L-cysteate sulfo-lyase

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L-cysteate sulfo-lyase
Identifiers
EC no. 4.4.1.25
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The enzyme L-cysteate sulfo-lyase (EC 4.4.1.25) catalyzes the reaction

L-cysteate + H2O = hydrogensulfite + pyruvate + NH3 (overall reaction)
(1a) L-cysteate = hydrogensulfite + 2-aminoprop-2-enoate
(1b) 2-aminoprop-2-enoate = 2-iminopropanoate (spontaneous)
(1c) 2-iminopropanoate + H2O = pyruvate + NH3 (spontaneous)

This enzyme belongs to the family of lyases, specifically the class of carbon-sulfur lyases. The systematic name of this enzyme class is L-cysteate bisulfite-lyase (deaminating; pyruvate-forming). Other names in common use include L-cysteate sulfo-lyase (deaminating), and CuyA.

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:

In enzymology, a tryptophan dehydrogenase (EC 1.4.1.19) is an enzyme that catalyzes the chemical reaction

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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 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-2-amino-4-chloropent-4-enoate dehydrochlorinase (EC 4.5.1.4) 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:

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<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:

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

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References