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Mannitol dehydrogenase (cytochrome)

Enzyme class From Wikipedia, the free encyclopedia

In enzymology, mannitol dehydrogenase (cytochrome) (EC 1.1.2.2) is an enzyme that catalyzes the chemical reaction

 
Fe3+
Fe2+
Reversible left-right reaction arrow with minor forward substrate(s) from top left, minor forward product(s) to top right, minor reverse substrate(s) from bottom right and minor reverse product(s) to bottom left
Fe3+
Fe2+
 
+ 2 H+
 

The substrate of this enzyme is D-mannitol, which is acted on by two equivalents of the cofactor, ferricytochrome c, which oxidises one of the hydroxy groups to a keto group, giving D-fructose, while the cofactor's iron is reduced.[1][2][3]

This enzyme belongs to the family of oxidoreductases, to be specific those acting on the CH-OH group of donor with a cytochrome as acceptor. The systematic name of this enzyme class is D-mannitol:ferricytochrome-c 2-oxidoreductase. This enzyme is also called polyol dehydrogenase. This enzyme participates in pentose and glucuronate interconversions and fructose and mannose metabolism

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