(R,R)-butanediol dehydrogenase

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(R,R)-butanediol dehydrogenase
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Meso-2,3-butanediol dehydrogenase from Klebsiella pneumoniae. PDB 1geg
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EC no. 1.1.1.4
CAS no. 37250-09-2
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In enzymology, a (R,R)-butanediol dehydrogenase (EC 1.1.1.4) is an enzyme that catalyzes the chemical reaction

(R,R)-butane-2,3-diol + NAD+ (R)-acetoin + NADH + H+

Thus, the two substrates of this enzyme are (R,R)-butane-2,3-diol and NAD+, whereas its 3 products are (R)-acetoin, NADH, and H+.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (R,R)-butane-2,3-diol:NAD+ oxidoreductase. Other names in common use include butyleneglycol dehydrogenase, D-butanediol dehydrogenase, D-(−)-butanediol dehydrogenase, butylene glycol dehydrogenase, diacetyl (acetoin) reductase, D-aminopropanol dehydrogenase, D-aminopropanol dehydrogenase, 1-amino-2-propanol dehydrogenase, 2,3-butanediol dehydrogenase, D-1-amino-2-propanol dehydrogenase, (R)-diacetyl reductase, (R)-2,3-butanediol dehydrogenase, D-1-amino-2-propanol:NAD+ oxidoreductase, 1-amino-2-propanol oxidoreductase, and aminopropanol oxidoreductase. This enzyme participates in butanoic acid metabolism.

Related Research Articles

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

Acetoin, also known as 3-hydroxybutanone or acetyl methyl carbinol, is an organic compound with the formula CH3CH(OH)C(O)CH3. It is a colorless liquid with a pleasant, buttery odor. It is chiral. The form produced by bacteria is (R)-acetoin.

Aromatic-ring-hydroxylating dioxygenases (ARHD) incorporate two atoms of dioxygen (O2) into their substrates in the dihydroxylation reaction. The product is (substituted) cis-1,2-dihydroxycyclohexadiene, which is subsequently converted to (substituted) benzene glycol by a cis-diol dehydrogenase.

In enzymology, a cholest-5-ene-3β,7α-diol 3β-dehydrogenase (EC 1.1.1.181) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">D-xylulose reductase</span>

In enzymology, a D-xylulose reductase (EC 1.1.1.9) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Glycerate dehydrogenase</span>

In enzymology, a glycerate dehydrogenase (EC 1.1.1.29) is an enzyme that catalyzes the chemical reaction

In enzymology, a L-glycol dehydrogenase (EC 1.1.1.185) is an enzyme that catalyzes the chemical reaction

In enzymology, a 1,3-propanediol dehydrogenase (EC 1.1.1.202) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">3alpha(or 20beta)-hydroxysteroid dehydrogenase</span> Class of enzymes

In enzymology, a 3alpha(or 20beta)-hydroxysteroid dehydrogenase (EC 1.1.1.53) is an enzyme that catalyzes the chemical reaction

In enzymology, a (R)-aminopropanol dehydrogenase (EC 1.1.1.75) is an enzyme that catalyzes the chemical reaction

In enzymology, a (S,S)-butanediol dehydrogenase (EC 1.1.1.76) is an enzyme that catalyzes the chemical reaction

In enzymology, a cis-1,2-dihydrobenzene-1,2-diol dehydrogenase (EC 1.3.1.19) is an enzyme that catalyzes the chemical reaction

In enzymology, a cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase (EC 1.3.1.56) is an enzyme that catalyzes the chemical reaction

In enzymology, a mycothiol-dependent formaldehyde dehydrogenase (EC 1.1.1.306) is an enzyme that catalyzes the chemical reaction

In enzymology, a ferric-chelate reductase (EC 1.16.1.7) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">NAD(P)H dehydrogenase (quinone)</span>

In enzymology, a NAD(P)H dehydrogenase (quinone) (EC 1.6.5.2) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Short-chain dehydrogenase</span>

The short-chain dehydrogenases/reductases family (SDR) is a very large family of enzymes, most of which are known to be NAD- or NADP-dependent oxidoreductases. As the first member of this family to be characterised was Drosophila alcohol dehydrogenase, this family used to be called 'insect-type', or 'short-chain' alcohol dehydrogenases. Most members of this family are proteins of about 250 to 300 amino acid residues. Most dehydrogenases possess at least 2 domains, the first binding the coenzyme, often NAD, and the second binding the substrate. This latter domain determines the substrate specificity and contains amino acids involved in catalysis. Little sequence similarity has been found in the coenzyme binding domain although there is a large degree of structural similarity, and it has therefore been suggested that the structure of dehydrogenases has arisen through gene fusion of a common ancestral coenzyme nucleotide sequence with various substrate specific domains.

Acetoin dehydrogenase (EC 2.3.1.190, acetoin dehydrogenase complex, acetoin dehydrogenase enzyme system, AoDH ES) is an enzyme with systematic name acetyl-CoA:acetoin O-acetyltransferase. This enzyme catalyses the following chemical reaction

Diacetyl reductase ((R)-acetoin forming) (EC 1.1.1.303, (R)-acetoin dehydrogenase) is an enzyme with systematic name (R)-acetoin:NAD+ oxidoreductase. This enzyme catalyses the following chemical reaction

<span class="mw-page-title-main">Diacetyl reductase ((S)-acetoin forming)</span>

Diacetyl reductase ((S)-acetoin forming) (EC 1.1.1.304, (S)-acetoin dehydrogenase) is an enzyme with systematic name (S)-acetoin:NAD+ oxidoreductase. This enzyme catalyses the following chemical reaction

<span class="mw-page-title-main">NADH:ubiquinone reductase (non-electrogenic)</span> Class of enzymes

NADH:ubiquinone reductase (non-electrogenic) (EC 1.6.5.9, NDH-2, ubiquinone reductase, coenzyme Q reductase, dihydronicotinamide adenine dinucleotide-coenzyme Q reductase, DPNH-coenzyme Q reductase, DPNH-ubiquinone reductase, NADH-coenzyme Q oxidoreductase, NADH-coenzyme Q reductase, NADH-CoQ oxidoreductase, NADH-CoQ reductase) is an enzyme with systematic name NADH:ubiquinone oxidoreductase. This enzyme catalyses the following chemical reaction:

References


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