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
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 (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 (NADH dehydrogenase (quinone)) requires NADH, is inhibited by AMP and 2,4-dinitrophenol but not by dicoumarol or folic acid derivatives. EC (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
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
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 was formerly listed as EC and EC
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
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
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 and EC
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
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
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
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 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)

... 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 ...
... 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 ...
Snake venom Oxidoreductase Oxidative deamination D-amino acid oxidase Portal: Biology (EC 1.4.3, Flavin enzymes, Enzymes of ... In enzymology, an L-amino acid oxidase (LAAO) (EC is an enzyme that catalyzes the chemical reaction an L-amino acid + ... The systematic name of this enzyme class is L-amino-acid:oxygen oxidoreductase (deaminating). This enzyme is also called ophio- ... 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 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 ...
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 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, ...
... (EC, 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 ...
... 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. - dopa decarboxylase MeSH D08.811.520.224.125.250 - ...
Oxidoreductase inhibitors, Tryptamines, Amino acids, All stub articles, Antineoplastic and immunomodulating drug stubs, ...
"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, ...
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 ...
L-methionine/branched chain amino acid transporter, D-alanine-D-alanine ligase, and hypothetical proteins. These CSIs are ... identified through genomic analyses for this family in the proteins bifunctional protein-disulfide isomerise/oxidoreductase ...
DAO D-amino-acid dehydrogenase D-amino acid oxidase D-aspartate oxidase Glycerol-3-phosphate dehydrogenase Sarcosine oxidase ... D-amino-acid dehydrogenase EC, D-aspartate oxidase EC D-amino acid oxidase EC (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 ... The Enzyme Commission (EC) number for SQR is 1.8.5.'. The number indicates that the protein is an oxidoreductase (indicated by ... Both amino acids are located in the hydrophobic region of the plasma membrane and are conserved among all sulfide: quinone ... Nübel T, Klughammer C, Huber R, Hauska G, Schütz M (April 2000). "Sulfide:quinone oxidoreductase in membranes of the ...
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) Portal: Biology (EC 1.21.3) ...
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 ...
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. "NDUFAF8 - NADH dehydrogenase [ ... 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, ...
... 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 ...
... amino acids, and lipids. Multiple dimethyl sulfoxide-molybdopterin (DMSO-MPT) oxidoreductase genes, which are implicated in the ... and casamino acids. The first of the Pyrobaculum species to be genetically sequenced, P. aerophilum (rod-shaped, 3-8 * 0.6 µm ...
IUPAC Name [2-amino-4-oxo-6,7-bis(sulfanyl)-3,5,5~{a},8,9~{a},10-hexahydropyrano[3,2-g]pteridin-8-yl]methyl dihydrogen ... Some bacterial oxidoreductases use tungsten in a similar manner as molybdenum by using it in a tungsten-pterin complex, with ... Tungsten-using enzymes typically reduce free carboxylic acids to aldehydes. The first tungsten-requiring enzyme to be ... 2-Amino-4-oxo-6,7-bis(sulfanyl)-3,5,5a,8,9a,10-hexahydropyrano[3,2-g]pteridin-8-yl]methyl dihydrogen phosphate". pubchem.ncbi. ...
... deoxymugineic acid + succinate + CO2 Mugineic-acid 3-dioxygenase contains iron(II). Mugineic acid is an amino acid excreted by ... oxygen oxidoreductase (3-hydroxylating). This enzyme catalyses the following chemical reaction (1) mugineic acid + 2- ... 3-hydroxymugineic acid, 2'-deoxymugineic acid, avenic acid, and distichonic acid. The effectiveness of mugineic acid under iron ... Mugineic-acid 3-dioxygenase (EC, IDS2) is an enzyme with systematic name mugineic acid,2-oxoglutarate: ...
Studies have shown that the particular identity of the amino-acid used to coordinate the Mo core greatly influences Mo redox ... ISBN 978-0-8247-4475-5. Portal: Biology (Oxidoreductases, EC 1.8.5). ...
It also lowers the concentration of low molecular weight molecules like sugars and amino acids and increases the concentration ... like oxidoreductases, transferases and hydrolases, which are necessary for metabolic functions and antioxidant responses. ...
The NDUFAF2 gene produces a 20 kDa protein composed of 169 amino acids. The protein is a chaperone of the complex I NDUFA12 ... NADH:ubiquinone oxidoreductase complex assembly factor 2 (NDUFAF2), also known as B17.2L or NDUFA12L is a protein that in ... NADH:ubiquinone oxidoreductase (complex I) catalyzes the transfer of electrons from NADH to ubiquinone (coenzyme Q) in the ... "UniProt: the universal protein knowledgebase". Nucleic Acids Research. 45 (D1): D158-D169. 2016-11-29. doi:10.1093/nar/gkw1099 ...
... binds to three conserved amino acids through hydrogen bonds. These amino acids include three Aspartate residues. NAD+ and NADP+ ... Oxidoreductase Myelodysplastic syndrome#IDH1 and IDH2 mutations Oncometabolism PDB: 1CW7​; Cherbavaz DB, Lee ME, Stroud RM, ... Isocitrate binds within the active site to a conserved sequence of about eight amino acids through hydrogen bonds. These acids ... Two aspartate amino acid residues (below left) are interacting with two adjacent water molecules (w6 and w8) in the Mn2+ ...
Several amino acids within the catalytic pocket have been identified as important to DLD function, including R281 and N473. ... Additionally, DLD is a flavoenzyme oxidoreductase that contains a reactive disulfide bridge and a FAD cofactor that are ... The DLD homodimer functions as the E3 component of the pyruvate, α-ketoglutarate, α-adipate and branched-chain amino acid- ... January 2008). "The role of amino acids T148 and R281 in human dihydrolipoamide dehydrogenase". Journal of Biomedical Science. ...
... longa secreted luciferase gene encodes a 24 kDa protein containing an N-terminal secretory signal peptide of 17 amino acid ... All luciferases are classified as oxidoreductases (EC 1.13.12.-), meaning they act on single donors with incorporation of ... additionally be made more sensitive for ATP detection by increasing the luminescence intensity by changing certain amino acid ... molecular oxygen oxidizes flavin mononucleotide and a long-chain aliphatic aldehyde to an aliphatic carboxylic acid. The ...
... and is thought to encode a hydrophobic protein containing 664 amino acids and to have a mass of 72.9 kDa. The ndhF fragment has ... v t e (CS1 errors: missing periodical, Harv and Sfn no-target errors, Photosynthesis, EC 4.1.1, EC 1.6.5, Oxidoreductases, ... NADPH-dependent enzymes, All stub articles, Oxidoreductase stubs). ...
In proteins, zinc ions are often coordinated to the amino acid side chains of aspartic acid, glutamic acid, cysteine and ... oxidoreductases, and isomerases (42,43). Bitanihirwe BK, Cunningham MG (November 2009). "Zinc: the brain's dark horse". Synapse ... of the nine or ten Zn2+ ions in a zinc finger helps maintain the finger's structure by coordinately binding to four amino acids ... The non-related β-carbonic anhydrase is required in plants for leaf formation, the synthesis of indole acetic acid (auxin) and ...
ABC-type polar-amino-acid transporter * EC ABC-type nonpolar-amino-acid transporter * EC mitochondrial ... ferredoxin-quinone oxidoreductase (H+-translocating) * EC ferredoxin-NAD+ oxidoreductase (H+-transporting) * * No ... Nucleic Acids Res. 37: D593-D597. doi:10.1093/nar/gkn582. Hydron is a generic term that includes all isotopes of H+, i.e. not ... ABC-type teichoic-acid transporter * EC ABC-type lipopolysaccharide transporter * EC ABC-type lipid A-core ...
NAD+ 3-oxidoreductase. This enzyme catalyses the following chemical reaction: UDP-N-acetyl-2-amino-2-deoxy-alpha-D-glucuronate ... 3-dideoxy-D-mannuronic acid". Biochemistry. 50 (9): 1483-91. doi:10.1021/bi101871f. PMC 3050068. PMID 21241053. UDP-N-acetyl-2- ... UDP-N-acetyl-2-amino-2-deoxyglucuronate dehydrogenase (EC, WlbA, WbpB) is an enzyme with systematic name UDP-N-acetyl ... amino-2-deoxyglucuronate+dehydrogenase at the US National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology ( ...
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). A deficiency is responsible ... Xylulose Xylitol (Note conversion of ketone to alcohol) This enzyme belongs to the superfamily of short-chain oxidoreductases, ...
Without heme, iron must be ligated to four amino acid residues (Tyr200, His226, Tyr164, His224) to maintain is catalytically ... Schomburg D, Schomburg I (2006). "Catechol 1,2-dioxygenase". Class I Oxidoreductases X. Springer Handbook of Enzymes. Vol. 25 ( ... through a series of trans influences and stabilizing hydrogen bonding between the substrate and other active site amino acid ... Sistrom WR, Stanier RY (October 1954). "The mechanism of formation of beta-ketoadipic acid by bacteria". The Journal of ...
This inner part of the pocket contains several amino acids with nonpolar side chains necessary for stabilization of the ... Cinnamoyl-CoA reductase (EC, systematically named cinnamaldehyde:NADP+ oxidoreductase (CoA-cinnamoylating) but ...
The NDUFB11 protein weighs 17 kDa and is composed of 153 amino acids. NDUFB11 is a subunit of the enzyme NADH dehydrogenase ( ... The protein encoded by this gene is an accessory subunit of the multisubunit NADH:ubiquinone oxidoreductase (complex I) that is ... This protein complex has NADH dehydrogenase activity and oxidoreductase activity. It transfers electrons from NADH to the ... "UniProt: the universal protein knowledgebase". Nucleic Acids Research. 45 (D1): D158-D169. January 2017. doi:10.1093/nar/ ...
... a non-essential amino acid in both plants and animals). It catalyzes the oxidative decarboxylation reaction of prephenate to 4- ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ ... The systematic name of this enzyme class is prephenate:NAD+ oxidoreductase (decarboxylating). Other names in common use include ... NADP+ oxidoreductase This enzyme so far has been found in sixteen different organisms; twelve different kinds of bacteria ( ...
Both the α- and β-subunits have a PCB at amino acid 84, but the β-subunit has an additional PCB at position 155 as well. This ... ferredoxin oxidoreductase. Insertion of 3Z-phycocyanobilin into the C-PC apo-protein via thioether bond formation is catalysed ... Complete amino acid sequence of the beta subunit". The Journal of Biological Chemistry. 256 (23): 12176-84. doi:10.1016/S0021- ... The (αβ) monomer consists of 332 amino acids and 3 thio-linked phycocyanobilin (PCB) cofactor molecules. ...
Genet R, Denoyelle C, Menez A (1994). "Purification and partial characterization of an amino acid alpha,beta- dehydrogenase, L- ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with oxygen as ... The systematic name of this enzyme class is L-tryptophan:oxygen alpha,beta-oxidoreductase. Other names in common use include L- ...
Transfer RNAs for all 20 amino acids and approximately 250 ribosomal RNA were all found on the same chromosome. Trichomonas has ... They do not require oxygen and instead use pyruvate:ferredoxin oxido-reductase and hydrogenase to produce ATP from pyruvate, ...
The MT-ND5 gene produces a 67 kDa protein composed of 603 amino acids. MT-ND5 is one of seven mitochondrial genes encoding ... MT-ND5 is a gene of the mitochondrial genome coding for the NADH-ubiquinone oxidoreductase chain 5 protein (ND5). The ND5 ... "NADH-ubiquinone oxidoreductase chain 5". Cardiac Organellar Protein Atlas Knowledgebase (COPaKB). "MT-ND5 - NADH-ubiquinone ... oxidoreductase chain 5 - Homo sapiens (Human)". UniProt.org: a hub for protein information. The UniProt Consortium. Alston CL, ...
nov., a versatile amino acid-degrading anaerobe producing or utilizing H2 or formate". Archives of Microbiology. 150 (3): 254- ... "Tungsten-containing aldehyde oxidoreductase of Eubacterium acidaminophilum". European Journal of Biochemistry. 271 (1): 212-219 ... notable for being an amino acid-degrading obligate anaerobe producing or utilizing H2 or formate. It is rod-shaped and motile ... "Phylogenetic relationships of three amino-acid-utilizing anaerobes, Selenomonas acidaminovorans, 'Selenomonas acidaminophila' ...
The NDUFS3 gene encodes a protein subunit consisting of 263 amino acids. This protein is synthesized in the cytoplasm and then ... This gene encodes one of the iron-sulfur protein (IP) components of complex I. The 45-subunit NADH:ubiquinone oxidoreductase ( ... This gene encodes one of the iron-sulfur protein (IP) components of mitochondrial NADH:ubiquinone oxidoreductase (complex I). ... an essential role of mitochondrial complex I in the interferon-beta and retinoic acid-induced cancer cell death". Cell Death ...
These small oxidoreductases are involved in flower development, salicylic acid, and plant defence signalling. Systemic ... and 2-amino-3-hydroxy-5-methyl-4-isoxazolepropionate (AMPA) receptors". Neurochemical Research. 22 (9): 1165-1171. doi:10.1023/ ... Glyoxalase II (EC catalyzes the hydrolysis of S-D-lactoylglutathione to glutathione and D-lactic acid. It maintains ... Reductive stress Glutathione synthetase deficiency Ophthalmic acid roGFP, a tool to measure the cellular glutathione redox ...
The MT-ND3 gene produces a 13 kDa protein composed of 115 amino acids. MT-ND3 is one of seven mitochondrial genes encoding ... "NADH-ubiquinone oxidoreductase chain 3". Cardiac Organellar Protein Atlas Knowledgebase (COPaKB). "Complete mitochondrial ... "MT-ND3 - NADH-ubiquinone oxidoreductase chain 3 - Homo sapiens (Human)". UniProt.org: a hub for protein information. The ...
The amino-terminal part contains a putative beta sheet rich in hydrophobic amino acids that may serve as mitochondrial import ... ubiquinone oxidoreductase: human complex I cDNA characterization completed". Biochemical and Biophysical Research ... The gene produces a 15 kDa protein composed of 141 amino acids. NDUFA11 is a subunit of the enzyme NADH dehydrogenase ( ... "Identification and primary structure of five human NADH-ubiquinone oxidoreductase subunits". Biochemical and Biophysical ...
... is most available to the body when chelated to amino acids and is also available for use as a common iron supplement. ... Boon EM, Downs A, Marcey D. "Proposed Mechanism of Catalase". Catalase: H2O2: H2O2 Oxidoreductase: Catalase Structural Tutorial ... Glycine, the least expensive amino acid, is most often used to produce iron glycinate supplements. The U.S. Institute of ... However, it does not react with concentrated nitric acid and other oxidizing acids due to the formation of an impervious oxide ...
... is an enzyme that is very important in the biosynthesis of amino acids in prokaryotes, fungi, and some higher plants. It forms ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of a donor with ... an enzyme involved in the biosynthesis of various amino acids from aspartate. It also contains the yeast and fungal Arg5,6 ... a key enzyme in the aspartate family of amino acid biosynthesis". J Mol Biol. 289 (4): 991-1002. doi:10.1006/jmbi.1999.2828. ...
It was also found that more polar amino acids and smaller amino acids were more likely to be barophilic. Through the comparison ... An oxidoreductase species in P. furiosus that does not contain tungsten is pyruvate ferredoxin oxidoreductase, or POR, which ... Growth is very slow, or nonexistent, on amino acids, organic acids, alcohols, and most carbohydrates (including glucose, ... It was found that most of the amino acids that determined barophilicity were also found to be important in the organization of ...
The POR gene provides instructions for making the enzyme cytochrome P450 oxidoreductase. Learn about this gene and related ... Most of the mutations that cause cytochrome P450 oxidoreductase deficiency change single protein building blocks (amino acids) ... The breakdown of retinoic acid requires cytochrome P450 oxidoreductase; if a shortage of cytochrome P450 oxidoreductase ... Cytochrome P450 oxidoreductase deficiency. More than 50 mutations in the POR gene have been found to cause cytochrome P450 ...
L-Amino acid oxidase Synonymes. Apoxine I Apoxine-I L-Amino acid-oxygen oxidoreductase (deaminating) Ophio-amino-acid oxidase ... L-Amino acid-oxygen oxidoreductase (deaminating). Ophio-amino-acid oxidase. Oxygène oxydoréductase des acides aminés de forme L ... An enzyme that catalyzes the oxidative deamination of L-amino acids to KETO ACIDS with the generation of AMMONIA and HYDROGEN ... L-Amino acid oxidase - Concept préféré Concept UI. M0072365. Terme préféré. ...
Oxidoreductases [D08.811.682] * Oxidoreductases Acting on CH-NH2 Group Donors [D08.811.682.664] * Amino Acid Oxidoreductases [ ...
Protein sequence analysis showed that the four 3α-oxidoreductases have identical catalytic amino acid residues. Mass ... An ancestral form of MAGE-A11 in the more distantly related lemur has significant amino acid sequence identity with human MAGE- ... MAGE-A11 in OWM and apes has nearly identical 5 coding exon amino acid sequence and conserved interaction sites for p300 ... NWM MAGE-A11 has greater amino acid sequence identity than lemur to human MAGE-A11, but inframe premature stop codons suggest ...
... aromatic amino acids, and other derivatives), alkanes (short and long chain), and abiotic enantiomers (D-amino acids and L- ... most of which serve oxidoreductase functions [70]. Biosynthesis of Sec is not a common trait of prokaryotes [71]. Considering ... A similar abundance of selA, selB, and selU genes encoding the synthesis of selenium-containing amino acids was observed in ... 5A, Additional file 1: Results, Additional file 3: Table S2). Notably, for D-amino acid (D-AA) metabolism, the catabolic ...
Oxidoreductases Acting on Sulfur Group Donors. D12 - Amino Acids, Peptides, and Proteins. Chimeric Proteins. Recombinant Fusion ... Amino Acid Neurotransmitters. Neurotransmitter Agents. Anti-Inflammatory Agents, Antirheumatic Agents, and Inflammation ... Oxidoreductases Acting on Sulfur Group Donors. Sulfite Reductases. ... Indoleacetic Acids. D08 - Enzymes and Coenzymes. Sulfite Oxidases. ...
Blood-Brain Barrier, Animals, Humans, Mice, Malaria, Cerebral, Disease Models, Animal, Amino Acid Oxidoreductases, Tumor ...
00470 D-Amino acid metabolism. K19744 dauB; L-arginine dehydrogenase. Enzymes [BR:ko01000]. 1. Oxidoreductases. 1.4 Acting on ...
Cluster 1 1140-1195 amino acids (not heteromeric) # UniProt::I7EJ57 Indolepyruvate oxidoreductase # reanno::BFirm:BPHYT_RS02015 ... 859 phenylpyruvate ferredoxin oxidoreductase (EC Marinobacter adhaerens HP15 Cluster1 Indolepyruvate oxidoreductase ... BPHYT_RS02015 phenylpyruvate ferredoxin oxidoreductase (EC Burkholderia phytofirmans PsJN # reanno::Marino:GFF880 HP15 ...
copper; copper metabolism, etc ; Schizosaccharomyces pombe; amino acid sequences; iron; ligands; microbiology; oxidoreductases ... tetracarboxylic acid, 1,3,5-benzenetricarboxylic acid, and terephthalic acid. The ML-Cu₂O@ .... DOI:. 10.1016/j.foodchem. ... 6. Graphene shell-encapsulated copper-based nanoparticles (G@Cu-NPs) effectively activate peracetic acid for elimination of ... copper, etc ; electron paramagnetic resonance spectroscopy; electron transfer; graphene; humic acids; nanoparticles; peracetic ...
... oxidoreductase activity, fatty acid and amino acid metabolism, were identified from iTRAQ. Four potential biomarkers for ... "acid-base-acid" Ceδ+-Rhδ--Ceδ+ site is proposed to strongly adsorb two NO molecules as well as the N2O intermediate that is ... Moreover, they contained functional groups with good hydrophilic properties, such as amino and hydroxyl groups, and elemental O ...
Acetylcholine, Amino Acid Oxidoreductases, Animals, Arginine, Calcimycin, Endothelium, Vascular, In Vitro Techniques, ...
"A Nutrient made up of amino acids joined by peptide bonds.") (subclass Enzyme Protein) (documentation Enzyme "A complex &% ... There are six main types of enzymes: oxidoreductases, transferases, hydrolases, lyases, isomerases, and ligases.") (subclass ... Included here are &%Substances such as saliva, dental enamel, sweat, and gastric acid.") (subclass Hormone BodySubstance) ( ... Organism consisting of a core of a single nucleic acid enclosed in a protective coat of protein. A virus may replicate only ...
Glycine/D-amino acid oxi... 42 0.043 gi,16263471,ref,NP_436264.1, Putative oxidoreductase [Sinorhizob... 42 0.056 gi,23502768, ... Glycine/D-amino acid oxi... 40 0.21 gi,28828736,gb,AAO51331.1, similar to Cavia porcellus (Guinea pi... 40 0.21 gi,18401311,ref ... Glycine/D-amino acid oxi... 40 0.21 gi,15802111,ref,NP_288133.1, flavoprotein; probably electron tra... 40 0.21 gi,30794320,ref ... Glycine/D-amino acid oxi... 40 0.21 gi,27376008,ref,NP_767537.1, bll0897 [Bradyrhizobium japonicum U... 40 0.21 gi,15234887,ref ...
... protein amino acid N-linked glycosylation via asparagine;0.0017454452860597!GO:0016679;oxidoreductase activity, acting on ... acid-amino acid ligase activity;4.32842461928683e-09!GO:0065004;protein-DNA complex assembly;4.50689221248338e-09!GO:0046930; ... sulfur amino acid metabolic process;0.0425275092940853!GO:0030330;DNA damage response, signal transduction by p53 class ... amino acid activation;2.24538098208788e-09!GO:0006418;tRNA aminoacylation for protein translation;2.24538098208788e-09!GO: ...
... quinone oxidoreductase (FaQR). The open reading frame of the FaQR cDNA consists of 969 bp encoding a 322-amino acid protein ... This study demonstrates the function of the FaQR enzyme in the biosynthesis of HDMF as enone oxidoreductase and provides a ... encodes an enone oxidoreductase. Raab, T., López-Ráez, J.A., Klein, D., Caballero, J.L., Moyano, E., Schwab, W., Muñoz-Blanco, ... oxidoreductase.. The flavor of strawberry (Fragaria x ananassa) fruit is dominated by an uncommon group of aroma compounds with ...
Metabolism Amino acid biosynthesis Glutamate family glutamate synthase (NADPH), homotetrameric (TIGR01316; EC; HMM- ... FAD dependent oxidoreductase TIGR03364 (TIGR03364; HMM-score: 19.1) mycofactocin system FadH/OYE family oxidoreductase 1 ( ... Metabolism Energy metabolism Amino acids and amines sarcosine oxidase, alpha subunit family (TIGR01372; HMM-score: 20.2) ... Metabolism Energy metabolism Amino acids and amines alanine dehydrogenase (TIGR00518; EC; HMM-score: 25) ...
Amino Acid Sequence / Ion Transport / Membrane Protein / Plasmid / Mercury compounds / Molecular Sequence Data / Gram Positive ... Oxidoreductases / Bacteria / Nitrate Reductase / Gene / Enzyme / Gen / Gram-negative bacteria / Chromosome / Ecosystem / Toxic ... Amino Acid Sequence / Ion Transport / Membrane Protein / Plasmid / Mercury compounds / Molecular Sequence Data. ... Evolutionary Biology / Microbiology / Medical Microbiology / Taxonomy / Phylogeny / Korea / Nucleic acid hybridization / ...
Oxidoreductases, N-Demethylating [D08.811.682.662.582]. *Sarcosine Oxidase [D08.811.682.662.582.700]. *Amino Acids, Peptides, ... Oxidoreductases Acting on CH-NH Group Donors [D08.811.682.662]. * ... Oxidase, L-Pipecolic Acid. *Sarcosine-Oxygen Oxidoreductase ( ...
The nucleotide polymorphisms found within the dsb gene did not change the predicted amino acid sequence in relation to E. ... Identification and functional analysis of an immunoreactive DsbA-like thio-disulfide oxidoreductase of Ehrlichia spp. Infect ... chaffeensis disulfide oxidoreductase gene (dsb) sequences in GenBank (CP000236) (24). A single sample from A. cajennense ticks ...
2S)-2-amino-5-(N,N-dimethylcarbamimidamido)pentanoic acid IUPAC (S)-2-amino-5-(N,N-dimethylguanidino)pentanoic acid ChEBI ... An EC 1.14.13.* (oxidoreductase acting on paired donors, incorporating 1 atom of oxygen, with NADH or NADPH as one donor) ... nsted acid).. (via organic amino compound ). Bronsted acid A molecular entity capable of donating a hydron to an acceptor (Br. ... arginine (CHEBI:25682) is a non-proteinogenic L-α-amino acid (CHEBI:83822) Nω,Nω-. dimethyl-. L-. arginine (CHEBI:25682) is ...
... amino acids, a group of amino acids, a loop region, an alpha helix, neighboring beta-sheets or even an entire domain) of these ... EC 1 Oxidoreductases: catalyze oxidation/reduction reactions. *EC 2 Transferases: transfer a functional group (e.g. a methyl or ... linear chains of amino acids that fold to produce a three-dimensional product. Each unique amino acid sequence produces a ... A mutation of a single amino acid in the enzyme phenylalanine hydroxylase, which catalyzes the first step in the degradation of ...
A flavoprotein oxidoreductase that has specificity for long-chain fatty acids. It forms a complex with ELECTRON-TRANSFERRING ... Amino Acids, Peptides, and Proteins [D12]. *Proteins [D12.776]. *Flavoproteins [D12.776.331]. *Acyl-CoA Dehydrogenase, Long- ...
Both transcripts and metabolites enriched in H2-treated rats revealed alteration of amino acid metabolism pathways and ... H2 influences liver metabolism of lipids, carbohydrates, amino acids, and nucleic acids. We recently found that H2-treated rats ... 3D). However, the expression level of genes that encode cytochrome P450 oxidoreductases such as Cyp26b1, Cyp26a1, which lead to ... amino acids, and carboxylic acids (Fig. 3B, C), the main alteration that we observed (Figs. 1, 2) during the H2 intervention. ...
Oxidoreductases 100% * Hydrogen 76% * Enzymes 75% * Cytochrome P450 35% * Amino acids 31% ...
The biosynthesis of amino acids in plants. Amino acid biosynthesis inhibitors. British Crop Protection Monograph 42 . pp. 3-13 ... Purification and characterisation of an acyclic monoterpene primary alcohol: NADP+ oxidoreductase from catmint (Nepeta racemosa ... The biosynthesis of amino acids and amino acid-derived secondary metabolites in crop plants. Abstracts AFRC-DLO Workshop on ... The biosynthesis of amino acids and amino acid-derived secondary metabolites in crop plants. C2 - Non-edited contributions to ...
fatty acid synthase activity. 1.23679054027553. bayes_pls_golite062009. *oxidoreductase activity, acting on NADH or NADPH, ... 388 amino acids. Gene Ontology:. Cellular Component:. cytoplasm [IEA. ] Biological Process:. estrogen biosynthetic process [IEA ... fatty acid biosynthetic process [IEA. ] Molecular Function:. estradiol 17-beta-dehydrogenase activity [IEA. ] 3-oxoacyl-[acyl- ... oxidoreductase activity [IEA. ] NAD or NADH binding [IEA. ] 3-hydroxybutyrate dehydrogenase activity [IEA. ] 2-deoxy-D- ...
Amino acid. Brian R. Crane mainly focuses on Biophysics, Flavin group, Flagellum, Timeless and Circadian clock. Brian R. Crane ... In his research on the topic of Nitric oxide synthase, Oxidoreductase is strongly related with Peptide sequence. His Heme study ... Amino acid. His primary areas of study are Biochemistry, Stereochemistry, Nitric oxide, Nitric oxide synthase and Heme. His ... His Stereochemistry study combines topics in areas such as Oxidoreductase, Protein subunit, Active site, Dimer and Electron ...
  • oxidoreductase acting on paired donors, incorporating 1 atom of oxygen, with NADH or NADPH as one donor) inhibitor that interferes with the action of nitric oxide synthase (EC (ebi.ac.uk)
  • The POR gene provides instructions for making the enzyme cytochrome P450 oxidoreductase. (medlineplus.gov)
  • 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)
  • More than 50 mutations in the POR gene have been found to cause cytochrome P450 oxidoreductase deficiency. (medlineplus.gov)
  • Most of the mutations that cause cytochrome P450 oxidoreductase deficiency change single protein building blocks (amino acids) in cytochrome P450 oxidoreductase. (medlineplus.gov)
  • 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)
  • if a shortage of cytochrome P450 oxidoreductase prevents retinoic acid from being broken down, the resulting excess of that molecule can stimulate the abnormal growth and fusion of bones. (medlineplus.gov)
  • P450 oxidoreductase: genetic polymorphisms and implications for drug metabolism and toxicity. (medlineplus.gov)
  • Results: Two hundred and sixty-three DEPs, including proteins with multiple bioactivities, such as protein translation, mitochondrial function, oxidoreductase activity, fatty acid and amino acid metabolism, were identified from iTRAQ. (bvsalud.org)
  • Both transcripts and metabolites enriched in H 2 -treated rats revealed alteration of amino acid metabolism pathways and activation of purine nucleotides and carbohydrate biosynthesis pathways. (nature.com)
  • This expression included carbohydrate metabolism, amino acid synthesis, and response to stress-related proteins. (ophrp.org)
  • An enzyme that catalyzes the oxidative deamination of L-amino acids to KETO ACIDS with the generation of AMMONIA and HYDROGEN PEROXIDE. (bvsalud.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. (wikigenes.org)
  • L-amino acid oxidase is widely distributed in and is thought to contribute to the toxicity of SNAKE VENOMS. (bvsalud.org)
  • In his research on the topic of Nitric oxide synthase, Oxidoreductase is strongly related with Peptide sequence. (research.com)
  • His Stereochemistry study combines topics in areas such as Oxidoreductase, Protein subunit, Active site, Dimer and Electron transfer. (research.com)
  • Genetics of P450 oxidoreductase: sequence variation in 842 individuals of four ethnicities and activities of 15 missense mutations. (medlineplus.gov)
  • A flavoprotein containing oxidoreductase that catalyzes the dehydrogenation of SUCCINATE to fumarate. (bvsalud.org)
  • A molecular entity capable of accepting a hydron from a donor (Br o nsted acid). (ebi.ac.uk)
  • 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)
  • A class of enzymes that catalyze oxidation-reduction reactions of amino acids. (nih.gov)
  • The latter two are key enzymes in biogenic amine biosynthesis (ie, aromatic amino acid synthesis). (medscape.com)
  • [ 17 ] Schiff-base aldehyde adducts with other amino-containing molecules, including key membrane enzymes and proteins, may also be detrimental to their function. (medscape.com)
  • In addition to hydroxylating aromatic amino acids, BH4 serves as the cofactor for nitric oxide synthase and glyceryl-ether mono-oxygenase. (medscape.com)
  • In cases of such stress, it was observed that BH4 itself, sepiapterin, folic acid, resveratrol, and a small-molecular-weight compound AVE3085 have the ability to recouple endothelial nitric oxide synthase (eNOS) and improve endothelial function. (medscape.com)
  • More than 50 mutations in the POR gene have been found to cause cytochrome P450 oxidoreductase deficiency. (medlineplus.gov)
  • This gene encodes a protein with limited similarity to L-amino acid oxidase which contains the conserved amino acids thought to be involved in catalysis and binding of flavin adenine dinucleotide (FAD) cofactor. (nih.gov)
  • Studies suggest that a molecule called retinoic acid also plays a role in the skeletal abnormalities found in severe cases. (medlineplus.gov)
  • 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)
  • Lysosomal L-amino-acid oxidase with highest specific activity with phenylalanine. (nih.gov)

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