Mannitol dehydrogenase (cytochrome)

mannitol dehydrogenase (cytochrome)
Identifiers
EC no.1.1.2.2
CAS no.37250-78-5
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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PMCarticles
PubMedarticles
NCBIproteins

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

 
Fe3+
Fe2+
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

References

  1. ^ Enzyme 1.1.2.2 at KEGG Pathway Database.
  2. ^ ARCUS AC, EDSON NL (1956). "Polyol dehydrogenases. 2. The polyol dehydrogenases of Acetobacter suboxydans and Candida utilis". Biochem. J. 64 (3): 385–94. doi:10.1042/bj0640385. PMC 1199748. PMID 13373782.
  3. ^ Cho NC, Kim K, Jhon DY (1990). "Purification and characterization of polyol dehydrogenase from Gluconobacter melanogenus". Han'guk Saenghwa Hakhaochi. 23: 172–178.