3-methyl-2-oxobutanoate hydroxymethyltransferase

From Wikipedia, the free encyclopedia

In enzymology, a 3-methyl-2-oxobutanoate hydroxymethyltransferase (EC 2.1.2.11) is an enzyme that catalyzes the chemical reaction

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H₂O $\rightleftharpoons$ tetrahydrofolate + 2-dehydropantoate

The 3 substrates of this enzyme are 5,10-methylenetetrahydrofolate, 3-methyl-2-oxobutanoate, and H₂O, whereas its two products are tetrahydrofolate and 2-dehydropantoate.

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.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] 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.

[edit] References

IUBMB entry for 2.1.2.11
BRENDA references for 2.1.2.11 (Recommended.)
PubMed references for 2.1.2.11
PubMed Central references for 2.1.2.11
Google Scholar references for 2.1.2.11
Powers SG, Snell EE (1976). "Ketopantoate hydroxymethyltransferase. II. Physical, catalytic, and regulatory properties". J. Biol. Chem. 251: 3786–93. PMID 6463.
Teller JH, Powers SG, Snell EE (1976). "Ketopantoate hydroxymethyltransferase. I. Purification and role in pantothenate biosynthesis". J. Biol. Chem. 251: 3780–5. PMID 776976.