Benzamidines
Lyases
Heterocyclic Compounds
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.
Furans
Structure-Activity Relationship
Molecular Structure
Pectobacterium chrysanthemi
Crystallography, X-Ray
Chondroitinases and Chondroitin Lyases
Models, Molecular
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.
Chicory
Aldehyde-Lyases
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).
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
Polygalacturonase
Alginates
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).
Substrate Specificity
Phycobilins
Chondroitin ABC Lyase
Sphingomonas
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
Cytochromes c1
Bacteroides
Flavobacterium
Adenylosuccinate Lyase
Streptococcus anginosus
Glucuronic Acid
Hevea
Cloning, Molecular
Glycosaminoglycans
Proteus vulgaris
Sequence Homology, Amino Acid
Uronic Acids
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.
Sulfonium Compounds
Dermatan Sulfate
Carbohydrate Sequence
Carbon-Nitrogen Lyases
Carbon-Carbon Lyases
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.
Pseudomonas
N-Glycosyl Hydrolases
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.
Hydrogen-Ion Concentration
Kinetic and inhibition studies on substrate channelling in the bifunctional enzyme catalysing C-terminal amidation. (1/31)
A series of experiments has been conducted to investigate the possibility that substrate channelling might occur in the bifunctional forms of enzymes carrying out C-terminal amidation, a post-translational modification essential to the biological activity of many neuropeptides. C-terminal amidation entails sequential action by peptidylglycine mono-oxygenase (PAM, EC 1.14.17.3) and peptidylamidoglycolate lyase (PGL, EC 4.3.2.5), with the mono-oxygenase catalysing conversion of a glycine-extended pro-peptide into the corresponding alpha-hydroxyglycine derivative, which is then converted by the lyase into amidated peptide plus glyoxylate. Since the mono-oxygenase and lyase reactions exhibit tandem reaction stereospecificities, channelling of the alpha-hydroxy intermediate might occur, as is the case for some other multifunctional enzymes. Selective inhibition of the mono-oxygenase domain by competitive ester inhibitors, as well as mechanism-based mono-oxygenase inactivation by the novel olefinic inhibitor 5-acetamido-4-oxo-6-phenylhex-2-enoate (N-acetylphenylalanyl acrylate), has little to no effect on the kinetic parameters of the lyase domain of the AE from Xenopus laevis. Similarly, inhibition of the lyase domain by the potent dioxo inhibitor 2,4-dioxo-5-acetamido-6-phenylhexanoate has little effect on the activity of the monooxygenase domain in the bifunctional enzyme. A series of experiments on intermediate accumulation and conversion were also carried out, along with kinetic investigations of the reactivities of the monofunctional and bifunctional forms of PAM and PGL towards substrates and inhibitors. Taken together, the results demonstrate the kinetic independence of the mono-oxygenase and lyase domains, and provide no evidence for substrate channelling between these domains in the bifunctional amidating enzyme. (+info)Kinetic and stereochemical studies on novel inactivators of C-terminal amidation. (2/31)
C-terminal amidation, a required post-translational modification for the bioactivation of many neuropeptides, entails sequential enzymic action by peptidylglycine alpha-mono-oxygenase (PAM, EC 1.14.17.3) and peptidylamidoglycolate lyase (PGL, EC 4.3.2.5). Here we introduce novel compounds in which an olefinic functionality is incorporated into peptide analogues as the most potent turnover-dependent inactivators of PAM. Kinetic parameters for PAM inactivation by 4-oxo-5-acetamido-6-phenyl-hex-2-enoic acid and 4-oxo-5-acetamido-6-(2-thienyl)-hex-2-enoic acid were obtained by using both the conventional dilution assay method and the more complex progress curve method. The results obtained from the progress curve method establish that these compounds exhibit the kinetic characteristics of pure competitive inactivators (i.e. no ESI complex forms during inactivation). On the basis of k(inact)/K(i) values, 4-oxo-5-acetamido-6-(2-thienyl)-hex-2-enoic acid is almost two orders of magnitude more potent than benzoylacrylate, a chemically analogous olefinic inactivator that lacks the peptide moiety. Stereochemical studies established that PAM inactivation by 4-oxo-5-acetamido-6-(2-thienyl)-hex-2-enoic acid is stereospecific with respect to the moiety at the P(2) position, which is consistent with previous results with substrates and reversible inhibitors. In contrast, 2, 4-dioxo-5-acetamido-6-phenylhexanoic acid, which is a competitive inhibitor with respect to ascorbate, exhibits a low degree of stereospecificity in binding to the ascorbate sites of both PAM and dopamine-beta-hydroxylase. (+info)Urea is a product of ureidoglycolate degradation in chickpea. Purification and characterization of the ureidoglycolate urea-lyase. (3/31)
A ureidoglycolate-degrading activity was analyzed in different organs of chickpea (Cicer arietinum). Activity was detected in all the tissues analyzed, but highest levels of specific activity were found in pods, from which it has been purified and characterized. This is the first ureidoglycolate-degrading activity that has been purified to homogeneity from any photosynthetic organism. Only one ureidoglycolate-degrading activity was found during the purification. The enzyme was purified 1,500-fold, and specific activity for the pure enzyme was 8.6 units mg(-1), which corresponds with a turnover number of 1,600 min(-1). The native enzyme has a molecular mass of 180 kD and consists of six identical or similar-sized subunits of 31 kD each. The enzyme exhibited hyperbolic, Michaelian kinetics for (-) ureidoglycolate with K(m) values of 6 and 10 microM in the presence or absence of Mn(2+), respectively. Optimum pH was between 7 and 8 and maximum activity was found at temperatures above 70 degrees C, the enzyme being extremely stable and resistant to heat denaturation. The activity was inhibited by EDTA and enhanced by several bivalent cations, thus suggesting that the enzyme is a metalloprotein. This enzyme has been characterized as a ureidoglycolate urea-lyase (EC 4.3.2.3), which catalyzes the degradation of (-) ureidoglycolate to glyoxylate and urea. This is the first time that such an activity is detected in plant tissues. A possible function for this activity and its implications in the context of nitrogen mobilization in legume plants is also discussed. (+info)Pathways for urea production during early life of an air-breathing teleost, the African catfish Clarias gariepinus Burchell. (4/31)
Embryos and larvae of the African catfish Clarias gariepinus excrete significant quantities of urea. The present study focused on the potential urea-generating pathways during early development of this teleost; uricolysis, argininolysis and the ornithine-urea cycle (OUC). Uricase, allantoinase, allantoicase and ureidoglycollate lyase of the uricolytic pathway were expressed in all early life stages and in adult liver of C. gariepinus. Uricase activity increased in starved larvae compared with yolk-sac larvae. The key regulatory enzyme of the teleost OUC, carbamoyl phosphate synthetase III (CPSase III), was expressed predominantly in muscle of developing C. gariepinus larvae and showed negligible activity in the absence of its allosteric effector N-acetyl-L-glutamate. CPSase III and ornithine carbamoyl transferase activities increased in fed larvae compared with starved larvae. In contrast to the early developmental stages, adult C. gariepinus expressed only low and variable levels of CPSase III, suggesting that, under the experimental conditions employed, OUC expression is influenced by developmental stage in this species. The data indicate that early C. gariepinus life stages express the enzymes necessary for urea production by uricolysis, argininolysis and the OUC, and this may explain why urea tissue levels and urea excretion rates are substantial during the early development of this air-breathing teleost. (+info)Catalysis, stereochemistry, and inhibition of ureidoglycolate lyase. (5/31)
Ureidoglycolate lyase (UGL, EC 4.3.2.3) catalyzes the breakdown of ureidoglycolate to glyoxylate and urea, which is the final step in the catabolic pathway leading from purines to urea. Although the sequence of enzymatic steps was worked out nearly 40 years ago, the stereochemistry of the uric acid degradation pathway and the catalytic properties of UGL have remained very poorly described. We now report the first direct investigation of the absolute stereochemistry of UGL catalysis. Using chiral chromatographic analyses with substrate enantiomers, we demonstrate that UGL catalysis is stereospecific for substrates with the (S)-hydroxyglycine configuration. The first potent competitive inhibitors for UGL are reported here. These inhibitors are compounds which contain a 2,4-dioxocarboxylate moiety, designed to mimic transient species produced during lyase catalysis. The most potent inhibitor, 2,4-dioxo-4-phenylbutanoic acid, exhibits a KI value of 2.2 nM and is therefore among the most potent competitive inhibitors ever reported for a lyase enzyme. New synthetic alternate substrates for UGL, which are acyl-alpha-hydroxyglycine compounds, are described. Based on these alternate substrates, we introduce the first assay method for monitoring UGL activity directly. Finally, we report the first putative primary nucleotide and derived peptide sequence for UGL. This sequence exhibits a high level of similarity to the fumarylacetoacetate hydrolase family of proteins. Close mechanistic similarities can be visualized between the chemistries of ureidoglycolate lyase and fumarylacetoacetate hydrolase catalysis. (+info)Differentially regulated malate synthase genes participate in carbon and nitrogen metabolism of S. cerevisiae. (6/31)
We have isolated a second gene (MLS1), which in addition to DAL7, encodes malate synthase from S. cerevisiae. Expression of the two genes is specific for their physiological roles in carbon and nitrogen metabolism. Expression of MLS1, which participates in the utilization of non-fermentable carbon sources, is sensitive to carbon catabolite repression, but nearly insensitive to nitrogen catabolite repression. DAL7, which participates in catabolism of the nitrogenous compound allantoin, is insensitive to carbon catabolite repression, but highly sensitive to nitrogen catabolite repression. Results obtained with null mutations in these genes suggest that S. cerevisiae contains at least one and perhaps two additional malate synthase genes. (+info)The source of the oxygen atom in the alpha-hydroxyglycine intermediate of the peptidylglycine alpha-amidating reaction. (7/31)
Peptidylglycine alpha-amidating activity catalyses the oxidation of a C-terminally glycine-extended peptide to a desglycine alpha-amidated peptide at the expense of ascorbate and O2 in the presence of Cu2+. The reaction involves oxidative N-dealkylation within the terminal glycine residue, with retention of the glycine N atom and release of the remainder as glyoxylate. Recent studies by us and others have revealed that the reaction consists of two steps via a carbinolamide as an intermediate (peptidyl alpha-hydroxyglycine), and also that two separate enzymes derived from a common precursor protein catalyse these steps, formation of the carbinolamide and its conversion into alpha-amide and glyoxylate. As for the mechanism of carbinolamide formation, two distinct pathways can be considered: direct mono-oxygenation at the glycine alpha-C atom and dehydrogenation leading to an imine followed by hydration. To draw a distinction between them, we carried out the reaction with D-Tyr-Val-Gly as the substrate either in the H2(18)O-enriched medium or under an atmosphere of 18O2, and isolated the alpha-hydroxylglycine intermediate. The fast-atom-bombardment mass-spectral analysis demonstrated that the hydroxy O atom comes from O2, but not from H2O, indicating that the alpha-hydroxylation should be a monooxygenase reaction. (+info)Intermittent hypoxia activates peptidylglycine alpha-amidating monooxygenase in rat brain stem via reactive oxygen species-mediated proteolytic processing. (8/31)
(+info)
DAL3 - Ureidoglycolate lyase - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Bakers yeast) - DAL3 gene & protein
allA - Ureidoglycolate lyase - Shigella flexneri - allA gene & protein
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Ureidoglycolate lyase
... specifically amidine lyases. The systematic name of this enzyme class is (S)-ureidoglycolate urea-lyase (glyoxylate-forming). ... The enzyme ureidoglycolate lyase (EC 4.3.2.3) catalyzes the chemical reaction (S)-ureidoglycolate ⇌ {\displaystyle \ ... ureidoglycolate urea-lyase. This enzyme participates in purine metabolism. Trijbels F, Vogels GD (1967). "Allantoate and ... rightleftharpoons } glyoxylate + urea This enzyme belongs to the family of lyases, ...
Peptidylamidoglycolate lyase
... specifically amidine lyases. The systematic name of this enzyme class is [peptide]-(2S)-2-hydroxyglycine peptidyl-amide-lyase ( ... peptidyl-α-hydroxyglycine α-amidating lyase, HGAD, PGL, PAL, and peptidylamidoglycolate peptidylamide-lyase. Katopodis AG, Ping ... The enzyme peptidylamidoglycolate lyase (EC 4.3.2.5) catalyzes the chemical reaction [peptide]-(2S)-2-hydroxyglycine = [peptide ... amide + glyoxylate This enzyme belongs to the family of lyases, ...
List of MeSH codes (D08)
... tyrosine phenol-lyase MeSH D08.811.520.232.300 - amidine-lyases MeSH D08.811.520.232.300.200 - adenylosuccinate lyase MeSH ... chondroitin lyases MeSH D08.811.520.241.700.350.500.500 - chondroitin abc lyase MeSH D08.811.520.241.700.512 - heparin lyase ... ammonia-lyases MeSH D08.811.520.232.400.200 - aspartate ammonia-lyase MeSH D08.811.520.232.400.350 - ethanolamine ammonia-lyase ... lyase MeSH D08.811.520.241.300 - hydro-lyases MeSH D08.811.520.241.300.050 - aconitate hydratase MeSH D08.811.520.241.300.050. ...
Purine imidazole-ring cyclase
... specifically amidine lyases. The systematic name of this enzyme class is DNA-4,6-diamino-5-formamidopyrimidine C8-N9-lyase ( ... 9-N-lyase (cyclizing, DNA-adenine-forming). Chetsanga CJ, Grigorian C (1985). "In situ enzymatic reclosure of opened imidazole ... cyclizing DNA-adenine-forming). Other names in common use include DNA-4,6-diamino-5-formamidopyrimidine 8-C,9-N-lyase ( ... H2O This enzyme belongs to the family of lyases, ...
List of enzymes
EC 4.3.1 Phenylalanine ammonia-lyase (EC 4.3.1.24) Category:EC 4.4.1 Cystathionine gamma-lyase Cystathionine beta-lyase ... In linear amidines) Arginase (EC 3.5.3.1) Category:EC 3.5.4 (In cyclic amidines) Adenosine deaminase (EC 3.5.4.4) GTP ... lyase) ligase EC 6.2.1.23: Dicarboxylate-CoA ligase EC 6.2.1.24: Phytanate-CoA ligase EC 6.2.1.25: Benzoate-CoA ligase EC 6.2. ...
GO:0016842: amidine-lyase activity details
Argininosuccinate Lyase | Harvard Catalyst Profiles | Harvard Catalyst
Carbon-Nitrogen Lyases [D08.811.520.232]. *Amidine-Lyases [D08.811.520.232.300]. *Argininosuccinate Lyase [D08.811.520.232. ... "Argininosuccinate Lyase" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH (Medical ... Argininosuccinate lyase deficiency: longterm outcome of 13 patients detected by newborn screening. Mol Genet Metab. 2009 Nov; ... This graph shows the total number of publications written about "Argininosuccinate Lyase" by people in Harvard Catalyst ...
SymbC1.scaffold4327.2 details
DeCS
EDJ90283 details
EOD24208 details
Carbon-Nitrogen Lyases | Profiles RNS
Subclasses are the AMMONIA-LYASES, the AMIDINE-LYASES, the amine-lyases, and other carbon-nitrogen lyases. EC 4.3. ... "Carbon-Nitrogen Lyases" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH (Medical ... This graph shows the total number of publications written about "Carbon-Nitrogen Lyases" by people in this website by year, and ... Below are the most recent publications written about "Carbon-Nitrogen Lyases" by people in Profiles. ...
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boronic acids, carboxylic acids, imidazoles, thiazoles, azoles, indoles, oxindoles, pyridines, heterocycles, bormides, fluoro compounds, amines, aldehydes, isoquinolines, nitro compounds, trifluoroborates, PEG linkers, inhibitors, amino acids and peptides, catalysts and ligands, custom synthesis , other organics and fine chemicals supplier.
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boronic acids, carboxylic acids, imidazoles, thiazoles, azoles, indoles, oxindoles, pyridines, heterocycles, bormides, fluoro compounds, amines, aldehydes, isoquinolines, nitro compounds, trifluoroborates, PEG linkers, inhibitors, amino acids and peptides, catalysts and ligands, custom synthesis , other organics and fine chemicals supplier.
Aspartate ammonia-lyase - Wikipedia
This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic ... Other names in common use include aspartase, fumaric aminase, L-aspartase, and L-aspartate ammonia-lyase. This enzyme ... In enzymology, an aspartate ammonia-lyase (EC 4.3.1.1) is an enzyme that catalyzes the chemical reaction ... This lyase article is a stub. You can help Wikipedia by expanding it. ...
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Carbon-Oxygen Lyases,N0000008169, Amines,N0000008168, Amidines,N0000008167, Nitric Acid,N0000008166, Carotenoids,N0000008165, ... Polysaccharide-Lyases,N0000007834, Amino Acids, Peptides, and Proteins,N0000007833, Amino Acids, Dicarboxylic,N0000007832, ... Lyases,N0000008273, Electrolytes,N0000008272, Eicosanoids,N0000008271, Glucosidases,N0000008270, Acids, Aldehydic,N0000008269, ...
MeSH Browser
Lyases [D08.811.520] * Carbon-Nitrogen Lyases [D08.811.520.232] * Amidine-Lyases [D08.811.520.232.300] * Adenylosuccinate Lyase ... Amidine-Lyases Preferred Term Term UI T058744. Date01/01/1999. LexicalTag NON. ThesaurusID NLM (1998). ... Amidine-Lyases Preferred Concept UI. M0029322. Registry Number. EC 4.3.2.-. Scope Note. These enzymes catalyze the elimination ... Amidine-Lyases. Tree Number(s). D08.811.520.232.300. Unique ID. D019760. RDF Unique Identifier. http://id.nlm.nih.gov/mesh/ ...
MeSH Browser
Lyases [D08.811.520] * Carbon-Nitrogen Lyases [D08.811.520.232] * Amidine-Lyases [D08.811.520.232.300] * Adenylosuccinate Lyase ... Amidine-Lyases Preferred Term Term UI T058744. Date01/01/1999. LexicalTag NON. ThesaurusID NLM (1998). ... Amidine-Lyases Preferred Concept UI. M0029322. Registry Number. EC 4.3.2.-. Scope Note. These enzymes catalyze the elimination ... Amidine-Lyases. Tree Number(s). D08.811.520.232.300. Unique ID. D019760. RDF Unique Identifier. http://id.nlm.nih.gov/mesh/ ...
Lyase
EC 4.1 includes lyases that cleave carbon-carbon bonds, such as decarboxylases (EC 4.1.1), aldehyde lyases (EC 4.1.2), oxo acid ... EC 4.5 includes lyases that cleave carbon-halide bonds. *EC 4.6 includes lyases that cleave phosphorus-oxygen bonds, such as ... For the language, see Lyase language.. In biochemistry, a lyase is an enzyme that catalyzes the breaking (an "elimination" ... Lyases are classified as EC 4 in the EC number classification of enzymes. Lyases can be further classified into seven ...
Solyc04g072940.4.1 details
IntEnz - EC 4.3.2.8
MESH TREE NUMBER CHANGES - 2004 MeSH
D8.811.464.259.200 Amidine-Lyases D8.586.520.232.300 D8.811.520.232.300 Amidinotransferases D8.586.913.555.150 D8.811.913.555. ... G11.427.792.560.180 Chondroitin ABC Lyase D8.586.520.241.700.350.500.500 D8.811.520.241.700.350.500.500 Chondroitin Lyases ... D8.811.913.200 Aldehyde-Lyases D8.586.520.224.62 D8.811.520.224.62 Aldose-Ketose Isomerases D8.586.399.475.200 D8.811.399.475. ... G9.188.229.552 Lyases D8.586.520 D8.811.520 Lymecycline D4.615.638.638.900.450 Lymnaea B1.644.776.645 B1.500.644.776.645 Lymph ...
Temperature Controlled Chiller for Grain Storage
The level of amidine functionality is dependent on hydrolysis conditions such as time, temperature, caustic amount, and other ... The pH-Ce Approved Hyaluronidase for Dissolving Dermal Filler Hyaluronic Acid Lyase. Levels from 0.5% to 100% polymer,Rising ... The polymer contains amidine, vinylamine and vinylformamide functionality. Available from Hercules Incorporated as ... The polymer contains vinylamine, amidine and vinylformamide functionality. Available from Hercules Incorporated as Hercobond® ...
TERM
Amidine-Lyases Amidines Amidinotransferases Amido Black Amidohydrolases Amidophosphoribosyltransferase Amifostine Amikacin ... Carbon-Nitrogen Lyases Carbon-Oxygen Ligases Carbon-Oxygen Lyases Carbon-Sulfur Ligases Carbon-Sulfur Lyases Carbonated ... Chondroitin ABC Lyase Chondroitin Lyases Chondroitin Sulfate Proteoglycans Chondroitin Sulfates Chondroitinases and Chondroitin ... Lyase DNA-Activated Protein Kinase DNA-Binding Proteins DNA-Cytosine Methylases DNA-Directed DNA Polymerase DNA-Directed RNA ...
Classification-Schedules
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The level of amidine functionality is dependent on hydrolysis conditions such as time, temperature, caustic amount, and other ... Ce Approved Hyaluronidase for Dissolving Dermal Filler Hyaluronic Acid Lyase. WO2005083174A1. 2005-09-09. Rising Stem Resilient ... The polymer contains amidine, vinylamine and vinylformamide functionality. Available from Hercules Incorporated as ... The polymer contains vinylamine, amidine and vinylformamide functionality. Available from Hercules Incorporated as Hercobond® ...
Proximal Tubule Transcriptomic Database
Also capable of catalyzing the synthesis of a range of neuroactive guanidino compounds by utilizing alternative amidine donors ... "hydroxymethylglutaryl-CoA lyase, mitochondrial precursor" Hmgcl Rattus norvegicus Involved in the catabolism of branched amino ... 058683 6.72 ATP-citrate synthase isoform 1 Acly Rattus norvegicus ATP citrate-lyase is the primary enzyme responsible for the ... intermediate that is dismutated to glyoxylate and the corresponding desglycine peptide amide by the lyase part. C-terminal ...
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... sulfate lyase acharan sulfate lyase 1 acharan sulfate lyase 2 acharan sulfate lyases acharan sulphate acharan sulphate lyase ... amidations amidazine amidazophen amide amidefrine amidephrine amidepin amidepine amides amidic amidination amidine amidines ... argininosuccinate lyase argininosuccinate lyase deficiencies argininosuccinate lyase deficiency argininosuccinate lyases ... acharan sulphate lyase 1 acharan sulphate lyase 2 acharan sulphate lyases Achard-Thiers syndrome Achard-Thiers syndromes ...
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Polymer OPN further enhanced the phagocytosis of aliphatic amine and aldehyde amidine microspheres. Taken together, these ... and it is degraded through cleavage by sphingosine lyase to form palmitaldehyde and phosphoethanolamine or through ... aldehyde amidine, carboxyl and aliphatic amine) which were coated with either serum albumin, immunoglobulin, monomer OPN or ...
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... sulfate lyase acharan sulfate lyase 1 acharan sulfate lyase 2 acharan sulfate lyases acharan sulphate acharan sulphate lyase ... amidations amidazine amidazophen amide amidefrine amidephrine amidepin amidepine amides amidic amidination amidine amidines ... argininosuccinate lyase argininosuccinate lyase deficiencies argininosuccinate lyase deficiency argininosuccinate lyases ... acharan sulphate lyase 1 acharan sulphate lyase 2 acharan sulphate lyases Achard-Thiers syndrome Achard-Thiers syndromes ...
M3i - IBMC - Institut de biologie Moléculaire et Cellulaire- Strasbourg
Résumé , BibTeX , Étiquettes: *RNA, cerevisiae, Cloning, Fractions/metabolism, Fungal, Fungal/metabolism, Govt, Hydro-Lyases/ ... Résumé , BibTeX , Étiquettes: *Cell, *DNA, &, Adenosylmethionine, Amidines/pharmacology, Caco-2, Cells, Decarboxylase/ ... keywords = {*RNA, cerevisiae, Cloning, Fractions/metabolism, Fungal, Fungal/metabolism, Govt, Hydro-Lyases/biosynthesis/ ... Lyase/*chemistry, Models, Molecular, Non-U.S., Oxygenases/chemistry, P.H.S., Phylogeny, Protein, Proteins/*chemistry, Secondary ...
Ceramidases. Medical search
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The level of amidine functionality is dependent on hydrolysis conditions such as time, temperature, caustic amount, and other ... Ce Approved Hyaluronidase for Dissolving Dermal Filler Hyaluronic Acid Lyase. *Silicone Cartoon Schoolbag Shape Coin Purse ... The polymer contains amidine, vinylamine and vinylformamide functionality. Available from Hercules Incorporated as ... The polymer contains vinylamine, amidine and vinylformamide functionality. Available from Hercules Incorporated as Hercobond® ...
2021 : WestminsterResearch
Peptidylarginine Deiminase Inhibitor Application, Using Cl-Amidine, PAD2, PAD3 and PAD4 Isozyme-Specific Inhibitors in ... Novel Inhibitors for Isocitrate Lyase as a Potent Antitubercular Agent for Mycobacterium Tuberculosis ... Controlled Delivery of Pan-PAD-Inhibitor Cl-Amidine Using Poly(3-Hydroxybutyrate) Microspheres. ... Controlled Delivery of Pan-PAD-Inhibitor Cl-Amidine Using Poly(3-Hydroxybutyrate) Microspheres ...
Amino acid | a2bchem.com
boronic acids, carboxylic acids, imidazoles, thiazoles, azoles, indoles, oxindoles, pyridines, heterocycles, bormides, fluoro compounds, amines, aldehydes, isoquinolines, nitro compounds, trifluoroborates, PEG linkers, inhibitors, amino acids and peptides, catalysts and ligands, custom synthesis , other organics and fine chemicals supplier.
Product Index | a2bchem.com
boronic acids, carboxylic acids, imidazoles, thiazoles, azoles, indoles, oxindoles, pyridines, heterocycles, bormides, fluoro compounds, amines, aldehydes, isoquinolines, nitro compounds, trifluoroborates, PEG linkers, inhibitors, amino acids and peptides, catalysts and ligands, custom synthesis , other organics and fine chemicals supplier.
Product Index | a2bchem.com
boronic acids, carboxylic acids, imidazoles, thiazoles, azoles, indoles, oxindoles, pyridines, heterocycles, bormides, fluoro compounds, amines, aldehydes, isoquinolines, nitro compounds, trifluoroborates, PEG linkers, inhibitors, amino acids and peptides, catalysts and ligands, custom synthesis , other organics and fine chemicals supplier.
HMGCR | a2bchem.com
boronic acids, carboxylic acids, imidazoles, thiazoles, azoles, indoles, oxindoles, pyridines, heterocycles, bormides, fluoro compounds, amines, aldehydes, isoquinolines, nitro compounds, trifluoroborates, PEG linkers, inhibitors, amino acids and peptides, catalysts and ligands, custom synthesis , other organics and fine chemicals supplier.
Product Index | a2bchem.com
boronic acids, carboxylic acids, imidazoles, thiazoles, azoles, indoles, oxindoles, pyridines, heterocycles, bormides, fluoro compounds, amines, aldehydes, isoquinolines, nitro compounds, trifluoroborates, PEG linkers, inhibitors, amino acids and peptides, catalysts and ligands, custom synthesis , other organics and fine chemicals supplier.
Carbon-Nitrogen Lyases1
- Subclasses are the AMMONIA-LYASES, the AMIDINE-LYASES, the amine-lyases, and other carbon-nitrogen lyases. (uchicago.edu)
Descriptor1
- Argininosuccinate Lyase" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (harvard.edu)
Profiles2
- This graph shows the total number of publications written about "Argininosuccinate Lyase" by people in Harvard Catalyst Profiles by year, and whether "Argininosuccinate Lyase" was a major or minor topic of these publication. (harvard.edu)
- Below are the most recent publications written about "Argininosuccinate Lyase" by people in Profiles. (harvard.edu)
Cleave carbon-nitrogen bonds1
- This enzyme belongs to the family of lyases , specifically ammonia lyases, which cleave carbon-nitrogen bonds. (wikipedia.org)
Ammonia4
- Aspartate ammonia-lyase homotetramer, Bacillus sp. (wikipedia.org)
- The systematic name of this enzyme class is L-aspartate ammonia-lyase (fumarate-forming) . (wikipedia.org)
- Other names in common use include aspartase , fumaric aminase , L-aspartase , and L-aspartate ammonia-lyase . (wikipedia.org)
- These enzymes catalyze the elimination of ammonia from amidines with the formation of a double bond. (nih.gov)
Systematic1
- Systematic names are formed as " substrate group-lyase . (ipfs.io)
Catalyzes1
- In biochemistry , a lyase is an enzyme that catalyzes the breaking (an "elimination" reaction ) of various chemical bonds by means other than hydrolysis (a "substitution" reaction ) and oxidation , often forming a new double bond or a new ring structure. (ipfs.io)
Elimination1
- A combination of both an elimination and a Michael addition is seen in O-succinylhomoserine (thiol)-lyase (MetY or MetZ) which catalyses first the γ-elimination of O-succinylhomoserine (with succinate as a leaving group) and then the addition of sulfide to the vinyl intermediate, this reaction was first classified as a lyase (EC 4.2.99.9), but was then reclassified as a transferase (EC 2.5.1.48). (ipfs.io)
Article1
- This lyase article is a stub . (wikipedia.org)