Lyases
Chondroitin Lyases
Enzymes which catalyze the elimination of delta-4,5-D-glucuronate residues from polysaccharides containing 1,4-beta-hexosaminyl and 1,3-beta-D-glucuronosyl or 1,3-alpha-L-iduronosyl linkages thereby bringing about depolymerization. EC 4.2.2.4 acts on chondroitin sulfate A and C as well as on dermatan sulfate and slowly on hyaluronate. EC 4.2.2.5 acts on chondroitin sulfate A and C.
Pectobacterium chrysanthemi
Chondroitinases and Chondroitin Lyases
Pectins
High molecular weight polysaccharides present in the cell walls of all plants. Pectins cement cell walls together. They are used as emulsifiers and stabilizers in the food industry. They have been tried for a variety of therapeutic uses including as antidiarrheals, where they are now generally considered ineffective, and in the treatment of hypercholesterolemia.
Molecular Sequence Data
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.
Amino Acid Sequence
Chicory
Aldehyde-Lyases
Carbon-Oxygen Lyases
Erwinia
Heparin Lyase
An enzyme of the isomerase class that catalyzes the eliminative cleavage of polysaccharides containing 1,4-linked D-glucuronate or L-iduronate residues and 1,4-alpha-linked 2-sulfoamino-2-deoxy-6-sulfo-D-glucose residues to give oligosaccharides with terminal 4-deoxy-alpha-D-gluc-4-enuronosyl groups at their non-reducing ends. (From Enzyme Nomenclature, 1992) EC 4.2.2.7.
Oxo-Acid-Lyases
Cloning, Molecular
Polygalacturonase
Substrate Specificity
Base Sequence
Alginates
Sequence Homology, Amino Acid
Hexuronic Acids
Isocitrate Lyase
Rhodophyta
Plants of the division Rhodophyta, commonly known as red algae, in which the red pigment (PHYCOERYTHRIN) predominates. However, if this pigment is destroyed, the algae can appear purple, brown, green, or yellow. Two important substances found in the cell walls of red algae are AGAR and CARRAGEENAN. Some rhodophyta are notable SEAWEED (macroalgae).
Phycobilins
Chondroitin ABC Lyase
Sphingomonas
Cytochromes c1
Sequence Alignment
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.
Escherichia coli
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.
Binding Sites
Bacteroides
Flavobacterium
Adenylosuccinate Lyase
Streptococcus anginosus
Glucuronic Acid
Hevea
Hydrogen-Ion Concentration
Mutation
Glycosaminoglycans
Proteus vulgaris
Uronic Acids
Electrophoresis, Polyacrylamide Gel
Chondroitin Sulfates
Derivatives of chondroitin which have a sulfate moiety esterified to the galactosamine moiety of chondroitin. Chondroitin sulfate A, or chondroitin 4-sulfate, and chondroitin sulfate C, or chondroitin 6-sulfate, have the sulfate esterified in the 4- and 6-positions, respectively. Chondroitin sulfate B (beta heparin; DERMATAN SULFATE) is a misnomer and this compound is not a true chondroitin sulfate.
Protein Conformation
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).
Protein Structure, Tertiary
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.
Mutagenesis, Site-Directed
Sulfonium Compounds
Protein Binding
Dermatan Sulfate
Models, Molecular
Carbohydrate Sequence
Carbon-Nitrogen Lyases
Carbon-Carbon Lyases
Sequence Analysis, DNA
DNA-(Apurinic or Apyrimidinic Site) Lyase
A DNA repair enzyme that catalyses the excision of ribose residues at apurinic and apyrimidinic DNA sites that can result from the action of DNA GLYCOSYLASES. The enzyme catalyzes a beta-elimination reaction in which the C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate. This enzyme was previously listed under EC 3.1.25.2.
Crystallography, X-Ray
Recombinant Fusion Proteins
Pseudomonas
Structure-Activity Relationship
N-Glycosyl Hydrolases
Catalysis
Chromatography, Gel
Fungi
A kingdom of eukaryotic, heterotrophic organisms that live parasitically as saprobes, including MUSHROOMS; YEASTS; smuts, molds, etc. They reproduce either sexually or asexually, and have life cycles that range from simple to complex. Filamentous fungi, commonly known as molds, refer to those that grow as multicellular colonies.
Isoenzymes
Plants
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.
DNA Glycosylases
A family of DNA repair enzymes that recognize damaged nucleotide bases and remove them by hydrolyzing the N-glycosidic bond that attaches them to the sugar backbone of the DNA molecule. The process called BASE EXCISION REPAIR can be completed by a DNA-(APURINIC OR APYRIMIDINIC SITE) LYASE which excises the remaining RIBOSE sugar from the DNA.
Bacillus
Protein Structure, Secondary
Intramolecular Lyases
Heparitin Sulfate
Biocatalysis
Catalytic Domain
Chromatography, High Pressure Liquid
Temperature
Oligosaccharides
Gene Expression Regulation, Bacterial
Peptide Fragments
Multigene Family
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)
Sequence Homology, Nucleic Acid
Chromatography
Techniques used to separate mixtures of substances based on differences in the relative affinities of the substances for mobile and stationary phases. A mobile phase (fluid or gas) passes through a column containing a stationary phase of porous solid or liquid coated on a solid support. Usage is both analytical for small amounts and preparative for bulk amounts.
Enzyme Stability
Cell Wall
Transfection
Naphthols
Phosphorus-Oxygen Lyases
Conserved Sequence
Plasmids
DNA-Binding Proteins
Chromatography, Ion Exchange
Protein Sorting Signals
Protein Processing, Post-Translational
Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility.
DNA
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).
Precipitin Tests
Carrier Proteins
Nuclear Proteins
Crystallization
Viral Envelope Proteins
Layers of protein which surround the capsid in animal viruses with tubular nucleocapsids. The envelope consists of an inner layer of lipids and virus specified proteins also called membrane or matrix proteins. The outer layer consists of one or more types of morphological subunits called peplomers which project from the viral envelope; this layer always consists of glycoproteins.
Membrane Proteins
Peptides
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.
Saccharomyces cerevisiae
Ficain
Transcription, Genetic
Viral Matrix Proteins
Nucleocapsid Proteins
Phosphorylation
Mutagenesis
Restriction Mapping
Endopeptidases
Cell Compartmentation
Carbon-Sulfur Lyases
HeLa Cells
Transcription Factors
COS Cells
CELL LINES derived from the CV-1 cell line by transformation with a replication origin defective mutant of SV40 VIRUS, which codes for wild type large T antigen (ANTIGENS, POLYOMAVIRUS TRANSFORMING). They are used for transfection and cloning. (The CV-1 cell line was derived from the kidney of an adult male African green monkey (CERCOPITHECUS AETHIOPS).)
Cytoplasm
DNA Repair
The reconstruction of a continuous two-stranded DNA molecule without mismatch from a molecule which contained damaged regions. The major repair mechanisms are excision repair, in which defective regions in one strand are excised and resynthesized using the complementary base pairing information in the intact strand; photoreactivation repair, in which the lethal and mutagenic effects of ultraviolet light are eliminated; and post-replication repair, in which the primary lesions are not repaired, but the gaps in one daughter duplex are filled in by incorporation of portions of the other (undamaged) daughter duplex. Excision repair and post-replication repair are sometimes referred to as "dark repair" because they do not require light.
Saccharomyces cerevisiae Proteins
RNA, Messenger
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.
Fluorescent Antibody Technique
Test for tissue antigen using either a direct method, by conjugation of antibody with fluorescent dye (FLUORESCENT ANTIBODY TECHNIQUE, DIRECT) or an indirect method, by formation of antigen-antibody complex which is then labeled with fluorescein-conjugated anti-immunoglobulin antibody (FLUORESCENT ANTIBODY TECHNIQUE, INDIRECT). The tissue is then examined by fluorescence microscopy.
Bluetongue virus
Peptide Mapping
Analysis of PEPTIDES that are generated from the digestion or fragmentation of a protein or mixture of PROTEINS, by ELECTROPHORESIS; CHROMATOGRAPHY; or MASS SPECTROMETRY. The resulting peptide fingerprints are analyzed for a variety of purposes including the identification of the proteins in a sample, GENETIC POLYMORPHISMS, patterns of gene expression, and patterns diagnostic for diseases.
Point Mutation
Virion
Cell Membrane
Repetitive Sequences, Nucleic Acid
Sequences of DNA or RNA that occur in multiple copies. There are several types: INTERSPERSED REPETITIVE SEQUENCES are copies of transposable elements (DNA TRANSPOSABLE ELEMENTS or RETROELEMENTS) dispersed throughout the genome. TERMINAL REPEAT SEQUENCES flank both ends of another sequence, for example, the long terminal repeats (LTRs) on RETROVIRUSES. Variations may be direct repeats, those occurring in the same direction, or inverted repeats, those opposite to each other in direction. TANDEM REPEAT SEQUENCES are copies which lie adjacent to each other, direct or inverted (INVERTED REPEAT SEQUENCES).
Genetic Complementation Test
Cricetinae
Gene Expression
Inclusion Bodies, Viral
An area showing altered staining behavior in the nucleus or cytoplasm of a virus-infected cell. Some inclusion bodies represent "virus factories" in which viral nucleic acid or protein is being synthesized; others are merely artifacts of fixation and staining. One example, Negri bodies, are found in the cytoplasm or processes of nerve cells in animals that have died from rabies.
DNA, Complementary
Cells, Cultured
Genes
Transmissible gastroenteritis virus
Open Reading Frames
Gene Expression Regulation, Enzymologic
Antigens, Polyomavirus Transforming
Polyomavirus antigens which cause infection and cellular transformation. The large T antigen is necessary for the initiation of viral DNA synthesis, repression of transcription of the early region and is responsible in conjunction with the middle T antigen for the transformation of primary cells. Small T antigen is necessary for the completion of the productive infection cycle.
Oncogene Protein pp60(v-src)
A tyrosine-specific protein kinase encoded by the v-src oncogene of ROUS SARCOMA VIRUS. The transforming activity of pp60(v-src) depends on both the lack of a critical carboxy-terminal tyrosine phosphorylation site at position 527, and the attachment of pp60(v-src) to the plasma membrane which is accomplished by myristylation of its N-terminal glycine.
Gene Deletion
Virus Assembly
Epitope Mapping
Rabbits
Viral Structural Proteins
Viral proteins that are components of the mature assembled VIRUS PARTICLES. They may include nucleocapsid core proteins (gag proteins), enzymes packaged within the virus particle (pol proteins), and membrane components (env proteins). These do not include the proteins encoded in the VIRAL GENOME that are produced in infected cells but which are not packaged in the mature virus particle,i.e. the so called non-structural proteins (VIRAL NONSTRUCTURAL PROTEINS).
Cercopithecus aethiops
Protein Biosynthesis
Retroviridae Proteins
Blotting, Western
Rhodamines
Biological Transport
Macromolecular Substances
Amino Acid Substitution
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.
Amino Acids
Cattle
Bacterial Outer Membrane Proteins
Proteins
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.
Amino Acid Motifs
DNA Primers
Cell Nucleus
Within a eukaryotic cell, a membrane-limited body which contains chromosomes and one or more nucleoli (CELL NUCLEOLUS). The nuclear membrane consists of a double unit-type membrane which is perforated by a number of pores; the outermost membrane is continuous with the ENDOPLASMIC RETICULUM. A cell may contain more than one nucleus. (From Singleton & Sainsbury, Dictionary of Microbiology and Molecular Biology, 2d ed)
Immunoblotting
Murine hepatitis virus
Avian Sarcoma Viruses
Tyrosine
Oligodeoxyribonucleotides
Carboxylic Acids
Two-Hybrid System Techniques
Screening techniques first developed in yeast to identify genes encoding interacting proteins. Variations are used to evaluate interplay between proteins and other molecules. Two-hybrid techniques refer to analysis for protein-protein interactions, one-hybrid for DNA-protein interactions, three-hybrid interactions for RNA-protein interactions or ligand-based interactions. Reverse n-hybrid techniques refer to analysis for mutations or other small molecules that dissociate known interactions.
Glycoproteins
Protein Kinases
Alternative Splicing
A process whereby multiple RNA transcripts are generated from a single gene. Alternative splicing involves the splicing together of other possible sets of EXONS during the processing of some, but not all, transcripts of the gene. Thus a particular exon may be connected to any one of several alternative exons to form a mature RNA. The alternative forms of mature MESSENGER RNA produce PROTEIN ISOFORMS in which one part of the isoforms is common while the other parts are different.
Viral Nonstructural Proteins
Polymerase Chain Reaction
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.
A kinetic study of ribulose bisphosphate carboxylase from the photosynthetic bacterium Rhodospirillum rubrum. (1/1854)
The activation kinetics of purified Rhodospirillum rubrum ribulose bisphosphate carboxylase were analysed. The equilibrium constant for activation by CO(2) was 600 micron and that for activation by Mg2+ was 90 micron, and the second-order activation constant for the reaction of CO(2) with inactive enzyme (k+1) was 0.25 X 10(-3)min-1 . micron-1. The latter value was considerably lower than the k+1 for higher-plant enzyme (7 X 10(-3)-10 X 10(-3)min-1 . micron-1). 6-Phosphogluconate had little effect on the active enzyme, and increased the extent of activation of inactive enzyme. Ribulose bisphosphate also increased the extent of activation and did not inhibit the rate of activation. This effect might have been mediated through a reaction product, 2-phosphoglycolic acid, which also stimulated the extent of activation of the enzyme. The active enzyme had a Km (CO2) of 300 micron-CO2, a Km (ribulose bisphosphate) of 11--18 micron-ribulose bisphosphate and a Vmax. of up to 3 mumol/min per mg of protein. These data are discussed in relation to the proposed model for activation and catalysis of ribulose bisphosphate carboxylase. (+info)A general method for selection of alpha-acetolactate decarboxylase-deficient Lactococcus lactis mutants to improve diacetyl formation. (2/1854)
The enzyme acetolactate decarboxylase (Ald) plays a key role in the regulation of the alpha-acetolactate pool in both pyruvate catabolism and the biosynthesis of the branched-chain amino acids, isoleucine, leucine, and valine (ILV). This dual role of Ald, due to allosteric activation by leucine, was used as a strategy for the isolation of Ald-deficient mutants of Lactococcus lactis subsp. lactis biovar diacetylactis. Such mutants can be selected as leucine-resistant mutants in ILV- or IV-prototrophic strains. Most dairy lactococcus strains are auxotrophic for the three amino acids. Therefore, the plasmid pMC004 containing the ilv genes (encoding the enzymes involved in the biosynthesis of IV) of L. lactis NCDO2118 was constructed. Introduction of pMC004 into ILV-auxotrophic dairy strains resulted in an isoleucine-prototrophic phenotype. By plating the strains on a chemically defined medium supplemented with leucine but not valine and isoleucine, spontaneous leucine-resistant mutants were obtained. These mutants were screened by Western blotting with Ald-specific antibodies for the presence of Ald. Selected mutants lacking Ald were subsequently cured of pMC004. Except for a defect in the expression of Ald, the resulting strain, MC010, was identical to the wild-type strain, as shown by Southern blotting and DNA fingerprinting. The mutation resulting in the lack of Ald in MC010 occurred spontaneously, and the strain does not contain foreign DNA; thus, it can be regarded as food grade. Nevertheless, its application in dairy products depends on the regulation of genetically modified organisms. These results establish a strategy to select spontaneous Ald-deficient mutants from transformable L. lactis strains. (+info)Reconstitution of a bacterial/plant polyamine biosynthesis pathway in Saccharomyces cerevisiae. (3/1854)
Polyamine synthesis in most organisms is initiated by the decarboxylation of ornithine to form putrescine via ornithine decarboxylase (ODC). Plants, some bacteria and some fungi and protozoa generate putrescine from arginine, via arginine decarboxylase (ADC) and agmatine ureohydrolase (AUH) or agmatine iminohydrolase. A polyamine-requiring strain of Saccharomyces cerevisiae with a mutation in the gene encoding ODC was transformed with plasmids bearing genes encoding Escherichia coli ADC and AUH. Transformants regained the ability to grow in the absence of exogenous polyamines and contained enzyme activities consistent with the presence of both prokaryotic enzymes. Similar results were obtained when a plasmid containing a gene encoding oat (Avena sativa L.) ADC was substituted for the E. coli gene. These data demonstrate the successful complementation of a yeast biosynthetic polyamine synthesis defect by genes encoding an alternative pathway found in bacteria; they also show that plant ADC can substitute for the bacterial enzyme in this pathway. The recombinant yeast provides a tool for the study of the functional properties of these enzymes and for discovery of compounds that specifically inhibit this pathway. (+info)Characterization of mdcR, a regulatory gene of the malonate catabolic system in Klebsiella pneumoniae. (4/1854)
The Klebsiella pneumoniae mdcR gene, which encodes a LysR-type regulator, was overexpressed in Escherichia coli. Purified MdcR was found to bind specifically to the control region of either the malonate decarboxylase (mdc) genes or mdcR. We have also demonstrated that MdcR is an activator of the expression of the mdc genes, whereas it represses the transcription of the putative control region of mdcR, PmdcR, indicating a negative autoregulatory control. (+info)Genetic heterogeneity in propionic acidemia patients with alpha-subunit defects. Identification of five novel mutations, one of them causing instability of the protein. (5/1854)
The inherited metabolic disease propionic acidemia (PA) can result from mutations in either of the genes PCCA or PCCB, which encode the alpha and beta subunits, respectively, of the mitochondrial enzyme propionyl CoA-carboxylase. In this work we have analyzed the molecular basis of PCCA gene defects, studying mRNA levels and identifying putative disease causing mutations. A total of 10 different mutations, none predominant, are present in a sample of 24 mutant alleles studied. Five novel mutations are reported here for the first time. A neutral polymorphism and a variant allele present in the general population were also detected. To examine the effect of a point mutation (M348K) involving a highly conserved residue, we have carried out in vitro expression of normal and mutant PCCA cDNA and analyzed the mitochondrial import and stability of the resulting proteins. Both wild-type and mutant proteins were imported into mitochondria and processed into the mature form with similar efficiency, but the mature mutant M348K protein decayed more rapidly than did the wild-type, indicating a reduced stability, which is probably the disease-causing mechanism. (+info)Cyclic AMP can decrease expression of genes subject to catabolite repression in Saccharomyces cerevisiae. (6/1854)
External cyclic AMP (cAMP) hindered the derepression of gluconeogenic enzymes in a pde2 mutant of Saccharomyces cerevisiae, but it did not prevent invertase derepression. cAMP reduced nearly 20-fold the transcription driven by upstream activation sequence (UAS1FBP1) from FBP1, encoding fructose-1,6-bisphosphatase; it decreased 2-fold the activation of transcription by UAS2FBP1. Nuclear extracts from cells derepressed in the presence of cAMP were impaired in the formation of specific UASFBP1-protein complexes in band shift experiments. cAMP does not appear to act through the repressing protein Mig1. Control of FBP1 transcription through cAMP is redundant with other regulatory mechanisms. (+info)Brown adipose tissue triacylglycerol synthesis in rats adapted to a high-protein, carbohydrate-free diet. (7/1854)
Adaptation of rats to a high-protein, carbohydrate-free (HP) diet induced a marked reduction of brown adipose tissue (BAT) fatty acid (FA) synthesis from both 3H2O and [14C]glucose in vivo, with pronounced decreases in the activities of four enzymes associated with lipogenesis: glucose-6-phosphate dehydrogenase, malic enzyme, citrate lyase, and acetyl-CoA carboxylase. In both HP-adapted and control rats, in vivo incorporation of 3H2O and [14C]glucose into BAT glyceride-glycerol was much higher than into FA. It could be estimated that most of the glycerol synthetized was used to esterify preformed FA. Glycerol synthesis from nonglucose sources (glyceroneogenesis) was increased in BAT from HP rats, as evidenced by an increased capacity of tissue fragments to incorporate [1-14C]pyruvate into glycerol and by a fourfold increase in the activity of phosphoenolpyruvate carboxykinase activity, a key glyceroneogenic enzyme. The data suggest that high rates of glyceroneogenesis and of esterification of preformed FA in BAT from HP-adapted rats are essential for preservation of tissue lipid stores, necessary for heat generation when BAT is recruited in nonshivering thermogenesis. (+info)Evidence for an inducible nucleotide-dependent acetone carboxylase in Rhodococcus rhodochrous B276. (8/1854)
The metabolism of acetone was investigated in the actinomycete Rhodococcus rhodochrous (formerly Nocardia corallina) B276. Suspensions of acetone- and isopropanol-grown R. rhodochrous readily metabolized acetone. In contrast, R. rhodochrous cells cultured with glucose as the carbon source lacked the ability to metabolize acetone at the onset of the assay but gained the ability to do so in a time-dependent fashion. Chloramphenicol and rifampin prevented the time-dependent increase in this activity. Acetone metabolism by R. rhodochrous was CO2 dependent, and 14CO2 fixation occurred concomitant with this process. A nucleotide-dependent acetone carboxylase was partially purified from cell extracts of acetone-grown R. rhodochrous by DEAE-Sepharose chromatography. Analysis by sodium dodecyl sulfate-polyacrylamide gel electrophoresis suggested that the acetone carboxylase was composed of three subunits with apparent molecular masses of 85, 74, and 16 kDa. Acetone metabolism by the partially purified enzyme was dependent on the presence of a divalent metal and a nucleoside triphosphate. GTP and ITP supported the highest rates of acetone carboxylation, while CTP, UTP, and XTP supported carboxylation at 10 to 50% of these rates. ATP did not support acetone carboxylation. Acetoacetate was determined to be the stoichiometric product of acetone carboxylation. The longer-chain ketones butanone, 2-pentanone, 3-pentanone, and 2-hexanone were substrates. This work has identified an acetone carboxylase with a novel nucleotide usage and broader substrate specificity compared to other such enzymes studied to date. These results strengthen the proposal that carboxylation is a common strategy used for acetone catabolism in aerobic acetone-oxidizing bacteria. (+info)
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TIGR01195
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组氨酸脱羧酶 - 维基百科,自由的百科
carboxy-lyase activity. · lyase activity. · amino acid binding. · histidine decarboxylase activity. · pyridoxal phosphate ...
Sulfinoalanine decarboxylase
This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic ... JACOBSEN JG, THOMAS LL, SMITH LH (1964). "Properties and Distribution of Mammalian L-Cysteine Sulfinate Carboxy-Lyases". ... and 3-sulfino-L-alanine carboxy-lyase. This enzyme participates in taurine metabolism. It employs one cofactor, pyridoxal ... name of this enzyme class is 3-sulfino-L-alanine carboxy-lyase (hypotaurine-forming). Other names in common use include ...
Sulfopyruvate decarboxylase
This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic ... This enzyme is also called sulfopyruvate carboxy-lyase. Graupner M, Xu H, White RH (2000). "Identification of the gene encoding ... name of this enzyme class is 3-sulfopyruvate carboxy-lyase (2-sulfoacetaldehyde-forming). ...
Carnitine decarboxylase
This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic ... name of this enzyme class is carnitine carboxy-lyase (2-methylcholine-forming). This enzyme is also called carnitine carboxy- ... lyase. It employs one cofactor, ATP. Khairallah EA, Wolf G (1967). "Carnitine decarboxylase. The conversion of carnitine to ...
Hydroxypyruvate decarboxylase
This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic ... This enzyme is also called hydroxypyruvate carboxy-lyase. This enzyme participates in glyoxylate and dicarboxylate metabolism. ... name of this enzyme class is hydroxypyruvate carboxy-lyase (glycolaldehyde-forming). ...
Orsellinate decarboxylase
4-dihydroxy-6-methylbenzoate carboxy-lyase (orcinol-forming). This enzyme is also called orsellinate carboxy-lyase. Pettersson ... This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic ...
O-pyrocatechuate decarboxylase
3-dihydroxybenzoate carboxy-lyase (catechol-forming). This enzyme is also called 2,3-dihydroxybenzoate carboxy-lyase. This ... This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic ... Rao PV, Moore K, Towers GH (1967). "O-pyrocatechiuc acid carboxy-lyase from Aspergillus niger". Arch. Biochem. Biophys. 122 (2 ...
Phenylpyruvate decarboxylase
This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic ... This enzyme is also called phenylpyruvate carboxy-lyase. This enzyme participates in phenylalanine and tryptophan metabolism. ... name of this enzyme class is phenylpyruvate carboxy-lyase (phenylacetaldehyde-forming). ...
Oxalate decarboxylase
The systematic name of this enzyme class is oxalate carboxy-lyase (formate-forming). This enzyme is also called oxalate carboxy ... This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. ... lyase. This enzyme participates in glyoxylate and dicarboxylate metabolism. As of late 2007, 5 structures have been solved for ...
Stipitatonate decarboxylase
This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic ... This enzyme is also called stipitatonate carboxy-lyase (decyclizing). Bentley R, Thiessen CP (November 1963). "Biosynthesis of ... name of this enzyme class is stipitatonate carboxy-lyase (decyclizing, stipitatate-forming). ...
4-oxalocrotonate decarboxylase
This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic ... This enzyme is also called 4-oxalocrotonate carboxy-lyase. This enzyme participates in 3 metabolic pathways: benzoate ... name of this enzyme class is 4-oxalocrotonate carboxy-lyase (2-oxopent-4-enoate-forming). ...
Phosphonopyruvate decarboxylase
This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic ... This enzyme is also called 3-phosphonopyruvate carboxy-lyase. This enzyme participates in aminophosphonate metabolism. Zhang G ... name of this enzyme class is 3-phosphonopyruvate carboxy-lyase (2-phosphonoacetaldehyde-forming). ...
UDP-glucuronate decarboxylase
This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic ... 1. Uridine diphosphate glucuronate carboxy-lyase of wheat germ". Biochemistry. 4 (11): 2468-2475. doi:10.1021/bi00887a028. ... and UDP-D-glucuronate carboxy-lyase. This enzyme participates in starch and sucrose metabolism and nucleotide sugars metabolism ... name of this enzyme class is UDP-D-glucuronate carboxy-lyase (UDP-D-xylose-forming). Other names in common use include uridine- ...
David Sidney Feingold
V. UDP-D-glucuronate and UDP-D-galacturonate carboxy-lyase of Ampullariella digitata. Fan, D. F. and Feingold, D. S. Arch. ... V. UDP-D-glucuronate and UDP-D-galacturonate carboxy-lyase of Ampullariella digitata. Uridine diphosphate-D-glucose ... Mechanism of action of UDP-glucuronate carboxyl-lyase. Schutzbach, J. S. and Feingold D. S. J. Biol. Chem. 245:2476-2482, 1970 ... Mechanism of action of UDP-glucuronate carboxyl-lyase. Biosynthesis of uridine diphosphate-D-xylose. ...
4,5-dihydroxyphthalate decarboxylase
This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic ... 5-dihydroxyphthalate carboxy-lyase (3,4-dihydroxybenzoate-forming). This enzyme is also called 4,5-dihydroxyphthalate carboxy- ... lyase. This enzyme participates in 2,4-dichlorobenzoate degradation. Ribbons DW, Evans WC (1966). "Oxidative metabolism of ...
3,4-dihydroxyphthalate decarboxylase
This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic ... 4-dihydroxyphthalate carboxy-lyase (3,4-dihydroxybenzoate-forming). This enzyme is also called 3,4-dihydroxyphthalate carboxy- ... lyase. Eaton RW, Ribbons DW (1982). "Metabolism of dibutylphthalate and phthalate by Micrococcus sp. strain 12B". J. Bacteriol ...
Tartrate decarboxylase
... tartrate carboxy-lyase (D-glycerate-forming). This enzyme is also called (R,R)-tartrate carboxy-lyase. Furuyoshi S, Kawabata N ... This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic ...
Aspartate 4-decarboxylase
This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic ... Wilson EM; Kornberg HL (1963). "Properties of crystalline l-aspartate 4-carboxy-lyase from Achromobacter sp". Biochem. J. 88 (3 ... and L-aspartate 4-carboxy-lyase. This enzyme participates in alanine and aspartate metabolism and cysteine metabolism. It ... name of this enzyme class is L-aspartate 4-carboxy-lyase (L-alanine-forming). Other names in common use include desulfinase, ...
Hydroxyglutamate decarboxylase
This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic ... This enzyme is also called 3-hydroxy-L-glutamate 1-carboxy-lyase. It employs one cofactor, pyridoxal phosphate. Umbreit WW, ... name of this enzyme class is 3-hydroxy-L-glutamate 1-carboxy-lyase (4-amino-3-hydroxybutanoate-forming). ...
Benzoylformate decarboxylase
This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic ... and benzoylformate carboxy-lyase. This enzyme participates in benzoate degradation via hydroxylation and toluene and xylene ... name of this enzyme class is benzoylformate carboxy-lyase (benzaldehyde-forming). Other names in common use include ...
Gallate decarboxylase
This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic ... and gallate carboxy-lyase. This enzyme participates in benzoate degradation via coa ligation. Grant DJ, Patel JC (1969). "The ... 5-trihydroxybenzoate carboxy-lyase (pyrogallol-forming). Other names in common use include gallic acid decarboxylase, ...
Aminobenzoate decarboxylase
This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic ... name of this enzyme class is aminobenzoate carboxy-lyase (aniline-forming). It employs one cofactor, pyridoxal phosphate. ...
Valine decarboxylase
This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic ... Other names in common use include leucine decarboxylase and L-valine carboxy-lyase. It employs one cofactor, pyridoxal ... name of this enzyme class is L-valine carboxy-lyase (2-methylpropanamine-forming). ...
Acetylenedicarboxylate decarboxylase
This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic ... and acetylenedicarboxylate carboxy-lyase. This enzyme participates in pyruvate metabolism. Yamada EW, Jakoby WB (September 1958 ... name of this enzyme class is acetylenedicarboxylate carboxy-lyase (pyruvate-forming). Other names in common use include ...
3-oxolaurate decarboxylase
This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic ... and 3-oxododecanoate carboxy-lyase. FRANKE W, PLATZECK A, EICHHORN G (1961). "[On the knowledge of fatty acid catabolism by ... name of this enzyme class is 3-oxododecanoate carboxy-lyase (2-undecanone-forming). Other names in common use include beta- ...
Glutaconyl-CoA decarboxylase
... pent-2-enoyl-CoA carboxy-lyase, and 4-carboxybut-2-enoyl-CoA carboxy-lyase. This enzyme participates in benzoate degradation ... This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic ... name of this enzyme class is 4-carboxybut-2-enoyl-CoA carboxy-lyase (but-2-enoyl-CoA-forming). Other names in common use ...
Methylmalonyl-CoA decarboxylase
2-methyl-3-oxopropanoyl-CoA carboxy-lyase [incorrect], and (S)-methylmalonyl-CoA carboxy-lyase. This enzyme participates in ... This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic ... methylmalonyl-CoA carboxy-lyase (propanoyl-CoA-forming). Other names in common use include propionyl-CoA carboxylase, propionyl ...
Phenylalanine decarboxylase
This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic ... and L-phenylalanine carboxy-lyase. This enzyme participates in phenylalanine metabolism. It employs one cofactor, pyridoxal ... name of this enzyme class is L-phenylalanine carboxy-lyase (phenylethylamine-forming). Other names in common use include L- ...
3-hydroxy-2-methylpyridine-4,5-dicarboxylate 4-decarboxylase
This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic ... 5-dicarboxylate 4-carboxy-lyase. This enzyme participates in vitamin B6 metabolism. Snell EE, Smucker AA, Ringelmann E, Lynen F ... 5-dicarboxylate 4-carboxy-lyase (3-hydroxy-2-methylpyridine-5-carboxylate-forming). This enzyme is also called 3-hydroxy-2- ...
Aconitate decarboxylase
... cis-aconitate carboxy-lyase, and cis-aconitate carboxy-lyase. This enzyme participates in c5-branched dibasic acid metabolism. ... This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic ... name of this enzyme class is cis-aconitate carboxy-lyase (itaconate-forming). Other names in common use include cis-aconitic ...
Homoisocitrate dehydrogenase
Other names in common use include 2-hydroxy-3-carboxyadipate dehydrogenase, 3-carboxy-2-hydroxyadipate dehydrogenase, ... homoisocitric dehydrogenase, (−)-1-hydroxy-1,2,4-butanetricarboxylate:NAD+ oxidoreductase, (decarboxylating), 3-carboxy-2- ...
Glutamate decarboxylase
4.1.1: Carboxy-lyases. *Acetoacetate decarboxylase. *Adenosylmethionine decarboxylase. *Arginine decarboxylase. *Aromatic L- ...
Leukotriene-A4 hydrolase
EC4 Lyases (list). *EC5 Isomerases (list). *EC6 Ligases (list). *EC7 Translocases (list) ... Antagonists: 20-Carboxy-LTB4. *Amelubant. *CGS-23131 (LY-223982). *CGS-25019C ...
DAHP synthase
D-erythrose-4-phosphate lyase (pyruvate-phosphorylating), D-erythrose-4-phosphate-lyase, D-erythrose-4-phosphate-lyase ( ... 2-carboxy-2-oxoethyl-forming). Other names in common use include 2-dehydro-3-deoxy-phosphoheptonate aldolase, 2-keto-3-deoxy-D- ... lyase (pyruvate-phosphorylating), 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate, ...
Glucose 6-phosphatase
EC4 Lyases (list). *EC5 Isomerases (list). *EC6 Ligases (list). *EC7 Translocases (list) ... Ubiquitin carboxy-terminal hydrolase L1. *4-hydroxybenzoyl-CoA thioesterase. 3.1.3: Phosphatase. *Alkaline phosphatase *ALPI ...
Phosphoribosylaminoimidazolecarboxamide formyltransferase
EC4 Lyases (list). *EC5 Isomerases (list). *EC6 Ligases (list). *EC7 Translocases (list) ... 2.1.3: Carboxy-. and Carbamoyl. Carboxy. *methylmalonyl-CoA carboxytransferase. Carbamoyl. *Aspartate carbamoyltransferase ...
DNA methyltransferase
2.1.3: Carboxy-. and Carbamoyl. Carboxy. *methylmalonyl-CoA carboxytransferase. Carbamoyl. *Aspartate carbamoyltransferase ...
Carbamoyl phosphate synthetase
This enzyme catalyzes the reaction of ATP and bicarbonate to produce carboxy phosphate and ADP. Carboxy phosphate reacts with ... The large subunit has two homologous carboxy phosphate domains, both of which have ATP-binding sites; however, the N-terminal ... The large subunit in bacterial CPSase has four structural domains: the carboxy phosphate domain 1, the oligomerisation domain, ... The carboxy phosphate domain found duplicated in the large subunit of CPSase is also present as a single copy in the biotin- ...
BCKDHA
carboxy-lyase activity. • 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity. • alpha-ketoacid ...
Fatty acid
The position of the carbon atoms in a fatty acid can be indicated from the −COOH (or carboxy) end, or from the −CH3 (or methyl ... There it is cleaved by ATP citrate lyase into acetyl-CoA and oxaloacetate. The oxaloacetate is returned to the mitochondrion as ...
Fructose-bisphosphate aldolase
4.1.1: Carboxy-lyases. *Acetoacetate decarboxylase. *Adenosylmethionine decarboxylase. *Arginine decarboxylase. *Aromatic L- ...
Dihydrofolate reductase
... of piritrexim and other diaminopyrimidine dihydrofolate reductase inhibitors with omega-carboxyalkoxy or omega-carboxy-1- ...
Arachidonate 5-lipoxygenase
Antagonists: 20-Carboxy-LTB4. *Amelubant. *CGS-23131 (LY-223982). *CGS-25019C ...
List of enzymes
Intramolecular lyases: EC number. Examples EC 5.5.1.1. Muconate cycloisomerase EC 5.5.1.2. 3-carboxy-cis,cis-muconate ... Category:Lyases (EC 4) (Lyase)Edit. Category:EC 4.1 (carbon-carbon lyases)Edit. *Category:EC 4.1.1 *Ornithine decarboxylase (EC ... 4 Category:Lyases (EC 4) (Lyase) *4.1 Category:EC 4.1 (carbon-carbon lyases) ... Category:EC 4.3 (carbon-nitrogen lyases)Edit. *Category:EC 4.3.1 *Phenylalanine ammonia-lyase (EC 4.3.1.24) ...
Cathepsin A
1990). "Galactosialidosis: simultaneous deficiency of esterase, carboxy-terminal deamidase and acid carboxypeptidase activities ... EC4 Lyases (list). *EC5 Isomerases (list). *EC6 Ligases (list). *EC7 Translocases (list) ...
N-acylneuraminate-9-phosphate synthase
The systematic name of this enzyme class is phosphoenolpyruvate:N-acyl-D-mannosamine-6-phosphate 1-(2-carboxy-2-oxoethyl) ... Other names in common use include N-acetylneuraminate 9-phosphate lyase, N-acetylneuraminate 9-phosphate sialic acid 9- ... phosphate synthase, N-acetylneuraminate 9-phosphate synthetase, N-acylneuraminate-9-phosphate pyruvate-lyase, (pyruvate- ...
Eosinophil-derived neurotoxin
lyase activity. Cellular component. • extracellular region. • lysosome. • extracellular exosome. • azurophil granule lumen. ... Ubiquitin carboxy-terminal hydrolase L1. *4-hydroxybenzoyl-CoA thioesterase. 3.1.3: Phosphatase. *Alkaline phosphatase *ALPI ...
GAD1
lyase activity. • protein heterodimerization activity. • pyridoxal phosphate binding. • carboxy-lyase activity. • glutamate ...
Category:Protein pages needing a picture
2-hydroxyphytanoyl-CoA lyase. *2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase ...
Deoxyribonuclease II
Ubiquitin carboxy-terminal hydrolase L1. *4-hydroxybenzoyl-CoA thioesterase. 3.1.3: Phosphatase. *Alkaline phosphatase *ALPI ...
Cyclin-dependent kinase 8
RNA polymerase II carboxy-terminal domain kinase activity. • ATP binding. • protein serine/threonine kinase activity. • cyclin- ...
Restriction enzyme
Ubiquitin carboxy-terminal hydrolase L1. *4-hydroxybenzoyl-CoA thioesterase. 3.1.3: Phosphatase. *Alkaline phosphatase *ALPI ...
Oxalyl-CoA decarboxylase
CO2 OXC belongs to the family of lyases, specifically the carboxy-lyases (decarboxylases), which cleave carbon-carbon bonds. ... The systematic name of this enzyme class is oxalyl-CoA carboxy-lyase (formyl-CoA-forming). Other names in common use include ... and oxalyl-CoA carboxy-lyase. This enzyme participates in glyoxylate and dicarboxylate metabolism. It employs one cofactor, ...
Indole-3-glycerol-phosphate synthase
This enzyme belongs to the family of lyases, to be specific, the carboxy-lyases, which cleave carbon-carbon bonds. The ... and carboxy-lyase (cyclizing). This enzyme participates in phenylalanine, tyrosine and tryptophan biosynthesis and two- ... 1-deoxy-D-ribulose-5-phosphate carboxy-lyase [cyclizing 1-C-(indol-3-yl)glycerol-3-phosphate-forming]. Other names in common ...
UXS1
Carboxy-lyases Golgi apparatus Tetrameric protein Uridine diphosphate (UDP) GRCh38: Ensembl release 89: ENSG00000115652 - ...
carboxy-lyase activity Gene Ontology Term (GO:0016831)
The Gene Ontology (GO) project is a collaborative effort to address the need for consistent descriptions of gene products across databases. You can use this browser to view terms, definitions, and term relationships in a hierarchical display. Links to summary annotated gene data at MGI are provided in Term Detail reports.
S-adenosyl-L-methionine:(3-phospho-D-glycerate-carboxy-lyase (dimerizing))-lysine 6-N-methyltransferase - Wikipedia
ubiD - 3-octaprenyl-4-hydroxybenzoate carboxy-lyase - Escherichia coli (strain K12) - ubiD gene & protein
carboxy-lyase activity Source: GO_Central ,p>Inferred from Biological aspect of Ancestor,/p> ,p>A type of phylogenetic evidence ... 3-octaprenyl-4-hydroxybenzoate carboxy-lyaseAdd BLAST. 497. Proteomic databases. jPOST - Japan Proteome Standard Repository/ ... 3-Octaprenyl-4-hydroxybenzoate carboxy-lyase.". Leppik R.A., Young I.G., Gibson F.. Biochim. Biophys. Acta 436:800-810(1976) [ ... 3-Octaprenyl-4-hydroxybenzoate carboxy-lyase.". Leppik R.A., Young I.G., Gibson F.. Biochim. Biophys. Acta 436:800-810(1976) [ ...
Carboxy-Lyases | Semantic Scholar
Hematological Cancers Drug Pipeline Update 2012
Identification of the active site residues in ATP-citrate lyase's carboxy-terminal portion. - NextBio article
Identification of the active site residues in ATP-citrate lyases carboxy-terminal portion. Vinh H Nguyen, Noreen Singh, Ana ... Identification of the active site residues in ATP-citrate lyases carboxy-terminal portion. Protein science : a publication of ... ATP-citrate lyase (ACLY) catalyzes production of acetyl-CoA and oxaloacetate from CoA and citrate using ATP. In humans, this ... The carboxy(C)-terminal portion of ACLY shows sequence similarity to citrate synthase of the tricarboxylic acid cycle. To ...
HDC histidine decarboxylase [Homo sapiens (human)] - Gene - NCBI
De novo NAD + synthesis enhances mitochondrial function and improves health
Initial characterization of a HTC cell variant partially resistant to the anti-proliferative effect of ornithine decarboxylase...
UROD gene: MedlinePlus Genetics
Pyridoxal phosphate-dependent decarboxylase (IPR002129) | InterPro | EMBL-EBI
Decarboxylase MfnA, archaea (IPR020931) | InterPro | EMBL-EBI
组氨酸脱羧酶 - 维基百科,自由的百科
KEGG ENZYME: 4.1.1.90
KEGG ENZYME: 4.1.1.21
1-(5-phosphoribosyl)-5-amino-4-imidazolecarboxylate carboxy-lyase;. ADE2;. class II PurE;. 5-amino-1-(5-phospho-D-ribosyl) ... 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate carboxy-lyase [5-amino-1-(5-phospho-D-ribosyl)imidazole-forming]. ... Lyases;. Carbon-carbon lyases;. Carboxy-lyases. BRITE hierarchy. Sysname. ...
FlyBase Gene Report: Dmel\Pepck2
Identification of a toxic mechanism of the plasticizers, phtahlic acid esters, which are putative endocrine disrupters: time...
Biotin requirements are lower in human Jurkat lymphoid cells but homeostatic mechanisms are similar to those of HepG2 liver...
MEDLINE - Resultado p gina 1
Comparative properties of crude L-aspartate 4-Carboxy-lyase of Cunninghamella elegans and Penicillium citrinum | Egyptian...
Studies on the biosynthesis of L-aspartate 4-carboxy-lyase by Cunninghamella elegans and Penicillium citrinum | Egyptian...
Characterization and expression of the complementary DNA encoding rat histidine decarboxylase | PNAS
A1JIG1 | SWISS-MODEL Repository
C4LD33 | SWISS-MODEL Repository
SWISSPROT: Q5LVU5 RUEPO
SWISSPROT: D7TDV1 VITVI
RP821 - Uncharacterized protein RP821 - Rickettsia prowazekii (strain Madrid E) - RP821 gene & protein
UXS1 Gene - GeneCards | UXS1 Protein | UXS1 Antibody
Decarboxylase1
- 5UOU: High resolution structure of 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase from Klebsiella pneumoniae subsp. (rcsb.org)
Enzymes1
- We have isolated cDNA clones for the maize leaf enzymes phosphoenolpyruvate (P-ePrv) carboxylase [orthophosphate:oxaloacetate carboxy-lyase (phosphorylating) EC 4.1.1.31] and pyruvate,orthophosphate (Prv,Pi) dikinase (ATP:pyruvate,orthophosphate phosphotransferase, EC 2.7.9.1) by exploiting the light-inducibility and large size of the mRNAs (3.5 kilobases) that encode the two enzymes. (caltech.edu)
Orthophosphate:oxaloacetate carboxy-lyase1
- Phosphoenolpyruvate carboxylase is the recommended name for EC 4.1.1.31, orthophosphate:oxaloacetate carboxy-lyase (phosphorylating). (thefreedictionary.com)
PORPHYRINOGEN CARBOXY-LYASE1
- Pentacarboxylporphyrin I is a bile product produced by conversion of Pentacarboxylporphyrinogen I by porphyrinogen carboxy-lyase. (scbt.com)
Enzyme3
- S-adenosyl-L-methionine:(3-phospho-D-glycerate-carboxy-lyase (dimerizing))-lysine 6-N-methyltransferase may refer to: (Ribulose-bisphosphate carboxylase)-lysine N-methyltransferase (Fructose-bisphosphate aldolase)-lysine N-methyltransferase This set index page lists enzyme articles associated with the same name. (wikipedia.org)
- This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. (wikipedia.org)
- The systematic name of this enzyme class is 3-sulfino-L-alanine carboxy-lyase (hypotaurine-forming). (wikipedia.org)
Activity3
- GO annotations related to this gene include protein heterodimerization activity and carboxy-lyase activity . (genecards.org)
- Livers from newborn mice homozygous for either one of the lethal deletions c14CoS or c3H in chromosome 7 have drastically reduced levels of cytosolic phosphoenolpyruvate carboxykinase (GTP) [GTP:oxaloacetate carboxy-lyase (transphosphorylating), EC 4.1.1.32] activity when compared with normal littermates. (pnas.org)
- Molecular function: 3-octaprenyl-4-hydroxybenzoate carboxy-lyase activity. (expasy.org)
Phosphoenolpyruvate1
- The effect of 3-mercaptopicolinate, an inhibitor of phosphoenolpyruvate carboxykinase [GTP:oxaloacetate carboxy-lyase (transphosphorylating), EC 4.1.1.32], was tested on NH3 formation via the purine nucleotide cycle and glutamate dehydrogenase (EC 1.4.1.2). (biochemj.org)
Decarboxylases1
- Carboxy-lyases are involved in the the addition of a carboxyl group to a compound (carboxylases) or the removal of a carboxyl group from a compound (decarboxylases). (flybase.org)
1.221
- L-histidine carboxy-lyase, EC 4.1.1.22). (pnas.org)
Residues1
- Identification of the active site residues in ATP-citrate lyase's carboxy-terminal portion. (illumina.com)
Term1
- Term, carboxy-lyases ( EC number 4.1.1 ) ester Synthesis is also an overall increase in entropy to! (icsantos.com.br)