Carnitine dehydratase

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carnitine dehydratase
Identifiers
EC no. 4.2.1.89
CAS no. 104382-17-4
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In enzymology, a carnitine dehydratase (EC 4.2.1.89) is an enzyme that catalyzes the chemical reaction

L-carnitine 4-(trimethylammonio)but-2-enoate + H2O

Hence, this enzyme has one substrate, L-carnitine, and two products, 4-(trimethylammonio)but-2-enoate and H2O.

This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is L-carnitine hydro-lyase [4-(trimethylammonio)but-2-enoate-forming]. This enzyme is also called L-carnitine hydro-lyase.

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 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-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

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:

The enzyme 4-(2-carboxyphenyl)-2-oxobut-3-enoate aldolase (EC 4.1.2.34) 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

The enzyme bile-acid 7α-dehydratase (EC 4.2.1.106) catalyzes the chemical reaction

The enzyme ectoine synthase (EC ) catalyzes the chemical reaction

The enzyme L-arabinonate dehydratase (EC 4.2.1.25) catalyzes the chemical reaction

The enzyme L-fuconate dehydratase (EC 4.2.1.68) catalyzes the chemical reaction

The enzyme Lrhamnonate dehydratase (EC 4.2.1.90) catalyzes the chemical reaction

The enzyme (S)-2-methylmalate dehydratase (EC 4.2.1.34) catalyzes the chemical reaction:

trans-o-Hydroxybenzylidenepyruvate hydratase-aldolase (EC 4.1.2.45, 2′-hydroxybenzalpyruvate aldolase, NsaE, tHBPA hydratase-aldolase) is an enzyme with systematic name (3E)-4-(2-hydroxyphenyl)-2-oxobut-3-enoate hydro-lyase. This enzyme catalyses the following chemical reaction

References


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