3-methyl-2-oxobutanoate hydroxymethyltransferase

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 tetrahydrofolate + 2-dehydropantoate
3-methyl-2-oxobutanoate hydroxymethyltransferase
Identifiers
EC number2.1.2.11
CAS number56093-17-5
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

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 1M3U, 1O66, 1O68, and 1OY0.

gollark: Files which don't actually exist on-disk but are part of the filesystem which is visible.
gollark: The sandbox behind PotatOS - YAFSS - supports "pseudofiles".
gollark: You can also uninstall PotatOS using an uninstall disk or tape.
gollark: The best part is that if you overnest it it crashes with "too long without yielding"!
gollark: Er, *yes*.

References
    • Powers SG, Snell EE (1976). "Ketopantoate hydroxymethyltransferase. II. Physical, catalytic, and regulatory properties". J. Biol. Chem. 251 (12): 3786–93. PMID 6463.
    • Teller JH, Powers SG, Snell EE (1976). "Ketopantoate hydroxymethyltransferase. I. Purification and role in pantothenate biosynthesis". J. Biol. Chem. 251 (12): 3780–5. PMID 776976.


    This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.