- Source: Mannitol 2-dehydrogenase
In enzymology, a mannitol 2-dehydrogenase (EC 1.1.1.67) is an enzyme that catalyzes the chemical reaction
D-mannitol + NAD+
⇌
{\displaystyle \rightleftharpoons }
D-fructose + NADH + H+
Thus, the two substrates of this enzyme are D-mannitol and NAD+, whereas its 3 products are D-fructose, 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 D-mannitol:NAD+ 2-oxidoreductase. Other names in common use include D-mannitol dehydrogenase, and mannitol dehydrogenase. This enzyme participates in fructose and mannose metabolism.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1LJ8 and 1M2W.
References
Martinez G, Barker HA, Horecker BL (1963). "A specific mannitol dehydrogenase from Lactobacillus brevis". J. Biol. Chem. 238 (5): 1598–1603. doi:10.1016/S0021-9258(18)81106-1.
Kata Kunci Pencarian:
- Mannitol 2-dehydrogenase
- Mannitol
- Mannitol 2-dehydrogenase (NADP+)
- Mannitol dehydrogenase
- Mannitol dehydrogenase (cytochrome)
- Mannitol-1-phosphate 5-dehydrogenase
- Glyceraldehyde
- Sorbitol-6-phosphate 2-dehydrogenase
- Sorbitol
- D-arabinitol dehydrogenase (NADP+)