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

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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⁺ $\rightleftharpoons$ 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.

[edit] References

IUBMB entry for 4.1.1.85
BRENDA references for 4.1.1.85 (Recommended.)
PubMed references for 4.1.1.85
PubMed Central references for 4.1.1.85
Google Scholar references for 4.1.1.85
Yew WS, Gerlt JA (2002). "Utilization of L-ascorbate by Escherichia coli K-12: assignments of functions to products of the yjf-sga and yia-sgb operons". J. Bacteriol. 184: 302–6. doi:10.1128/JB.184.1.302-306.2002. PMID 11741871.
Wise E, Yew WS, Babbitt PC, Gerlt JA, Rayment I (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: 3861–9. doi:10.1021/bi012174e. PMID 11900527.