Dihydroxy-acid dehydratase

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In enzymology, a dihydroxy-acid dehydratase (EC 4.2.1.9) is an enzyme that catalyzes the chemical reaction

2,3-dihydroxy-3-methylbutanoate $\rightleftharpoons$ 3-methyl-2-oxobutanoate + H₂O

Hence, this enzyme has one substrate, 2,3-dihydroxy-3-methylbutanoate, and two products, 3-methyl-2-oxobutanoate 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 2,3-dihydroxy-3-methylbutanoate hydro-lyase (3-methyl-2-oxobutanoate-forming). Other names in common use include acetohydroxyacid dehydratase, alpha,beta-dihydroxyacid dehydratase, 2,3-dihydroxyisovalerate dehydratase, alpha,beta-dihydroxyisovalerate dehydratase, dihydroxy acid dehydrase, DHAD, and 2,3-dihydroxy-acid hydro-lyase. This enzyme participates in valine, leucine and isoleucine biosynthesis and pantothenate and coa biosynthesis.

[edit] References

IUBMB entry for 4.2.1.9
BRENDA references for 4.2.1.9 (Recommended.)
PubMed references for 4.2.1.9
PubMed Central references for 4.2.1.9
Google Scholar references for 4.2.1.9
KANAMORI M, WIXOM RL (1963). "Studies in valine biosynthesis. V. Characteristics of the purified dihydroxyacid dehydratase from spinach leaves". J. Biol. Chem. 238: 998–1005. PMID 14030545.
MYERS JW (1961). "Dihydroxy acid dehydrase: an enzyme involved in the biosynthesis of isoleucine and valine". J. Biol. Chem. 236: 1414–8. PMID 13727223.