3-dehydro-L-gulonate-6-phosphate decarboxylase

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3-dehydro-L-gulonate-6-phosphate decarboxylase
Identifiers
EC number 4.1.1.85
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

In enzymology, a 3-dehydro-L-gulonate-6-phosphate decarboxylase (EC 4.1.1.85) is an enzyme that catalyzes the chemical reaction

3-dehydro-L-gulonate 6-phosphate + H+ L-xylulose 5-phosphate + CO2

Thus, the two substrates of this enzyme are 3-dehydro-L-gulonate 6-phosphate and H+, whereas its two products are L-xylulose 5-phosphate 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 3-dehydro-L-gulonate-6-phosphate carboxy-lyase (L-xylulose-5-phosphate-forming). Other names in common use include 3-keto-L-gulonate 6-phosphate decarboxylase, UlaD, SgaH, SgbH, KGPDC, and 3-dehydro-L-gulonate-6-phosphate carboxy-lyase. This enzyme participates in pentose and glucuronate interconversions and ascorbate and aldarate metabolism.

References[edit]

  • Yew WS, Gerlt JA (January 2002). "Utilization of L-ascorbate by Escherichia coli K-12: assignments of functions to products of the yjf-sga and yia-sgb operons". Journal of Bacteriology. 184 (1): 302–6. doi:10.1128/JB.184.1.302-306.2002. PMC 134747. PMID 11741871.
  • Wise E, Yew WS, Babbitt PC, Gerlt JA, Rayment I (March 2002). "Homologous (beta/alpha)8-barrel enzymes that catalyze unrelated reactions: orotidine 5'-monophosphate decarboxylase and 3-keto-L-gulonate 6-phosphate decarboxylase". Biochemistry. 41 (12): 3861–9. doi:10.1021/bi012174e. PMID 11900527.