Threonine aldolase
From Wikipedia, the free encyclopedia
Threonine aldolase
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Identifiers | |
Symbol | THA1P |
Entrez | 390816 |
HUGO | 18004 |
RefSeq | XM_372682 |
Other data | |
Locus | Chr. 17 q25.3 |
In enzymology, a threonine aldolase (EC 4.1.2.5) is an enzyme that catalyzes the chemical reaction
- L-threonine glycine + acetaldehyde
Hence, this enzyme has one substrate, L-threonine, and two products, glycine and acetaldehyde.
This enzyme belongs to the family of lyases, specifically the aldehyde-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is L-threonine acetaldehyde-lyase (glycine-forming). This enzyme is also called L-threonine acetaldehyde-lyase. This enzyme participates in glycine, serine and threonine metabolism. It employs one cofactor, pyridoxal phosphate.
Contents |
[edit] Structural studies
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 1JG8, 1LW4, 1LW5, 1M6S, and 1SVV.
[edit] References
- IUBMB entry for 4.1.2.5
- BRENDA references for 4.1.2.5 (Recommended.)
- PubMed references for 4.1.2.5
- PubMed Central references for 4.1.2.5
- Google Scholar references for 4.1.2.5
- Bell SC and Turner JM (1973). "Bacterial threonine aldolase and serine hydroxymethyltransferase enzyme". Biochem. Soc. Trans. 1: 678–681.
- KARASEK MA, GREENBERG DM (1957). "Studies on the properties of threonine aldolases". J. Biol. Chem. 227: 191–205. PMID 13449064.
- Kumagai H, Nagate T, Yoshida H, Yamada H (1972). "Threonine aldolase from Candida humicola. II. Purification, crystallization and properties". Biochim. Biophys. Acta. 258: 779–90. PMID 5017702.
[edit] External links
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- The CAS registry number for this enzyme class is 62213-23-4.
[edit] Gene Ontology (GO) codes
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