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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 ${\displaystyle \rightleftharpoons }$ 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.

Structural studies

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

References

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

• 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.

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