Tartronate-semialdehyde synthase

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tartronate-semialdehyde synthase
Identifiers
EC number4.1.1.47
CAS number9027-24-1
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

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.

References[edit]

  • 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 (3): 593–4. doi:10.1016/0006-3002(56)90208-6. PMID 13363977.