2-acetolactate mutase
| 2-acetolactate mutase | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| EC number | 5.4.99.3 | ||||||
| CAS number | 37318-52-8 | ||||||
| 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 | ||||||
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In enzymology, a 2-acetolactate mutase (EC 5.4.99.3) is an enzyme that catalyzes the chemical reaction
- 2-acetolactate
3-hydroxy-3-methyl-2-oxobutanoate
Hence, this enzyme has one substrate, 2-acetolactate, and one product, 3-hydroxy-3-methyl-2-oxobutanoate.
This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring other groups. The systematic name of this enzyme class is 2-acetolactate methylmutase. Other names in common use include acetolactate mutase, and acetohydroxy acid isomerase. This enzyme participates in valine, leucine and isoleucine biosynthesis. It employs one cofactor, ascorbate.
References
- Allaudeen HS, Ramakrishnan T (1968). "Biosynthesis of isoleucine and valine in Mycobacterium tuberculosis H37 Rv". Arch. Biochem. Biophys. 125 (1): 199–209. doi:10.1016/0003-9861(68)90655-3. PMID 4384955.