Dihydroxy-acid dehydratase
| dihydroxy-acid dehydratase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 4.2.1.9 | ||||||||
| CAS number | 9024-32-2 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / EGO | ||||||||
| |||||||||
In enzymology, a dihydroxy-acid dehydratase (EC 4.2.1.9) is an enzyme that catalyzes the chemical reaction
- 2,3-dihydroxy-3-methylbutanoate 3-methyl-2-oxobutanoate + H2O
Hence, this enzyme has one substrate, 2,3-dihydroxy-3-methylbutanoate, and two products, 3-methyl-2-oxobutanoate (α-ketoisovaleric acid) and H2O.
This enzyme participates in valine, leucine and isoleucine biosynthesis and pantothenate and coenzyme A (CoA) biosynthesis.
Nomenclature
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.
References
Further reading
- Kanamori M, Wixom RL (Mar 1963). "Studies in valine biosynthesis. V. Characteristics of the purified dihydroxyacid dehydratase from spinach leaves". The Journal of Biological Chemistry. 238: 998–1005. PMID 13962154.
- Myers JW (May 1961). "Dihydroxy acid dehydrase: an enzyme involved in the biosynthesis of isoleucine and valine". The Journal of Biological Chemistry. 236: 1414–8. PMID 13727223.
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