are consistently absent in the other suborder. In addition to demarcating taxonomic ranks, CSIs ... Nucleic Acids Research. 18 (7): 1929. doi:10.1093/nar/18.7.1929. PMC 330654. PMID 1692410. Khadka B, Adeolu M, Blankenship RE, ...
FAD is also bound by hydrogen bonds with neighboring amino acid main chains and side chains. The co-crystallization of THCA ... and aclacinomycin oxidoreductase (AknOx). The FAD moiety is the location of enzymatic activity and is covalently bound to ... THCA synthase is a 60 kDa (~500 amino acids) monomeric enzyme with the isoelectric point at 6.4. Post-translational N-linked ... Enzymes that share similar amino acid sequences include the flavoproteins berberine bridge enzyme (BBE), glucooligosaccharide ...
The amino acids surrounding the quinone are all hydrophobic. Also, there is a highly conserved region of uncharged amino acids ... Where does sulfide:quinone oxidoreductase fit into metabolism? As mentioned previously, sulfide:quinone oxidoreductase is an ... Both amino acids are located in the hydrophobic region of the plasma membrane and are conserved among all sulfide: quinone ... number indicates that the protein is an oxidoreductase (indicated by 1). The oxidoreductase reacts with a sulfur molecule in ...
This enzyme is a flavoprotein belonging to the FAD dependent oxidoreductase family, and acts on the CH-NH2 group of D-amino ... D-amino acid oxidase reacts to D-amino acids and can be used to detect the amount of D-amino acids in foods to act as a ... DAOA-AS1 D-amino acid dehydrogenase D-amino acid oxidase activator D-aspartate oxidase Diamine oxidase D-Amino-Acid+Oxidase at ... D-amino acid oxidase (DAAO; also OXDA, DAMOX) is an enzyme with the function on a molecular level to oxidize D-amino acids to ...
Its amino acid sequence is partly (40-50%) homologous to several other oxidoreductases, such as berberine bridge enzyme in ... oxygen oxidoreductase (cyclizing, cannabidiolate-forming). It is an oxidoreductase found in Cannabis sativa that catalyses the ... Biochemical analysis of a novel enzyme that catalyzes the oxidocyclization of cannabigerolic acid to cannabidiolic acid". The ... Cannabidiolic+acid+synthase at the US National Library of Medicine Medical Subject Headings (MeSH) Biology portal. ...
Broadly, it is suggested that tsRNAs regulate carbohydrate and amino acid metabolism in Burkholderia. They are more highly ... Specific targets include 4-hydroxyphenylpyruvic acid dioxygenase (hppD) and indolepyruvate ferredoxin oxidoreductase (ior). ... Conversely, overexpression of tsRNAs impairs growth in an amino-acid rich environment. This attenuation of growth depends on ... Likely targets include many genes that regulate carbohydrate transport and the degradation of aromatic amino acids. ...
1-amino-2-propanol oxidoreductase, and aminopropanol oxidoreductase. This enzyme participates in butanoic acid metabolism. ... D-1-amino-2-propanol dehydrogenase, (R)-diacetyl reductase, (R)-2,3-butanediol dehydrogenase, D-1-amino-2-propanol:NAD+ ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ ... The systematic name of this enzyme class is (R,R)-butane-2,3-diol:NAD+ oxidoreductase. Other names in common use include ...
CH-NH2 oxidoreductases (EC 1.4) - primarily amino acid oxidoreductases. 1.4.1: NAD/NADP acceptor. *Glutamate dehydrogenase * ... Glycine oxidase (EC 1.4.3.19) is an enzyme with systematic name glycine:oxygen oxidoreductase (deaminating).[1][2] This enzyme ...
The gene produces a 7.756 kDa protein composed of 74 amino acids. The protein encoded by the NDUFAF8 gene is involved in the ... NADH:ubiquinone oxidoreductase complex assembly factor 8 is a protein that in humans is encoded by the NDUFAF8 gene. This ... "Entrez Gene: NADH:ubiquinone oxidoreductase complex assembly factor 8". Retrieved 2018-07-27. CS1 maint: discouraged parameter ... assembly of mitochondrial Complex I (NADH-ubiquinone oxidoreductase). This protein is required to stabilize NDUFAF5 during ...
Four with the pattern of C-X-X-C-at amino acids 45, 70, 86, and 96-and the fifth spacing at amino acid 89 (CAC). The C-X-X-C ... pattern is known to be present in metal-binding proteins and oxidoreductases. Additionally, three of the five cysteine spacings ... The amino acid cysteine appears the most throughout the protein sequence as a conserved amino acids; 8 out of 20 instances. ... 20 amino acids were discovered to be conserved among all 15 sequences at the beginning of the protein sequence; within the ...
Jaiswal AK, Burnett P, Adesnik M, McBride OW (1990). "Nucleotide and deduced amino acid sequence of a human cDNA (NQO2) ... Strassburg A, Strassburg CP, Manns MP, Tukey RH (2002). "Differential gene expression of NAD(P)H:quinone oxidoreductase and NRH ... Kwiek JJ, Haystead TA, Rudolph J (2004). "Kinetic mechanism of quinone oxidoreductase 2 and its inhibition by the antimalarial ... Wang W, Jaiswal AK (2005). "Sp3 repression of polymorphic human NRH:quinone oxidoreductase 2 gene promoter". Free Radic. Biol. ...
Human ferrochelatase is a homodimer composed of two 359 amino acid polypeptide chains. It has a total molecular weight of 85.07 ... Furthermore, heme B is found in cytochrome b, a key component in Q-cytochrome c oxidoreductase (complex III) in oxidative ...
The amino acid sequence of soybean FLbR is highly related to that of the flavin-nucleotide disulfide oxidoreductases, ... The amino acid sequence of soybean FLbR contains a 30-residue signal peptide for translocation into the mitochondria as well as ... The amino acid sequence of soybean FLbR2 has considerable homology with soybean FLbR1 and pea leaf mitochondria DLDH and ... This enzyme belongs to the family of oxidoreductases, specifically those acting on NADH or NADPH with a heme protein as ...
Leukocyte-type 12-lipoxygenase in these animal species shares 73-86% amino acid identity with human ALOX15 but only 57-66% ... oxygen 12-oxidoreductase, Delta12-lipoxygenase, 12Delta-lipoxygenase, and C-12 lipoxygenase. ALOX12, often termed plate ... It metabolizes the omega-3 fatty acid, docosahexaenoic acid (DHA i.e., 4(Z),7(Z),10(Z),13(Z),16(Z),19(Z)-docosahexaenoic acid ... ALOX12 is 75 kilodalton protein composed of 663 amino acids. Other systematic names for ALOX12 include 12S-Lipoxygenase, ...
These particular proteins are involved in carbohydrate, lipid, and amino acid metabolism. The archaeal proteins involved are ... Bacterial proteins involved are ferredoxin-NADP reductase, acetate kinase, and NADH-quinone oxidoreductase found in the ... amino acid and nucleotide metabolism. A similar study done in 2017 by Maier et. al. combined metaproteomics with metagenomics ... These proteins participate in biochemical pathways involving acetic acid utilization, CO2 reduction, and methyl nutrient usage ...
... lacks the genes for methionine and lysine biosynthesis but has the enzymes that are utilized to biosynthesize amino acids. The ... S. thermophilum contains genes for ferredoxin oxidoreductases, pyruvate, and 2-oxoacid. S. thermophilum ... Nucleic Acids Research. 32 (16): 4937-44. doi:10.1093/nar/gkh830. PMC 519118. PMID 15383646. Ueda K, Ohno M, Yamamoto K, Nara H ...
The amino acid tyrosine contains a single phenolic ring that may be oxidised by the action of PPOs to form o-quinone. Hence, ... Enzyme nomenclature differentiates between monophenol oxidase enzymes (tyrosinases) and o-diphenol:oxygen oxidoreductase ... The brown or black pigments are produced from the reaction of PPO quinone products with amino acid groups in the tuber. In ... doi:10.1111/j.1399-3054.1984.tb04258.x. Kampatsikas I, Rompel A (October 2020). "Similar but Still Different: Which Amino Acid ...
L-amino-acid oxidase Ja 1.4.3.3 D-amino-acid oxidase Ja ... S)-2-hydroxy-acid oxidase Ja 1.1.4.1 vitamin-K-epoxide ... Overgenomen van "https://nl.wikipedia.org/w/index.php?title=Oxidoreductase&oldid=53921510" ...
Thr where X is any amino acid except proline. This sequence is called a glycosylation sequon. The reaction catalyzed by OST is ... EC1 Oxidoreductases (list). *EC2 Transferases (list). *EC3 Hydrolases (list). *EC4 Lyases (list) ...
Branched-chain amino acid aminotransferase. *Alanine-glyoxylate transaminase *AGXT. 2.6.3: Oximinotransferases. * ... EC1 Oxidoreductases (list). *EC2 Transferases (list). *EC3 Hydrolases (list). *EC4 Lyases (list) ...
... encodes a 51.2 kDa protein that is composed of 474 amino acids; 124 peptides have been observed through mass spectrometry ... EC1 Oxidoreductases (list). *EC2 Transferases (list). *EC3 Hydrolases (list). *EC4 Lyases (list) ... fatty acid metabolic process. • metabolism. • cardiolipin acyl-chain remodeling. • fatty acid beta-oxidation. ... transferase activity, transferring acyl groups other than amino-acyl groups. • enoyl-CoA hydratase activity. • long-chain-3- ...
The glycogen phosphorylase monomer is a large protein, composed of 842 amino acids with a mass of 97.434 kDa in muscle cells. ... EC1 Oxidoreductases (list). *EC2 Transferases (list). *EC3 Hydrolases (list). *EC4 Lyases (list) ...
... as all ingested SOD is broken down into amino acids before being absorbed. However, ingestion of SOD bound to wheat proteins ... Other oxidoreductases (EC 1.15-1.21). 1.15: Acting on superoxide as acceptor. *Superoxide dismutase *SOD1 ... and their active sites contain the same type and arrangement of amino acid side-chains. They are usually dimers, but ... superoxide inactivates the citric acid cycle enzyme aconitase, can poison energy metabolism, and releases potentially toxic ...
The DCXR gene encodes a membrane protein that is approximately 34 kDa in size and composed of 224 amino acids. The protein is ... The systematic name of this enzyme class is xylitol:NADP+ 2-oxidoreductase (L-xylulose-forming). ... This enzyme belongs to the superfamily of short-chain oxidoreductases, specifically those acting on the CH-OH group of donor ...
Structural implications of novel amino acid substitutions in E1 protein". Molecular Genetics and Metabolism. 104 (4): 507-16. ... oxidoreductase activity. • pyruvate dehydrogenase (acetyl-transferring) activity. • oxidoreductase activity, acting on the ... "An amino acid substitution in the pyruvate dehydrogenase E1 alpha gene, affecting mitochondrial import of the precursor protein ...
cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases". The Journal of Biological Chemistry. 264 (16 ... oxidoreductase activity. • glyceraldehyde oxidoreductase activity. • alditol:NADP+ 1-oxidoreductase activity. • alcohol ... AKR1B1 consists of 316 amino acid residues and weighs 35853Da. It does not possess the traditional dinucleotide binding fold. ... "Nucleic Acids Research. 17 (20): 8368. doi:10.1093/nar/17.20.8368. PMC 334974. PMID 2510130.. ...
... beyond the twenty canonical amino acids found in nature, to include an unnatural amino acid as well. The unnatural amino acid ... the tRNA with the amino acid. Once the tRNA is charged, a ribosome can transfer the amino acid from the tRNA onto a growing ... and redox-active amino acids.[14] Another use is introducing amino acids bearing reactive functional groups for chemically ... the cavity that holds the amino acid can be mutated and modified to carry unnatural amino acids synthesized in the lab, and to ...
McMullen BA, Fujikawa K, Kisiel W, Sasagawa T, Howald WN, Kwa EY, Weinstein B (June 1983). "Complete amino acid sequence of the ... EC1 Oxidoreductases (list). *EC2 Transferases (list). *EC3 Hydrolases (list). *EC4 Lyases (list) ... 2fzz: Factor Xa in complex with the inhibitor 1-(3-amino-1,2-benzisoxazol-5-yl)-6-(2'-(((3r)-3-hydroxy-1-pyrrolidinyl)methyl)-4 ... 1mq6: Crystal Structure of 3-chloro-N-[4-chloro-2-[[(5-chloro-2-pyridinyl)amino]carbonyl]-6-methoxyphenyl]-4-[[(4,5-dihydro-2- ...
Human ALOX5 is a soluble, monomeric protein consisting of 673 amino acids with a molecular weight of ~78 kDa. Structurally, ... oxidoreductase activity. • oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, ... Arachidonic acidEdit. ALOX5 metabolizes the omega-6 fatty acid, Arachidonic acid (AA, i.e. 5Z,8Z,11Z,15Z-eicosatrienoic acid), ... Eicosapentaenoic acidEdit. ALOX5 metabolizes the omega-3 fatty acid, Eicosapentaenoic acid (EPA, i.e. 4Z,8Z,11Z,14Z,17Z- ...
"Exogenous γ-aminobutyric acid treatment affects citrate and amino acid accumulation to improve fruit quality and storage ... EC1 Oxidoreductases (list). *EC2 Transferases (list). *EC3 Hydrolases (list). *EC4 Lyases (list) ... Glutamic acid decarboxylase is the rate-limiting enzyme in the synthesis of γ-aminobutyric acid (GABA), and impaired function ... Glutamate decarboxylase or glutamic acid decarboxylase (GAD) is an enzyme that catalyzes the decarboxylation of glutamate to ...
... that appears to be associated with binding the incoming amino acid. The conserved sequence motifs found in the four Mur enzymes ... EC1 Oxidoreductases (list). *EC2 Transferases (list). *EC3 Hydrolases (list). *EC4 Lyases (list) ... 1) formation of UDP-N-acetylmuramic acid (UDPMurNAc) from N-acetylglucosamine (GlcNAc). ... N-acetylmuramic acid. All four Mur ligases are topologically similar to one another, even though they display low sequence ...
The amino acid side-chains of the active site are bent into positions so the enzyme does its catalytic work. In some cases, ... Oxido-reductases: catalyse transfer of electrons. *Transferases: move functional group from one molecule to another ... They break down other enzymes and proteins back into amino acids.[3] Nucleases are enzymes that cut DNA or RNA, often in ... For example, fatty acids are synthesized by one set of enzymes in the cytosol, endoplasmic reticulum and Golgi apparatus. Then ...
Glutamate is a principal amino donor to other amino acids in subsequent transamination reactions. The multiple roles of ... P. falciparum lactate dehydrogenase (PfLDH) is a 33 kDa oxidoreductase [EC 1.1.1.27].[14] It is the last enzyme of the ... glutamate in nitrogen balance make it a gateway between free ammonia and the amino groups of most amino acids. Its crystal ...
The complete amino acid sequence". European Journal of Biochemistry. 169 (3): 547-53. doi:10.1111/j.1432-1033.1987.tb13644.x. ... EC1 Oxidoreductases (list). *EC2 Transferases (list). *EC3 Hydrolases (list). *EC4 Lyases (list) ... The complete amino acid sequence". European Journal of Biochemistry. 169 (3): 547-53. doi:10.1111/j.1432-1033.1987.tb13644.x. ... sialic acid, and one of its two carbohydrate chains still reassembles with C1q and C1r to form a functional C1 complex". ...
... s (HATs) are enzymes that acetylate conserved lysine amino acids on histone proteins by transferring ... EC1 Oxidoreductases (list). *EC2 Transferases (list). *EC3 Hydrolases (list). *EC4 Lyases (list) ... a 110-amino acid module that recognizes acetylated lysine residues and is functionally linked to the co-activators in the ... The number of amino acid residues in each HAT is indicated at the right in each example. ...
In modern-day enzymes, although the three-dimensional structures are very similar, the amino acid sequences are more divergent ... EC1 Oxidoreductases (list). *EC2 Transferases (list). *EC3 Hydrolases (list). *EC4 Lyases (list) ... Taylor RK, LaPointe CF (2000). "The type 4 prepilin peptidases comprise a novel family of aspartic acid proteases". J. Biol. ... While a number of different mechanisms for aspartyl proteases have been proposed, the most widely accepted is a general acid- ...
A component of the fatty acid beta oxidation pathway. „J. Biol. Chem.". 252 (23), s. 8440-5, 1977. PMID: 925004. ... Kita K, Hirawake H, Miyadera H, Amino H, Takeo S. Role of complex II in anaerobic respiration of the parasite mitochondria from ... Brandt U, Kerscher S, Dröse S, Zwicker K, Zickermann V. Proton pumping by NADH: ubiquinone oxidoreductase. A redox driven ... menaquinol:fumarate oxidoreductase), przeprowadza reakcję odwrotną, redukując fumaran. Pozwala to przeżyć pasożytowi w ...
The LDHBx protein is seven amino acids longer than the LDHB (LDH-H) protein. This amino acid extension is generated by ... Oxidoreductase. References[edit]. This article incorporates text from the public domain Pfam and InterPro IPR015409 ... This leads to the addition of seven amino acid acids to the normal LDH-H protein. The extension contains a peroxisomal ... LDHBx is generated by translation of the LDHB mRNA, but the stop codon is interpreted as an amino acid-encoding codon. In ...
These residues can broadly be classified as surface- and interior-allosteric amino acids. Allosteric sites at the surface ... EC1 Oxidoreductases (list). *EC2 Transferases (list). *EC3 Hydrolases (list). *EC4 Lyases (list) ... that is not itself an amino acid. For instance, many enzymes require sodium binding to ensure proper function. However, the ... "Nucleic Acids Res. 39: D663-669. doi:10.1093/nar/gkq1022. PMC 3013650 . PMID 21051350.. CS1 maint: Explicit use of et al. (link ...
oxidoreductase activity. • iron ion binding. • ferric iron binding. • protein binding. • amino acid binding. • monooxygenase ... The amino terminal ~150 amino acids make up a regulatory domain, thought to control access of substrates to the active site.[17 ... aromatic amino acid family metabolic process. • response to lipopolysaccharide. • cerebral cortex development. • response to ... Tyrosine hydroxylase or tyrosine 3-monooxygenase is the enzyme responsible for catalyzing the conversion of the amino acid L- ...
Transamination, or the transfer of an amine (or NH2) group from an amino acid to a keto acid by an aminotransferase (also known ... hydrogen transfer is included under oxidoreductases, due to electron transfer considerations. EC 2.1 includes enzymes that ... Braunstein AE, Kritzmann MG (1937). "Formation and Breakdown of Amino-acids by Inter-molecular Transfer of the Amino Group". ... the growing amino acid chain from the tRNA molecule in the A-site of the ribosome and its subsequent addition to the amino acid ...
"Molecular cloning and amino acid sequence of leukotriene A4 hydrolase". Proc. Natl. Acad. Sci. U.S.A. 84 (19): 6677-81. doi: ... EC1 Oxidoreductases (list). *EC2 Transferases (list). *EC3 Hydrolases (list). *EC4 Lyases (list) ... Enzymatic conversion into 5,6-dihydroxy-7,9,11,14-eicosatetraenoic acid by mouse liver cytosolic epoxide hydrolase". J. Biol. ...
Herrmann K, Entus R (2001). "Shikimate Pathway: Aromatic Amino Acids and Beyond". Encyclopedia of Life Sciences. doi:10.1038/ ... EC1 Oxidoreductases (list). *EC2 Transferases (list). *EC3 Hydrolases (list). *EC4 Lyases (list) ... each of which sensitive to one of the amino acids produced in the shikimate pathway.[3] In a study of DAHP synthase sensitive ... which is responsible for the biosynthesis of the amino acids phenylalanine, tyrosine, and tryptophan. Since it is the first ...
Position of active site amino acid residues of vanadium containing chloroperoxidase shown in relation to enzyme surface.(From ... EC1 Oxidoreductases (list). *EC2 Transferases (list). *EC3 Hydrolases (list). *EC4 Lyases (list) ... Glucose 6-phosphatase consists of 357 amino acids, and is anchored to the endoplasmic reticulum (ER) by nine transmembrane ... Glucose 6-phosphatase-β is a ubiquitously expressed, 346-amino acid membrane protein that shares 36% sequence identity with ...
... has three key amino acids in its active site (known as the catalytic triad) which catalyze the conversion of ... EC1 Oxidoreductases (list). *EC2 Transferases (list). *EC3 Hydrolases (list). *EC4 Lyases (list) ... Citrate synthase's 437 amino acid residues are organized into two main subunits, each consisting of 20 alpha-helices. These ... 2.3.1: other than amino-acyl groups. *acetyltransferases: Acetyl-Coenzyme A acetyltransferase ...
Such Gα GAPs do not have catalytic residues (specific amino acid sequences) to activate the Gα protein. They work instead by ... EC1 Oxidoreductases (list). *EC2 Transferases (list). *EC3 Hydrolases (list). *EC4 Lyases (list) ...
In mammals, this metabolic pathway is important in beta oxidation of fatty acids and catabolism of amino acids and choline, as ... NADH-coenzyme Q oxidoreductase (complex I)Edit. Complex I or NADH-Q oxidoreductase. The abbreviations are discussed in the text ... Q-cytochrome c oxidoreductase (complex III)Edit. The two electron transfer steps in complex III: Q-cytochrome c oxidoreductase ... Each iron atom in these clusters is coordinated by an additional amino acid, usually by the sulfur atom of cysteine. Metal ion ...
Amino acid oxidoreductases are oxidoreductases, a type of enzyme, that act upon amino acids. They constitute the majority of ... Examples include: Glutamate dehydrogenase Nitric oxide synthase Amino+Acid+Oxidoreductases at the US National Library of ...
Scientific Experts about Experts and Doctors on amino acid oxidoreductases in United States ... amino acid oxidoreductases*biglycan*decorin*matrix metalloproteinase 3*fendiline*alanine dehydrogenase*exfoliation syndrome* ... Experts and Doctors on amino acid oxidoreductases in United States. Summary. Locale: United States ... You are here: Locale , Experts and Doctors on amino acid oxidoreductases in United States ...
Species about Experts and Doctors on amino acid oxidoreductases in Massachusetts, United States ... amino acid oxidoreductases*glycine decarboxylase complex*clorgyline*aminopropionitrile*selegiline*reticulocytes*monoamine ... Experts and Doctors on amino acid oxidoreductases in Massachusetts, United States. Summary. Locale: Massachusetts, United ... You are here: Locale , United States , Experts and Doctors on amino acid oxidoreductases in Massachusetts, United States ...
Science: enzyme) a class of enzymes that catalyze oxidation-reduction reactions of amino acids. ... Retrieved from "https://www.biology-online.org/dictionary/index.php?title=Amino_acid_oxidoreductases&oldid=54296" ... Amino acid oxidoreductases ( ... Amino acid oxidoreductases. From Biology-Online Dictionary , ...
This variant amino acid is located in an oxidoreductase domain; whether it represents a rare polymorphism or a missense ... involves a G to A transition at nucleotide 547 and results in an aspartic acid to asparagine substitution at amino acid 183 ( ... WW Domain Containing Oxidoreductase Gene Expression Is Altered in Non-Small Cell Lung Cancer. Sai Yendamuri, Tamotsu Kuroki, ... 4 The abbreviations used are: NSCLC, non-small cell lung cancer; WWOX, WW domain containing oxidoreductase gene; LOH, loss of ...
Amino Acid Oxidoreductases / metabolism* * Animals * Calcium / metabolism * Cardiomyopathy, Dilated / enzymology* * Enzyme ...
Amino Acid Oxidoreductases / antagonists & inhibitors * Amino Acid Oxidoreductases / metabolism * Animals * Arginine / analogs ...
D-Amino acid: oxygen oxidoreductase, deaminating, DAO, OXDA), A1373 - Get the Best Quote/Price and read Reviews, Features and ... D-Amino Acid Oxidase, Porcine Kidney (D-AAO, ... D-Amino Acid Oxidase, Porcine Kidney (D-AAO, D-Amino acid: ... D-Amino Acid Oxidase, Porcine Kidney (D-AAO, D-Amino acid: oxygen oxidoreductase, deaminating, DAO, OXDA). Cat no: A1373. ... Amino Acid Analysis and Molecular Weight of Homogeneous D-Amino Acid Oxidase from Pig Kidney, Biochim. Biophys. Acta, 327, 266 ...
0 (Antifungal Agents); 0 (Plant Extracts); EC 1.4.- (Amino Acid Oxidoreductases); EC 1.4.1.- (aspartate dehydrogenase); EC 3.1 ... While these substances all contain tannins, testing to possible constituents tannic acid and gallic acid was negative.. ... thereby affecting amino acid biosynthesis. CONCLUSION: Thus, this study confirms the anti-candidal potential of L. inermis and ... Amino cido Oxirredutases/metabolismo. Antif ngicos/farmacologia. Candida albicans/efeitos dos f rmacos. Medicina Herb ria. ...
0 (Antiviral Agents); 0 (Culture Media); 0 (Fungal Proteins); 0 (RNA, Viral); EC 1.4.- (Amino Acid Oxidoreductases); EC 1.4. ... Amino cido Oxirredutases/bioss ntese. Amino cido Oxirredutases/isolamento & purifica o. Antivirais/isolamento & purifica o. ... Amino cido Oxirredutases/farmacologia. Antivirais/farmacologia. Prote nas F ngicas/farmacologia. Nepovirus/efeitos dos f rmacos ...
L-amino acid: oxidoreductase deaminating; EC 1.4.1.X) are members of the wider superfamily of oxidoreductases that catalyze the ... reversible oxidative deamination of an amino acid to its keto acid and ammonia with ... BACKGROUND: Amino acid dehydrogenases (L-amino acid: oxidoreductase deaminating; EC 1.4.1.X) are members of the wider ... Amino Acid Oxidoreductases / isolation & purification, metabolism*. Amino Acids / metabolism. Bacteria / enzymology*, isolation ...
Previously, we found that expression of AhAREB1 was specifically induced by abscisic acid (ABA), dehydration and drought. To ... abscisic acid-insensitive 5). Constitutive expression of AhAREB1 confers water stress tolerance and is highly sensitive to ... Arachis hypogaea Abscisic-acid Response Element Binding Protein 1) is a member of the basic domain leucine zipper (bZIP)-type ... Reconstructing a Flavodoxin Oxidoreductase with Early Amino Acids. Previous Article in Journal. Putative Genes Involved in ...
Quinone oxidoreductaseAdd BLAST. 328. Amino acid modifications. Feature key. Position(s). DescriptionActions. Graphical view. ... It always involves more than one amino acid and includes all residues involved in nucleotide-binding.,p>,a href=/help/np_bind ... It always involves more than one amino acid and includes all residues involved in nucleotide-binding.,p>,a href=/help/np_bind ... It always involves more than one amino acid and includes all residues involved in nucleotide-binding.,p>,a href=/help/np_bind ...
Title: Mutations in NADH:ubiquinone oxidoreductase of Escherichia coli affect growth on mixed amino acids*Comment: *External ... Mutations in NADH:ubiquinone oxidoreductase of Escherichia coli affect growth on mixed amino acids. J.Bacteriol. 176:2143-2150 ...
Putative oxidoreductase that is recruited on chromatin and promotes KDM1B demethylase activity. Recognizes and binds ... Putative oxidoreductase GLYR1Add BLAST. 553. Amino acid modifications. Feature key. Position(s). DescriptionActions. Graphical ... It always involves more than one amino acid and includes all residues involved in nucleotide-binding.,p>,a href=/help/np_bind ... p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. ...
... they utilize aldehyde ferredoxin oxidoreductase to metabolize the amino acid carbon source. AOR is homodimeric. Each 67kDa ... Its primary role is to oxidize aldehyde coming derived from the metabolism of amino acids and glucoses. Aldehyde Ferredoxin ... However, other proposals include its role in oxidation of amino acid metabolism aldehyde side products coming from de-aminated ... Iron atom in the cluster is additionally bound by three other Cystein ligands: . Also, another linker amino acid residue ...
Supplementary Material 3. Amino acid alignment of arsenite oxidoreductase subunit A.. Supplementary Material 4. Spreadsheet of ... A total of 46 tRNA genes are present and cover the 20 standard amino acids, except as in BOGUAY, tRNA-Arg-TCT and tRNA-Leu-TAA ... Le, S. Q., and Gascuel, O. (2008). An improved general amino acid replacement matrix. Mol. Biol. Evol. 25, 1307-1320. doi: ... For maximum likelihood analysis, the LG amino acid substitution model (Le and Gascuel, 2008) with proportions of invariant ...
Cladogram of fungal cytochrome P450 oxidoreductases based on amino acid sequences. The accession numbers are as follows: ... R-OH-α-ionylideneacetic acid (structure 4), (1′R)-4′S-OH-α-ionylideneacetic acid (structure 5), 1′-OH-α-ionylideneacetic acid ( ... As expected from the EST data, the derived amino acid sequence of bcaba1 showed significant homology to fungal P450 ... A linear gradient of H2O (containing 10 mM ammonium acetate and 20 mM formic acid) and CH3CN (containing 20 mM formic acid) was ...
Class II and III ER oxidoreductases have an a-b-b′-a′ domain structure. Class II ER oxidoreductases have an acidic amino acid- ... GmERO1a and GmERO1b encoded proteins composed of 465 amino acids containing 19 Cys residues (Fig. 1A and Supplemental Fig. S1 ... ER oxidoreductase. GmPDIS. recombinant soybean class IV ER oxidoreductase. GSH. glutathione. GST. glutathione-s-transferase. IP ... Supplemental Figure S1. Amino acid sequences of GmERO1a, GmERO1b, and HsEro1α. ...
... amino acids), and enzymes. The antigenic conjugates are employed for the production of antibodies, which find particular use in ... Primarily, the enzymes of choice, based on the I.U.B. classification are: Class 1. Oxidoreductases and Class 3. Hydrolases. ... amino acid), which is antigenic or an enzyme, which poly(amino acid) is joined by a bond to a methylene group when m is 0 and ... Alternatively, synthetic poly(amino acids) may be prepared having a sufficient number of available amino groups, e.g., lysines. ...
Class: oxidoreductase. Keywords: Cysteine, Cys-Tyr cofactor, iron, unnatural amino acid, OXIDOREDUCTASE. Deposited on 2017-11- ... Nucleic Acids Research 42:D304-309. doi: 10.1093/nar/gkt1240. Chandonia JM, Fox NK, Brenner SE. 2019. Nucleic Acids Research ...
... is a 220 amino acid glycoprotein structurally similar to oxidoreductases. However, CREG does not have enzymatic activities ... is a 220 amino acid glycoprotein structurally similar to oxidoreductases. However, CREG does not have enzymatic activities ... The cellular repressor of E1A-stimulated genes (CREG) is a 220 amino acid glycoprotein structurally similar to oxidoreductases ... amino acids 1-31 in human and mice, 1-23 amino acids in Drosophila) and one or more N-glycosylation sites (three in human, N160 ...
Quantitative amino-acid analysis of bovine NADH:ubiquinone oxidoreductase (Complex I) and related enzymes. Consequences for the ... Amino acid replacements at the H2-activating site of the NAD-reducing hydrogenase from Alcaligenes eutrophus.Biochemistry38: ... The amino acids identified as conserved signatures, among which are two pairs of cysteines, surround the Ni-Fe active site (15 ... The hoxW gene encodes an SH-specific endopeptidase that removes 24 amino acids from the C-terminal end of the HoxH precursor ...
Oxidoreductase (EC 1). *1.1 Aldose reductase. *HMG-CoA reductase. *1.3 5α-Reductase ... An aromatic L-amino acid decarboxylase inhibitor (synonyms: DOPA decarboxylase inhibitor, DDCI and AAADI) is a medication which ... inhibits the synthesis of dopamine by the enzyme aromatic L-amino acid decarboxylase (AADC, AAAD, or DOPA decarboxylase). ... Retrieved from "https://en.wikipedia.org/w/index.php?title=Aromatic_L-amino_acid_decarboxylase_inhibitor&oldid=907336753" ...
The PduS protein is a possibility, since it is related in amino acid sequence to several membrane-bound oxidoreductases. In ... over 611 amino acids, to the DdrA proteinK. oxytoca, and the PduH protein is 87% identical in sequence (99 of 124 amino acids) ... The edited alignment consisted of sequences 85 amino acids in length that aligned to the following PduA amino acids: ... for tree construction consisted of a group of sequences 77 amino acids in length that aligned to the following PduN amino acid ...
... amino-acid biosynthesis lysine biosynthesis aspartate β -semialdehyde dehydrogenase oxidoreductases Francisella tularensis ... Among the acidic amino acid decarboxylases, GADL1 is most similar to cysteine sulfinic acid decarboxylase (CSAD), but the ... Structure of the mouse acidic amino acid decarboxylase GADL1. Pyridoxal 5 ′ -phosphate (PLP) is a ubiquitous cofactor in ... The two proposed forms, HicABL and HicABS, differed in the presence or absence of a seven-amino-acid segment at the N-terminus ...
... or proline amino acid residues and also that a conserved negatively charged amino acid residue at the end of the second β-sheet ... Dendrogram of type II NAD(P)H:quinone oxidoreductases, based on an amino acid sequence alignment of NDH-2 from prokaryotic and ... quinone oxidoreductases by using both the available annotations and amino acid sequence comparisons. Since a clear distinction ... In addition, the amino acid sequence of human AIF (1M6IA) was analyzed and the obtained predictions were cross-checked with the ...
Alignment of the amino acid sequence of P. furiosus NROR with other NADH:rubredoxin oxidoreductases. The GenBank accession ... The amino acid sequence of NROR (deduced from the gene sequence) contains both an NADH-binding domain and a FAD-binding domain ... The percentage of amino acid sequence similarities compared to the sequence of P. furiosus NROR are indicated. The ... Catalytic properties of recombinant NROR.Because amino acid sequence analysis and the UV-visible spectrum of NROR indicated the ...
Class: oxidoreductase. Keywords: Rossmann fold, Branched-chain amino acid biosynthesis, Knotted protein, NADPH, Isomerase, ... Compound: Putative ketol-acid reductoisomerase (Os05g0573700 protein). Species: Oryza sativa Japonica Group [TaxId:39947]. Gene ... Compound: Putative ketol-acid reductoisomerase (Os05g0573700 protein). Species: Oryza sativa Japonica Group [TaxId:39947]. Gene ... OXIDOREDUCTASE. Deposited on 2009-01-08, released 2009-04-14. The last revision prior to the SCOPe 2.07 freeze date was dated ...
311 amino acids (complete) Source: UniProtKB. Protein family membership. None predicted.. Homologous superfamilies. ...
  • It has been shown that the genes involved in gibberellic acid (GA 3 ) biosynthesis are arranged in a cluster ( 34 ) and that the biosynthesis in major respects is different from the higher plant pathway ( 12 ). (asm.org)
  • This study demonstrates the function of the FaQR enzyme in the biosynthesis of HDMF as enone oxidoreductase and provides a foundation for the improvement of strawberry flavor and the biotechnological production of HDMF. (plantcell.org)
  • Umbargar, H. E. (1978) Amino acid biosynthesis and its regulation. (springer.com)
  • 1986) Peptides of 2-aminopimelic acid: antibacterial agents that inhibit diaminopimelic acid biosynthesis. (springer.com)
  • Bhattacharjee, J. K. and Strassman, M. (1967) Accumulation of tricarboxylic acids related to lysine biosynthesis in a yeast mutant. (springer.com)
  • In the current model of medium-chain (C8-14) fatty acid biosynthesis in seeds, specialized FatB acyl-acyl-carrier-protein (ACP) thioesterases are responsible for the production of medium chains. (usda.gov)
  • Specifically, it integrates distributed information from the literature to provide a complete and detailed view for metabolic processes such as acetyl-CoA synthesis, pyruvate synthesis, glycolysis/gluconeogenesis, reductive tricarboxylic acid (RTCA) cycle, non-oxidative pentose phosphate pathway (NOPPP), nitrogen metabolism, amino acid metabolism, and nucleotide biosynthesis. (pubmedcentralcanada.ca)
  • In enzymology, an aldehyde ferredoxin oxidoreductase (EC 1.2.7.5) is an enzyme that catalyzes the chemical reaction an aldehyde + H2O + 2 oxidized ferredoxin ⇌ an acid + 2 H+ + 2 reduced ferredoxin This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with an iron-sulfur protein as acceptor. (wikipedia.org)
  • The conserved NAD-binding sites and sequence similarity to plant dehydrogenases suggest that this protein may have oxidoreductase activity. (uniprot.org)
  • Oxidative folding is catalyzed by protein disulfide isomerase ( PDI ) and PDI -related ER protein thiol disulfide oxidoreductases (ER oxidoreductases). (plantphysiol.org)
  • Enoyl-acyl carrier protein (ACP) reductase II (FabK) is a critical rate-limiting enzyme in the bacterial type II fatty-acid synthesis (FAS II) pathway. (medworm.com)
  • rNROR is a 39.9-kDa protein whose sequence contains both flavin adenine dinucleotide (FAD)- and NAD(P)H-binding motifs, and it shares significant similarity with known and putative Rd-dependent oxidoreductases from several anaerobic bacteria, both mesophilic and hyperthermophilic. (asm.org)
  • Sequence analysis of two peptide fragments showed total identity with the protein sequence of a strongly ripening-induced, auxin-dependent putative quinone oxidoreductase, Fragaria × ananassa quinone oxidoreductase (FaQR). (plantcell.org)
  • The open reading frame of the FaQR cDNA consists of 969 bp encoding a 322-amino acid protein with a calculated molecular mass of 34.3 kD. (plantcell.org)
  • Amino acids 50 - 65 have also been suggested to contain thiol-protein oxidoreductase activity (12). (rndsystems.com)
  • Most of the mutations that cause cytochrome P450 oxidoreductase deficiency change single protein building blocks (amino acids) in cytochrome P450 oxidoreductase. (medlineplus.gov)
  • Comparison of the amino acid sequence to those of other flavoproteins revealed two separate domains that are likely to be involved in flavin binding: a long segment (residues 77-228) homologous with Desulfovibrio vulgaris flavodoxin, an FMN-containing protein, and a shorter segment (residues 452-477) homologous with the FAD-binding segment of fumarate reductase from Escherichia coli. (pnas.org)
  • P450 (cytochrome) oxidoreductase is a reported synonym of the human protein 'cytochrome p450 oxidoreductase', encoded by the gene POR. (biocompare.com)
  • The full protein is reported to be 677 amino acid residues in length. (biocompare.com)
  • Type II enzymes, including both drug-metabolizing and some steroidogenic enzymes, require electron donation from a two-flavin protein, P450 oxidoreductase (POR). (sciencemag.org)
  • Effects of Flavin-Binding Motif Amino Acid Mutations in the NADH-Cytochrome b5 Reductase Catalytic Domain on Protein Stability and Catalysis1. (ebscohost.com)
  • These data demonstrate the involvement of a mitochondrial protein, ETFQO, in the catabolism of Leu and potentially of other amino acids in higher plants and also imply a novel role for this protein in the chlorophyll degradation pathway activated during dark-induced senescence and sugar starvation. (plantcell.org)
  • WWOX is a 414 amino acid protein that contains two WW domains and a short-chain dehydrogenase/reductase (SDR) domain. (atlasgeneticsoncology.org)
  • Recombinant Disulfide Oxidoreductase (rDsbA), produced from E.Coli is a periplasmic protein and thioredoxin superfamily member which introduces disulfide bonds directly into substrate proteins by donating the disulfide bond in its active-site Cys30-Pro31-His32-Cys33 to a pair of cysteines in substrate proteins. (acris-antibodies.com)
  • is 993 base pairs in length, and encodes a protein of 330 amino acids (40 kDa) with homology to oxidoreductases. (proquest.com)
  • Mutations causing single amino acid exchanges can dramatically affect protein stability and function, leading to disease. (springer.com)
  • We will review the function of these proteins and their dysfunction in cancer and then describe in some detail the effects of the most relevant cancer-associated single amino exchanges using a translational perspective, from the viewpoints of molecular genetics and pathology, protein biochemistry and biophysics, structural, and cell biology. (springer.com)
  • Anwar A, Dehn D, Siegel D, Kepa JK, Tang LJ, Pietenpol JA, Ross D (2003) Interaction of human NAD(P)H:quinone oxidoreductase 1 (NQO1) with the tumor suppressor protein p53 in cells and cell-free systems. (springer.com)
  • The deduced amino acid sequence indicated that the 333 aa protein contains an NAD(P)H-binding motif. (jove.com)
  • In contrast, modification of other active site residues or of amino acids in the flexible active site loops has little effect, highlighting these regions as potential targets in designing an enzyme that will accept larger substrates. (labome.org)
  • Thus, pterin and Tungsten atoms are connected to the AOR enzyme primarily through pterin's Hydrogen bonding networks with the amino acid residues. (wikipedia.org)
  • The deduced amino acid composition is in excellent agreement with that determined by direct amino acid analysis of purified rat liver P-450 oxidoreductase, and the amino-terminal region (residues 1-80) largely coincides with the amino-terminal sequence of the oxidoreductase isolated from rabbit liver. (pnas.org)
  • Cloning of rat aorta lysyl oxidase cDNA: complete codons and predicted amino acid sequence. (labome.org)
  • D-Amino Acid Oxidase is a flavoprotein oxidase, flavin being the only prosthetic group. (biosave.com)
  • 4. Tu, S., and McCormick, D.: Photoinactivation of Porcine D-Amino Acid Oxidase with Flavin Adenine Dinucleotide, J. Biol. (biosave.com)
  • Five types of terminal oxygen reductases are known in prokaryotes: three types of heme-copper reductases ( 64 ), the cytochrome bd (quinol:oxygen oxidoreductase) ( 13 ), and the so-called alternative oxidase (quinol:oxygen oxidoreductase), which harbors a di-iron center ( 78 ). (asm.org)
  • Disulphide oxidoreductase (DsbA) is the major oxidase responsible for generation of disulfide bonds in proteins of E. coli envelope. (abcam.com)
  • D-amino acid oxidase from porcine kidney has been extensively studied. (calzyme.com)
  • D-Amino acid oxidase has several possible applications such as the determination of D-amino acids, the separation of natural L- amino acid isomers from a racemic mixture and in the preparation of keto acids. (calzyme.com)
  • The usefulness and application of D-amino acid oxidase can be significantly increased if it is available in an immobilized form (Parkin, K. and Hultin, H.O., Biotech. (calzyme.com)
  • The decrease in the absorbance at 340 nm, due to the oxidation of NADH, is a measure of D-amino acid oxidase activity. (calzyme.com)
  • Initiate the reaction by adding 0.1 ml D-amino acid oxidase (enzyme) to the cuvette. (calzyme.com)
  • Concerning the in vivo function of the enzyme, new findings on the physiological role of D-amino acid oxidase point to a detoxifying function of the enzyme in metabolizing exogenous D-amino acids in animals. (semanticscholar.org)
  • Renal D-amino acid oxidase mediates chiral inversion of N(G)-nitro-D-arginine. (semanticscholar.org)
  • Role of arginine 285 in the active site of Rhodotorula gracilis D-amino acid oxidase. (semanticscholar.org)
  • Chemical mechanism of D-amino acid oxidase from Rhodotorula gracilis: pH dependence of kinetic parameters. (semanticscholar.org)
  • D-amino-acid oxidase gene from Rhodotorula gracilis (Rhodosporidium toruloides) ATCC 26217. (semanticscholar.org)
  • An illustrative serum-activated oxidoreductase enzyme is glucose oxidase with the corresponding. (google.com)
  • 3. The enzymatic material of claim 1 wherein the oxidoreductase enzyme is glucose oxidase. (google.com)
  • 11. The enzymatic material of claim 9 wherein the substrate is glucose and the oxidoreductase enzyme is glucose oxidase. (google.com)
  • L-amino acid oxidase is obtained by culturing a microorganism which can produce L-amino acid oxidase and belongs to the genus Colletotrichum, e.g. (patentgenius.com)
  • 1. A process for producing L-amino acid oxidase which comprises culturing in a culture medium a microorganism which produce L-amino acid oxidase and is a member of the genusColletotrichum, and recovering L-amino acid oxidase from the cells cultured. (patentgenius.com)
  • 2. A process as claimed in claim 1 wherein the L-amino acid oxidase producing microorganism is Collectotrichum sp. (patentgenius.com)
  • The presentinvention relates to a process for producing L-amino acid oxidase. (patentgenius.com)
  • L-amino acid oxidase is an enzyme with the classification No. EC 1.4.3.2. (patentgenius.com)
  • It has now been found that L-amino acid oxidase can be produced in the mycelium of a mold of M5073, isolated from seeds of Calophyllum inophyllum in Hahajima, Bonin Islands, Tokyo, Japan, and have isolated the said enzyme therefrom. (patentgenius.com)
  • Inthe accompanying drawings, FIGS. 1-4 show optimum pH, pH stability, heat stability and optimum temperature of the L-amino acid oxidase of this invention. (patentgenius.com)
  • AS08 and EO chain octylphenol dehydrogenase from Pseudomonas putida share common molecular characteristics with polyethylene glycol (PEG) dehydrogenases (PEG-DH) and comprise a PEG-DH subgroup in the family of glucose-methanol-choline (GMC) oxidoreductases that includes glucose/alcohol oxidase and glucose/choline dehydrogenase. (mdpi.com)
  • We produced α-ketoglutaric acid (α-KG) from L-glutamic acid, using enzymatic transformation approach with L-glutamate oxidase (LGOX). (bvsalud.org)
  • p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. (uniprot.org)
  • Human MIF is a 12.5 kDa, 115 amino acid (aa) nonglycosylated polypeptide that is synthesized without a signal sequence (4 - 7). (rndsystems.com)
  • To decode UGA as Sec, organisms evolved the Sec insertion machinery that allows incorporation of this amino acid at specific UGA codons in a process requiring a cis-acting Sec insertion sequence (SECIS) element. (nih.gov)
  • Genetics of P450 oxidoreductase: sequence variation in 842 individuals of four ethnicities and activities of 15 missense mutations. (medlineplus.gov)
  • The coding nucleotide sequence of the mRNA for NADPH-cytochrome P-450 oxidoreductase (NADPH:ferricytochrome oxidoreductase, EC 1.6.2.4) from rat liver was determined from two overlapping cDNA clones, pOR-7 and pOR-8, which together contain 2401 nucleotides complementary to rat liver oxidoreductase mRNA. (pnas.org)
  • amino acid sequence variant A503V is encoded by ~28% of human alleles. (sciencemag.org)
  • HKE6 possesses remarkable amino acid sequence conservation with several bacterial proteins with oxidoreductase function and also shows significant homology with the two unique functional domains containing the nucleotide cofactor binding site and the consensus motif characteristic of the members of the superfamily of short-chain alcohol dehydrogenases such as human and rat steroid and prostaglandin dehydrogenases. (tcdb.org)
  • Although the sequence similarities of this family are not high and its members catalyze diverse reactions, this family of flavoenzymes contains a conserved ADP-binding motif (an approximately 30 amino acid region) in its N -terminus and the signature 1 and 2 consensus sequences [ 1 ]. (mdpi.com)
  • These enzymes have been received much attention as biocatalysts for use in biosensors or diagnostic kits to screen amino acid metabolism disorders such as phenylketonuria (PKU), maple syrup urine disease (MSUD), homocystinuria (HCY) and hyperprolinemia. (biomedsearch.com)
  • Its primary role is to oxidize aldehyde coming derived from the metabolism of amino acids and glucoses. (wikipedia.org)
  • However, other proposals include its role in oxidation of amino acid metabolism aldehyde side products coming from de-aminated 2-ketoacids. (wikipedia.org)
  • Many metabolic changes take place throughout strawberry fruit growth and ripening, such as the degradation of chlorophyll, the accumulation of anthocyanin, softening, the metabolism of organic acid and sugars, and the production of flavor compounds. (plantcell.org)
  • Because cytochrome P450 oxidoreductase helps regulate the activity of these enzymes, researchers suspect that normal variations in the POR gene may influence a person's response to particular drugs (drug metabolism). (medlineplus.gov)
  • P450 oxidoreductase: genetic polymorphisms and implications for drug metabolism and toxicity. (medlineplus.gov)
  • The most recent research on D-amino acid oxidases and D-amino acid metabolism has revealed new, intriguing properties of flavoenzymes and enlighted novel biotechnological uses of this catalyst. (semanticscholar.org)
  • WWOX (WW domain containing oxidoreductase), a putative tumor suppressor gene that mapsto the common fragile site FRA16D on chromosome 16q23.3-24.1, is altered in breast, esophageal, and ovarian cancer. (aacrjournals.org)
  • Targeted inactivation of the gene bccpr1 encoding a cytochrome P450 oxidoreductase reduced the ABA production significantly, proving the involvement of P450 monooxygenases in the pathway. (asm.org)
  • Lei B, Liu M, Huang S, Tu SC: Vibrio harveyi NADPH-flavin oxidoreductase: cloning, sequencing and overexpression of the gene and purification and characterization of the cloned enzyme. (drugbank.ca)
  • The POR gene provides instructions for making the enzyme cytochrome P450 oxidoreductase. (medlineplus.gov)
  • More than 50 mutations in the POR gene have been found to cause cytochrome P450 oxidoreductase deficiency. (medlineplus.gov)
  • Predicted Amino Acid Sequences of SDHC Gene. (aacrjournals.org)
  • To study the role of the hinge region in nisin and to obtain mutants that exhibit altered or new biological activities and functional properties, we changed certain amino acids in the hinge region by performing site-directed mutagenesis with the nisinZ structural gene (nisZ). (ebscohost.com)
  • The coding sequences of the first 5 (LD5) and 10 (LD10) amino acids of the N-terminus were deleted and the gene was inserted into the. (ebscohost.com)
  • Amino acids in the dihydrofolate reductase-thymidylate synthase gene of Plasmodium falciparum involved in cycloguanil resistance differ from those involved in pyrimethamine resistance. (pnas.org)
  • Pubmed ID: 12624201 This work characterized the putative quinone oxidoreductase gene (qorA) from Staphylococcus aureus. (jove.com)
  • A novel NADPH:quinone oxidoreductase. (uniprot.org)
  • A specific reaction site for NADPH adds to the list of similarities between the SH and mitochondrial NADH:ubiquinone oxidoreductase (Complex I). (asm.org)
  • Oxidative-stress-inducible QorA Encodes an NADPH-dependent Quinone Oxidoreductase Catalysing a One-electron Reduction in Staphylococcus Aureus Microbiology (Reading, England). (jove.com)
  • In mammals, electron-transfer flavoprotein:ubiquinone oxidoreductase (ETFQO) and electron-transfer flavoprotein (ETF) are functionally associated, and ETF accepts electrons from at least nine mitochondrial matrix flavoprotein dehydrogenases and transfers them to ubiquinone in the inner mitochondrial membrane. (plantcell.org)
  • The group of glucose-methanol-choline (GMC) flavoprotein oxidoreductases was first outlined by Cavener [ 1 ] and encompasses a wide variety of enzymes from prokaryotic and eukaryotic organisms. (mdpi.com)
  • Mutations in NADH:ubiquinone oxidoreductase of Escherichia coli affect growth on mixed amino acids. (yale.edu)
  • The NADH:quinone oxidoreductase, also called rotenone-sensitive NADH dehydrogenase (complex I) (NDH-1), is the largest complex of the respiratory chain and is responsible for the transfer of electrons from NADH to quinones, coupled with proton or sodium translocation across the membrane. (asm.org)
  • While [Fe4S4] cluster is bound by four Cys ligands, Pterin - rich in amino and ether linkages - interacts with the Asp-X-X-Gly-Leu-(Cys/Asp) sequences in the AOR enzyme. (wikipedia.org)
  • The amino acid sequences of Escherichia coli (Genbank accession no. (aacrjournals.org)
  • The predicted amino acid sequences of HKE4 and HKE6 exhibited 81.5 and 85.6% identity to the mouse homologues, Ke4 and Ke6, respectively. (tcdb.org)
  • DOPA decarboxylase inhibitor , DDCI and AAADI ) is a medication which inhibits the synthesis of dopamine by the enzyme aromatic L-amino acid decarboxylase (AADC, AAAD, or DOPA decarboxylase). (rug.nl)
  • Aromatic L -amino acid decarboxylase ( AADC or AAAD ), also known as DOPA decarboxylase ( DDC ), tryptophan decarboxylase , and 5-hydroxytryptophan decarboxylase , is a lyase enzyme ( EC 4.1.1.28 ). (wikidoc.org)
  • Mammalian thioredoxin reductase (TR) is a pyridine nucleotide disulfide oxidoreductase that uses the rare amino acid selenocysteine (Sec) in place of the more commonly used amino acid cysteine (Cys) in the redox-active tetrapeptide Gly-Cys-Sec-Gly motif to catalyze thiol/disulfide exchange reactions. (acmbcb.org)
  • Preliminary report of NAD+-dependent amino acid dehydrogenase producing bacteria isolated from soil. (biomedsearch.com)
  • RESULTS: In total of 230 tested strains, four of them were recognized as amino acid dehydrogenase producers that belong to species of Pseudomonas, Citrobacter and Proteus. (biomedsearch.com)
  • Subsequently, propionaldehyde is catabolized to propionic acid and propanol, presumably by coenzyme A (CoA)-dependent aldehyde dehydrogenase, phosphotransacylase, propionate kinase, and alcohol dehydrogenase. (asm.org)
  • Succinate:quinone oxidoreductase, or succinate dehydrogenase (complex II), is an enzyme of the tricarboxylic acid cycle, which oxidizes succinate and reduces quinones, without proton translocation. (asm.org)
  • In D-amino acid dehydrogenase superfamily, these enzymes are physiologically related to L-proline dehydrogenase from archaea and hydrogen cyanide synthase from bacteria, whereas isozyme 2 of OpnDH from B. japonicum and other OpnDHs had appeared by convergent evolution. (intechopen.com)
  • Recently, a meso-2,6-diaminopimelate dehydrogenase from Symbiobacterium thermophilum (StDAPDH) has been found to be a useful biocatalyst for the production of D-amino acids, but it requires NADP(H) as co-enzyme. (bvsalud.org)
  • A scheme for the detoxification of superoxide in Pyrococcus furiosus has been previously proposed in which superoxide reductase (SOR) reduces (rather than dismutates) superoxide to hydrogen peroxide by using electrons from reduced rubredoxin (Rd). Rd is reduced with electrons from NAD(P)H by the enzyme NAD(P)H:rubredoxin oxidoreductase (NROR). (asm.org)
  • p>This subsection of the 'Function' section describes the interaction between a single amino acid and another chemical entity. (uniprot.org)
  • Type II NAD(P)H:quinone oxidoreductases (NDH-2) catalyze the two-electron transfer from NAD(P)H to quinones, without any energy-transducing site. (asm.org)
  • Anwar A, Siegel D, Kepa JK, Ross D (2002) Interaction of the molecular chaperone Hsp70 with human NAD(P)H:quinone oxidoreductase 1. (springer.com)
  • The mammalian mitochondrial proteins, ETF and ETFQO, are essential for the catabolism of fatty acids, several amino acids, and choline and are important in supplying mitochondria with respiratory substrates auxiliary to those derived from sucrose. (plantcell.org)
  • Described herein are multimeric oxidoreductase complexes which function in the enzymatic conversion of a carbon substrate. (freepatentsonline.com)
  • 9. The enzymatic material of claim 1 which also contains, per gram of material, from about 0.03 to about 1.2 millimoles of substrate specific to oxidoreductase enzyme in said material for producing hydrogen peroxide upon contact of said material with serum. (google.com)
  • Among 21 amino acids tested for substrate specificity, L-glutamate was almost exclusively oxidized. (bvsalud.org)
  • The systematic name of this enzyme class is aldehyde:ferredoxin oxidoreductase. (wikipedia.org)
  • Aldehyde Ferredoxin Oxidoreductase is a member of an AOR family, which includes glyceraldehyde-3-phosphate ferredoxin oxidoreductase (GAPOR) and Formaldehyde Ferredoxin Oxidoreductase. (wikipedia.org)
  • The main substrates for aldehyde ferredoxin oxidoreductase are acetaldehyde, phenylacetaldehyde, and isovalerdehyde, which is a metabolic product from common amino acids and glucose. (wikipedia.org)
  • thus, they utilize aldehyde ferredoxin oxidoreductase to metabolize the amino acid carbon source. (wikipedia.org)
  • oxygen oxidoreductase, an aa 3 -type enzyme (complex IV), receives these electrons and transfers them to oxygen. (asm.org)
  • L-amino acid: oxygen oxidoreductase (deaminating), which operates as shown in the following reaction: ##STR1## It has hitherto been known that this enzyme is found insnake venum, the kidneys of rats and mice, the livers of birds, invertebrate animals and Neurospora crassa [Arch. (patentgenius.com)
  • In addition, the mammalian ETF/ETFQO system plays a key role in β-oxidation of fatty acids and catabolism of amino acids and choline. (plantcell.org)
  • It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. (phosphosite.org)
  • The cellular repressor of E1A-stimulated genes (CREG) is a 220 amino acid glycoprotein structurally similar to oxidoreductases. (frontiersin.org)
  • These supported the predicted pathway, identified induced fatty-acid oxidation genes, and identified an apparent shift in the TCA cycle to a putative ATP-yielding succinyl-CoA synthase. (pubmedcentralcanada.ca)
  • The de novo synthesis of BCAAs has been an historical object of attention for two main reasons: this pathway is a known target for at least five independent classes of inhibitory herbicides [ 2 ] and, secondly, animals lack the necessary genes encoding enzymes for BCAA synthesis thus requiring that this class of essential amino acids be obtained via dietary intake. (biomedcentral.com)
  • EC 1.4.1.X) are members of the wider superfamily of oxidoreductases that catalyze the reversible oxidative deamination of an amino acid to its keto acid and ammonia with the concomitant reduction of either NAD+, NADP+ or FAD. (biomedsearch.com)
  • AOR has been proposed to be the primary enzyme responsible for oxidising the aldehydes that are produced by the 2-keto acid oxidoreductases. (wikipedia.org)
  • 5 ) presented evidence that ethylene is synthesized via α-keto-γ-methylthiobutyric acid, as in prokaryotic systems, and not via the 1-aminocyclopropane-1-carboxylic acid pathway used in higher plants. (asm.org)
  • DsbA consists of 208 amino acids containing signal peptide(1-19 amino acids). (acris-antibodies.com)
  • Imipramine functionalized compounds are provided for conjugation to antigenic compounds, particularly poly(amino acids), and enzymes. (google.com)
  • G. metallireducens appears to convert aromatic compounds to benzoyl-CoA, then to acetyl-CoA via fatty acid oxidation, and then to carbon dioxide via the TCA cycle. (pubmedcentralcanada.ca)
  • Oxidoreductases catalyze the reversible electron-transfer from many compounds such as amino acids, alcohols, sugars, and amines, and are classified into three main groups, based on available electron acceptor(s): oxidases, oxygenases and dehydrogenases/reductases. (intechopen.com)
  • 2 ) showed that ABA appears to negatively modulate the salicylic acid-dependent defense pathway in tomato plants during infection with B. cinerea . (asm.org)
  • donor, hydrogen peroxide oxidoreductase) are heme-containing enzymes of approximately 300 amino acids. (plantphysiol.org)
  • Enzymatic absorbent materials such as bandages and pads, for body contact applications, contain serum-activated oxidoreductase enzyme for producing hydrogen peroxide upon contact of the enzymatic materials with serum. (google.com)
  • 1. An enzymatic substantially organic absorbent material for body contact application containing, per gram of material, from about 1.0 to about 1,000 International Units of serum-activated oxidoreductase enzyme for producing hydrogen peroxide upon contact of said material with serum. (google.com)
  • Carbon fixation on both chimneys seems to have been primarily mediated through the reverse tricarboxylic acid cycle and fueled by sulfur-oxidation, while the abundant metabolic potential for hydrogen oxidation and carbon fixation via the Calvin-Benson-Bassham cycle was hardly utilized. (microbial-ecology.net)
  • Reduced activity of cytochrome P450 oxidoreductase can also disrupt the production of cholesterol, which likely impairs normal bone formation in severe cases of cytochrome P450 oxidoreductase deficiency. (medlineplus.gov)
  • Although selenoproteins represent diverse molecular pathways and biological functions, all these proteins contain at least one selenocysteine (Sec), a selenium-containing amino acid, and most serve oxidoreductase functions. (nih.gov)
  • Membranes are of fundamental importance for the interaction of I. hospitalis and N. equitans , as they harbour the proteins necessary for the transport of macromolecules like lipids, amino acids, and cofactors between these organisms. (springer.com)
  • Mutant P450 oxidoreductase causes disordered steroidogenesis with and without Antley-Bixler syndrome. (medlineplus.gov)
  • accumulation of homocitric, homoaconitic, and homoisocitric acids in a leaky mutant. (springer.com)
  • Inversely, the reciprocal rabbit A1081V mutant lost the activity entirely: amino acid 1081 of rabbit AOX1 corresponding to amino acid 1085 of monkey AOX1. (aspetjournals.org)
  • Analysis of free amino acid pools in the mutant backgrounds revealed that they differ in the absolute amount of individual BCAAs accumulated and exhibit elevated levels of BCAAs in leaf tissues. (biomedcentral.com)
  • The single open reading frame of 2034 nucleotides spanning these cDNAs codes for a 678 amino acid polypeptide with a molecular weight of 76,962. (pnas.org)
  • Anti-P450 (cytochrome) oxidoreductase antibodies are readily available from several suppliers. (biocompare.com)
  • Your search returned 316 P450 (cytochrome) oxidoreductase Antibodies across 36 suppliers. (biocompare.com)
  • This study was aimed to isolation and screening of novel amino acid dehydrogenases from soil bacteria. (biomedsearch.com)
  • Enzymes involved in bacterial fatty-acid synthesis represent viable drug targets for Gram-negative pathogens, and historical precedent exists for targeting them in the treatment of diseases of the oral cavity. (medworm.com)
  • Synthesis of L-Ascorbic Acid", Advances in Carbohydrate Chemistry and Biochemistry 37: 79-155, 1980. (freepatentsonline.com)
  • Resin for peptide synthesis (2-chlorotritylchloride) was from Novabiochem (San Diego CA). Fmoc amino acids were from Synbiosci Corp. (Livermore CA) except for Fmoc-homocysteine which was from Bachem (King of Prussia PA). (acmbcb.org)
  • Peptide Plerixafor 8HCl Synthesis All peptides in this study were synthesized on 2-chlorotritylchloride resin using standard Fmoc chemistry as previously detailed.19 25 36 Peptides were cleaved from the resin using trifluoroacetic acid (TFA) containing triisopropylsilane and water in a 96:2:2 ratio. (acmbcb.org)
  • Amino Acid Motifs" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (umassmed.edu)
  • Cherepanova NA, Shrimal S, Gilmore R. Oxidoreductase activity is necessary for N-glycosylation of cysteine-proximal acceptor sites in glycoproteins. (umassmed.edu)
  • 2. The enzymatic material of claim 1 wherein the concentration of oxidoreductase enzyme is from about 10 to about 500 International Units. (google.com)
  • Therefore, we propose that the relay of an oxidizing equivalent from one ER oxidoreductase to another may play an essential role in cooperative oxidative folding by multiple ER oxidoreductases in plants. (plantphysiol.org)
  • Science: enzyme) a class of enzymes that catalyze oxidation-reduction reactions of amino acids . (biology-online.org)
  • Finally, after 24 h enzymatic conversion under the optimal conditions, the maximum titer of α-KG reached 38.1 g/L from 47 g/L L-glutamic acid. (bvsalud.org)
  • Putative oxidoreductase that is recruited on chromatin and promotes KDM1B demethylase activity. (uniprot.org)