GDP-mannose 6-dehydrogenase explained

GDP-mannose 6-dehydrogenase
Ec Number:	1.1.1.132
Cas Number:	37250-63-8
Go Code:	0047919

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

GDP-D-mannose + 2 NAD⁺ + H₂O

\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.^[1]

Structural studies

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

Further reading

• Preiss J . Sugar nucleotide reaction in Arthrobacter. II. Biosynthesis of guanosine diphosphomannuronate . The Journal of Biological Chemistry . 239 . 3127–32 . October 1964 . 14245351 .

Notes and References

1. Selwood T, Jaffe EK . Dynamic dissociating homo-oligomers and the control of protein function . Archives of Biochemistry and Biophysics . 519 . 2 . 131–43 . March 2012 . 22182754 . 3298769 . 10.1016/j.abb.2011.11.020 .