2-acetolactate mutase
| 2-acetolactate mutase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 5.4.99.3 | ||||||||
| CAS no. | 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 / QuickGO | ||||||||
| |||||||||
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.