L-2-amino-4-chloropent-4-enoate dehydrochlorinase

Last updated
L-2-amino-4-chloropent-4-enoate dehydrochlorinase
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
Search
PMC articles
PubMed articles
NCBI proteins

The enzyme L-2-amino-4-chloropent-4-enoate dehydrochlorinase (EC 4.5.1.4) catalyzes the reaction

L-2-amino-4-chloropent-4-enoate + H2O 2-oxopent-4-enoate + chloride + NH3

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).

Related Research Articles

<span class="mw-page-title-main">Cystathionine gamma-lyase</span> Protein-coding gene in the species Homo sapiens

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

<span class="mw-page-title-main">L-serine ammonia-lyase</span>

The enzyme L-serine ammonia-lyase (EC 4.3.1.17) catalyzes the chemical reaction

<span class="mw-page-title-main">Methionine gamma-lyase</span>

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

<span class="mw-page-title-main">Threonine ammonia-lyase</span>

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

<span class="mw-page-title-main">Tryptophanase</span> Enzyme that converts tryptophan into indole

The enzyme tryptophanase (EC 4.1.99.1) catalyzes the chemical reaction

<span class="mw-page-title-main">2-oxopent-4-enoate hydratase</span> InterPro Family

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

<span class="mw-page-title-main">Chloroalanine</span> Chemical compound

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.

References