The enzyme 3-dehydro-L-gulonate-6-phosphate decarboxylase (EC 4.1.1.85) catalyzes the chemical reaction
| 3-dehydro-L-gulonate-6-phosphate decarboxylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 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 | ||||||||
| |||||||||
- 3-dehydro-L-gulonate 6-phosphate + H+ L-xylulose 5-phosphate + 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.
