| mannitol 2-dehydrogenase (NADP+) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.1.1.138 | ||||||||
| CAS no. | 37250-68-3 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a mannitol 2-dehydrogenase (NADP+) (EC 1.1.1.138) is an enzyme that catalyzes the chemical reaction
- D-mannitol + NADP+ D-fructose + NADPH + H+
Thus, the two substrates of this enzyme are D-mannitol and NADP+, whereas its 3 products are D-fructose, NADPH, 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 D-mannitol:NADP+ 2-oxidoreductase. This enzyme is also called mannitol 2-dehydrogenase (NADP+). This enzyme participates in fructose and mannose metabolism.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1H5Q.
References
- Edmundowicz JM, Wriston JC (1963). "Mannitol dehydrogenase from Agaricus campestris". J. Biol. Chem. 238: 3539–41. PMID 14109183.
- Strobel GA; Kosuge T (1965). "Polyol metabolism in Diplodia viticola Desm". Arch. Biochem. Biophys. 109 (3): 622–626. doi:10.1016/0003-9861(65)90409-1. PMID 14320506.
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