D-serine ammonia-lyase | |||||||||
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Identifiers | |||||||||
EC no. | 4.3.1.18 | ||||||||
CAS no. | 9015-88-7 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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The enzyme D-serine ammonia-lyase (EC 4.3.1.18), with systematic name D-serine ammonia-lyase (pyruvate-forming), catalyzes the chemical reaction
Other names in common use include D-hydroxyaminoacid dehydratase, D-serine dehydrase, D-hydroxy amino acid dehydratase, D-serine hydrolase, D-serine dehydratase (deaminating), D-serine deaminase, and D-serine hydro-lyase (deaminating). This enzyme participates in glycine, serine and threonine metabolism. It employs one cofactor, pyridoxal phosphate.
Serine dehydratase or L-serine ammonia lyase (SDH) is in the β-family of pyridoxal phosphate-dependent (PLP) enzymes. SDH is found widely in nature, but its structural and properties vary among species. SDH is found in yeast, bacteria, and the cytoplasm of mammalian hepatocytes. SDH catalyzes is the deamination of L-serine to yield pyruvate, with the release of ammonia.
The enzyme cystathionine γ-lyase (EC 4.4.1.1, CTH or CSE; also cystathionase; systematic name L-cystathionine cysteine-lyase (deaminating; 2-oxobutanoate-forming)) breaks down cystathionine into cysteine, 2-oxobutanoate (α-ketobutyrate), and ammonia:
The enzyme 3-chloro-D-alanine dehydrochlorinase (EC 4.5.1.2) catalyzes the reaction
The enzyme carbamoyl-serine ammonia-lyase (EC 4.3.1.13) catalyzes the chemical reaction
The enzyme cysteine-S-conjugate β-lyase (EC 4.4.1.13) catalyzes the chemical reaction
The enzyme D-cysteine desulfhydrase (EC 4.4.1.15) catalyzes the chemical reaction
The enzyme diaminopropionate ammonia-lyase (EC 4.3.1.15) catalyzes the chemical reaction
The enzyme Glucosaminate ammonia-lyase (EC 4.3.1.9) catalyzes the chemical reaction
The enzyme homocysteine desulfhydrase (EC 4.4.1.2) catalyzes the chemical reaction
The enzyme L-2-amino-4-chloropent-4-enoate dehydrochlorinase (EC 4.5.1.4) catalyzes the reaction
The enzyme L-cysteate sulfo-lyase (EC 4.4.1.25) catalyzes the reaction
The enzyme L-serine ammonia-lyase (EC 4.3.1.17) catalyzes the chemical reaction
Threonine ammonia-lyase (EC 4.3.1.19, systematic name L-threonine ammonia-lyase (2-oxobutanoate-forming), also commonly referred to as threonine deaminase or threonine dehydratase, is an enzyme responsible for catalyzing the conversion of L-threonine into α-ketobutyrate and ammonia:
The enzyme phosphatidylserine decarboxylase (EC 4.1.1.65) catalyzes the chemical reaction
The enzyme tryptophanase (EC 4.1.99.1) catalyzes the chemical reaction
The enzyme tyrosine phenol-lyase (EC 4.1.99.2) catalyzes the chemical reaction
The enzyme 2-methylcitrate dehydratase (EC 4.2.1.79) catalyzes the chemical reaction
The enzyme altronate dehydratase (EC 4.2.1.7) catalyzes the chemical reaction
The enzyme imidazoleglycerol-phosphate dehydratase (EC 4.2.1.19) catalyzes the chemical reaction
3-hydroxydecanoyl-(acyl-carrier-protein) dehydratase (EC 4.2.1.60, D-3-hydroxydecanoyl-[acyl-carrier protein] dehydratase, 3-hydroxydecanoyl-acyl carrier protein dehydrase, 3-hydroxydecanoyl-acyl carrier protein dehydratase, β-hydroxydecanoyl thioester dehydrase, β-hydroxydecanoate dehydrase, beta-hydroxydecanoyl thiol ester dehydrase, FabA, β-hydroxyacyl-acyl carrier protein dehydratase, HDDase, β-hydroxyacyl-ACP dehydrase, (3R)-3-hydroxydecanoyl-[acyl-carrier-protein] hydro-lyase) is an enzyme with systematic name (3R)-3-hydroxydecanoyl-(acyl-carrier protein) hydro-lyase. This enzyme catalyses the following chemical reaction