Biology:3-methyl-2-oxobutanoate hydroxymethyltransferase
| 3-methyl-2-oxobutanoate hydroxymethyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.1.2.11 | ||||||||
| CAS number | 56093-17-5 | ||||||||
| 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 | ||||||||
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In enzymology, a 3-methyl-2-oxobutanoate hydroxymethyltransferase (EC 2.1.2.11) is an enzyme that catalyzes the chemical reaction
- REDIRECT Template:Chemical reaction
The enzyme converts α-ketoisovaleric acid into ketopantoic acid by hydroxymethylation. The CH
2OH is transferred from the cofactor 5,10-methylenetetrahydrofolate (5,10-CH2-THF), which is converted to tetrahydrofolate (THF).[1][2][3]
This enzyme belongs to the family of transferases that transfer one-carbon groups, specifically the hydroxymethyl-, formyl- and related transferases. The systematic name of this enzyme class is 5,10-methylenetetrahydrofolate:3-methyl-2-oxobutanoate hydroxymethyltransferase. Other names in common use include alpha-ketoisovalerate hydroxymethyltransferase, dehydropantoate hydroxymethyltransferase, ketopantoate hydroxymethyltransferase, oxopantoate hydroxymethyltransferase, 5,10-methylene tetrahydrofolate:alpha-ketoisovalerate, and hydroxymethyltransferase. This enzyme participates in pantothenate and coa biosynthesis.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1M3U, 1O66, 1O68, and 1OY0.
References
- ↑ "Ketopantoate hydroxymethyltransferase. II. Physical, catalytic, and regulatory properties". J. Biol. Chem. 251 (12): 3786–93. 1976. doi:10.1016/S0021-9258(17)33413-0. PMID 6463.
- ↑ "Ketopantoate hydroxymethyltransferase. I. Purification and role in pantothenate biosynthesis". J. Biol. Chem. 251 (12): 3780–5. 1976. doi:10.1016/S0021-9258(17)33412-9. PMID 776976.
- ↑ Enzyme 2.1.2.11 at KEGG Pathway Database.
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