In enzymology, an ADP-L-glycero-D-manno-heptose 6-epimerase (EC 5.1.3.20) is an enzyme that catalyzes the chemical reaction
| ADP-glyceromanno-heptose 6-epimerase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 5.1.3.20 | ||||||||
| CAS no. | 85030-75-7 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
- ADP-D-glycero-D-manno-heptose ADP-L-glycero-D-manno-heptose
Hence, this enzyme has one substrate, ADP-D-glycero-D-manno-heptose, and one product, ADP-L-glycero-D-manno-heptose.
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and derivatives. The systematic name of this enzyme class is ADP-L-glycero-D-manno-heptose 6-epimerase. This enzyme participates in lipopolysaccharide biosynthesis. It employs one cofactor, NADP+ in a direct oxidation mechanism.
Structural studies
editAs of 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1EQ2.
References
edit- Read JA, Ahmed RA, Morrison JP, Coleman WG Jr, Tanner ME (2004). "The Mechanism of the Reaction Catalyzed by ADP-β-L-glycero-D-manno-heptose 6-Epimerase". J. Am. Chem. Soc. 126 (29): 8878–9. doi:10.1021/ja0485659. PMID 15264802.
- Ding L, Seto BL, Ahmed SA, Coleman WG Jr (1994). "Purification and properties of the Escherichia coli K-12 NAD-dependent nucleotide diphosphosugar epimerase, ADP-L-glycero-D-mannoheptose 6-epimerase". J. Biol. Chem. 269 (39): 24384–90. doi:10.1016/S0021-9258(19)51095-X. PMID 7929099.
- Raetz CR (1990). "Biochemistry of endotoxins". Annu. Rev. Biochem. 59: 129–70. doi:10.1146/annurev.bi.59.070190.001021. PMID 1695830.
