In enzymology, a GDP-mannose 6-dehydrogenase (EC 1.1.1.132) is an enzyme that catalyzes the chemical reaction
| GDP-mannose 6-dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.1.1.132 | ||||||||
| CAS no. | 37250-63-8 | ||||||||
| 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 | ||||||||
| |||||||||
- GDP-D-mannose + 2 NAD+ + H2O GDP-D-mannuronate + 2 NADH + 2 H+
The 3 substrates of this enzyme are GDP-D-mannose, NAD+, and H2O, whereas its 3 products are GDP-D-mannuronate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is GDP-D-mannose:NAD+ 6-oxidoreductase. Other names in common use include guanosine diphosphomannose dehydrogenase, GDP-mannose dehydrogenase, guanosine diphosphomannose dehydrogenase, and guanosine diphospho-D-mannose dehydrogenase. This enzyme participates in fructose and mannose metabolism.
This protein may use the morpheein model of allosteric regulation.[1]
Structural studies
editAs of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1MFZ, 1MUU, and 1MV8.
References
edit- ^ Selwood T, Jaffe EK (March 2012). "Dynamic dissociating homo-oligomers and the control of protein function". Archives of Biochemistry and Biophysics. 519 (2): 131–43. doi:10.1016/j.abb.2011.11.020. PMC 3298769. PMID 22182754.
Further reading
edit- Preiss J (October 1964). "Sugar nucleotide reaction in Arthrobacter. II. Biosynthesis of guanosine diphosphomannuronate". The Journal of Biological Chemistry. 239 (10): 3127–32. doi:10.1016/S0021-9258(18)97693-3. PMID 14245351.
