Mannitol dehydrogenase
In enzymology, a mannitol dehydrogenase (EC 1.1.1.255) is an enzyme that catalyzes the chemical reaction
- D-mannitol + NAD+ D-mannose + NADH + H+
| mannitol dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.1.1.255 | ||||||||
| CAS number | 144941-29-7 | ||||||||
| 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 | ||||||||
| |||||||||
Thus, the two substrates of this enzyme are D-mannitol and NAD+, whereas its 3 products are D-mannose, 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 mannitol:NAD+ 1-oxidoreductase. Other names in common use include MTD, and NAD+-dependent mannitol dehydrogenase.
References
- Stoop JM, Pharr DM (1992). "Partial purification and characterization of mannitol: mannose 1-oxidoreductase from celeriac (Apium graveolens var. rapaceum) roots". Arch. Biochem. Biophys. 298 (2): 612–9. doi:10.1016/0003-9861(92)90456-7. PMID 1416989.
- Stoop JM, Williamson JD, Conkling MA, Pharr DM (1995). "Purification of NAD-dependent mannitol dehydrogenase from celery suspension cultures". Plant Physiol. 108 (3): 1219–25. doi:10.1104/pp.108.3.1219. PMC 157476. PMID 7630943.
- Williamson JD, Stoop JM, Massel MO, Conkling MA, Pharr DM (1995). "Sequence analysis of a mannitol dehydrogenase cDNA from plants reveals a function for the pathogenesis-related protein ELI3". Proc. Natl. Acad. Sci. U.S.A. 92 (16): 7148–52. doi:10.1073/pnas.92.16.7148. PMC 41296. PMID 7638158.
- Stoop, JMH, Chilton WS, Pharr DM (1996). "Substrate specificity of the NAD-dependent mannitol dehydrogenase from celery". Phytochemistry. 43 (6): 1145–1150. doi:10.1016/S0031-9422(96)00423-2.
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