Fucosterol-epoxide lyase

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fucosterol-epoxide lyase
Identifiers
EC no. 4.1.2.33
CAS no. 99676-42-3
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The enzyme fucosterol-epoxide lyase (EC 4.1.2.33) catalyzes the chemical reaction

(24R,24′R)-fucosterol epoxide desmosterol + acetaldehyde

This enzyme belongs to the family of lyases, specifically the aldehyde-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is (24R,24'R)-fucosterol-epoxide acetaldehyde-lyase (desmosterol-forming). This enzyme is also called (24R,24'R)-fucosterol-epoxide acetaldehyde-lyase.

Related Research Articles

In biochemistry, a lyase is an enzyme that catalyzes the breaking of various chemical bonds by means other than hydrolysis and oxidation, often forming a new double bond or a new ring structure. The reverse reaction is also possible. For example, an enzyme that catalyzed this reaction would be a lyase:

<span class="mw-page-title-main">Pyruvate decarboxylase</span> Class of enzymes

Pyruvate decarboxylase is an enzyme that catalyses the decarboxylation of pyruvic acid to acetaldehyde. It is also called 2-oxo-acid carboxylase, alpha-ketoacid carboxylase, and pyruvic decarboxylase. In anaerobic conditions, this enzyme is participates in the fermentation process that occurs in yeast, especially of the genus Saccharomyces, to produce ethanol by fermentation. It is also present in some species of fish where it permits the fish to perform ethanol fermentation when oxygen is scarce. Pyruvate decarboxylase starts this process by converting pyruvate into acetaldehyde and carbon dioxide. Pyruvate decarboxylase depends on cofactors thiamine pyrophosphate (TPP) and magnesium. This enzyme should not be mistaken for the unrelated enzyme pyruvate dehydrogenase, an oxidoreductase, that catalyzes the oxidative decarboxylation of pyruvate to acetyl-CoA.

<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:

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<span class="mw-page-title-main">Leukotriene-C4 synthase</span>

The enzyme leukotriene-C4 synthase (EC 4.4.1.20) catalyzes the reaction

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<span class="mw-page-title-main">4-hydroxy-2-oxovalerate aldolase</span> InterPro Family

The enzyme 4-hydroxy-2-oxovalerate aldolase catalyzes the chemical reaction

<span class="mw-page-title-main">Aminocarboxymuconate-semialdehyde decarboxylase</span>

The enzyme aminocarboxymuconate-semialdehyde decarboxylase (EC 4.1.1.45) catalyzes the chemical reaction

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

The enzyme threonine aldolase is an enzyme that catalyzes the chemical reaction

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The enzyme carboxymethyloxysuccinate lyase catalyzes the chemical reaction

The enzyme ethanolamine-phosphate phospho-lyase (EC 4.2.3.2) catalyzes the chemical reaction

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The enzyme 2-hydroxypropyl-CoM lyase (EC 4.4.1.23, epoxyalkane:coenzyme M transferase, epoxyalkane:CoM transferase, epoxyalkane:2-mercaptoethanesulfonate transferase, coenzyme M-epoxyalkane ligase, epoxyalkyl:CoM transferase, epoxypropane:coenzyme M transferase, epoxypropyl:CoM transferase, EaCoMT, 2-hydroxypropyl-CoM:2-mercaptoethanesulfonate lyase (epoxyalkane-ring-forming), (R)-2-hydroxypropyl-CoM 2-mercaptoethanesulfonate lyase (cyclizing, (R)-1,2-epoxypropane-forming)) is an enzyme with systematic name (R)-[or (S)]-2-hydroxypropyl-CoM:2-mercaptoethanesulfonate lyase (epoxyalkane-ring-forming). This enzyme catalyses the following reaction:

References