L-2-amino-4-chloropent-4-enoate dehydrochlorinase | |||||||||
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Identifiers | |||||||||
EC no. | 4.5.1.4 | ||||||||
CAS no. | 113066-37-8 | ||||||||
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 L-2-amino-4-chloropent-4-enoate dehydrochlorinase (EC 4.5.1.4) catalyzes the reaction
This enzyme belongs to the family of lyases, specifically the class of carbon-halide lyases. The systematic name of this enzyme class is L-2-amino-4-chloropent-4-enoate chloride-lyase (adding water; deaminating; 2-oxopent-4-enoate-forming). Other names in common use include L-2-amino-4-chloro-4-pentenoate dehalogenase, and L-2-amino-4-chloropent-4-enoate chloride-lyase (deaminating).
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 cysteine-S-conjugate β-lyase (EC 4.4.1.13) catalyzes the chemical reaction
The enzyme D-serine ammonia-lyase (EC 4.3.1.18), with systematic name D-serine ammonia-lyase (pyruvate-forming), 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-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
The enzyme methionine γ-lyase (EC 4.4.1.11, MGL) is in the γ-family of PLP-dependent enzymes. It degrades sulfur-containing amino acids to α-keto acids, ammonia, and thiols:
In enzymology, a S-alkylcysteine lyase is an enzyme that catalyzes the chemical reaction
The enzyme S-carboxymethylcysteine synthase catalyzes the 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:
In enzymology, a 2,6-dioxo-6-phenylhexa-3-enoate hydrolase (EC 3.7.1.8) is an enzyme that catalyzes the chemical reaction
The enzyme 4-oxalocrotonate decarboxylase (EC 4.1.1.77) catalyzes the chemical reaction
The enzyme tryptophanase (EC 4.1.99.1) catalyzes the chemical reaction
The enzyme 2-oxopent-4-enoate hydratase (EC 4.2.1.80) catalyzes the chemical reaction
In enzymology, a carnitine dehydratase (EC 4.2.1.89) is an enzyme that catalyzes the chemical reaction
The enzyme ethanolamine-phosphate phospho-lyase (EC 4.2.3.2) catalyzes the chemical reaction
5-Phosphonooxy-L-lysine phospho-lyase (EC 4.2.3.134, 5-phosphohydroxy-L-lysine ammoniophospholyase, AGXT2L2 (gene)) is an enzyme with systematic name (5R)-5-phosphonooxy-L-lysine phosphate-lyase (deaminating; (S)-2-amino-6-oxohexanoate-forming). This enzyme catalyses the following chemical reaction
Chloroalanine (3-chloroalanine) is an unnatural amino acid with the formula ClCH2CH(NH2)CO2H. It is a white, water-soluble solid. The compound is usually derived from chlorination of serine. The compound is used in the synthesis of other amino acids by replacement of the chloride. Protected forms of the related iodoalanine are also known.