Tartronate-semialdehyde synthase
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In enzymology, a tartronate-semialdehyde synthase (EC 4.1.1.47) is an enzyme that catalyzes the chemical reaction
- 2 glyoxylate
tartronate semialdehyde + CO2
Hence, this enzyme has one substrate, glyoxylate, and two products, tartronate semialdehyde and CO2.
This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is glyoxylate carboxy-lyase (dimerizing tartronate-semialdehyde-forming). Other names in common use include tartronate semialdehyde carboxylase, glyoxylate carbo-ligase, glyoxylic carbo-ligase, hydroxymalonic semialdehyde carboxylase, tartronic semialdehyde carboxylase, glyoxalate carboligase, and glyoxylate carboxy-lyase (dimerizing). This enzyme participates in glyoxylate and dicarboxylate metabolism. It has 2 cofactors: FAD, and Thiamin diphosphate.
[edit] References
- IUBMB entry for 4.1.1.47
- BRENDA references for 4.1.1.47 (Recommended.)
- PubMed references for 4.1.1.47
- PubMed Central references for 4.1.1.47
- Google Scholar references for 4.1.1.47
- GUPTA NK, VENNESLAND B (1964). "GLYOXYLATE CARBOLIGASE OF ESCHERICHIA COLI: A FLAVOPROTEIN". J. Biol. Chem. 239: 3787–9. PMID 14257608.
- BARKULIS SS, KRAKOW G (1956). "Conversion of glyoxylate to hydroxypyruvate by extracts of Escherichia coli". Biochim. Biophys. Acta. 21: 593–4. doi:. PMID 13363977.
[edit] External links
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- The CAS registry number for this enzyme class is 9027-24-1.
[edit] Gene Ontology (GO) codes
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