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GDP-mannose 6-dehydrogenase

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GDP-mannose 6-dehydrogenase
Identifiers
EC no.1.1.1.132
CAS no.37250-63-8
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

In enzymology, a GDP-mannose 6-dehydrogenase (EC 1.1.1.132) is an enzyme that catalyzes the chemical reaction

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

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As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1MFZ, 1MUU, and 1MV8.

References

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  1. ^ 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

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