1. Structural studies

2. References

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

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H₂O 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.

Structural studies

As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes {{PDB link|1M3U}}, {{PDB link|1O66}}, {{PDB link|1O68}}, and {{PDB link|1OY0}}.

References

• {{cite journal | vauthors = Powers SG, Snell EE | date = 1976 | title = Ketopantoate hydroxymethyltransferase. II. Physical, catalytic, and regulatory properties | journal = J. Biol. Chem. | volume = 251 | pages = 3786–93 | pmid = 6463 | issue = 12 }}
• {{cite journal | vauthors = Teller JH, Powers SG, Snell EE | date = 1976 | title = Ketopantoate hydroxymethyltransferase. I. Purification and role in pantothenate biosynthesis | journal = J. Biol. Chem. | volume = 251 | pages = 3780–5 | pmid = 776976 | issue = 12 }}

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