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Overview
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Pathways & interactions
Mannitol dehydrogenase, C-terminal (IPR013118)
Short name: Mannitol_DH_C
Overlapping homologous superfamilies
Domain relationships
None.
Description
Long-chain mannitol dehydrogenases are a group of secondary alcohol dehydrogenases that differ from other alcohol or polyol dehydrogenases in that they do not utilise Zn(2+) or other metal cofactors and do not contain a conserved catalytic tyrosine residue. The proteins in this family that have been studied are monomeric enzymes of ~54 kDa and include:
- Mannitol-1-phosphate 5-dehydrogenase (EC:1.1.1.17) [PMID: 11160802]
- Mannitol 2-dehydrogenase (EC:1.1.1.67) [PMID: 8254318]
- D-arabinitol 4-dehydrogenase (EC:1.1.1.11) [PMID: 9639934]
- Altronate oxidoreductase (EC:1.1.1.58)
- D-mannonate oxidoreductase (EC:1.1.1.57)
This entry represents the C-terminal substrate-binding domain of long-chain mannitol dehydrogenases. This domain is primarily alpha-helical in nature, being composed of eleven helices and a small beta hairpin [PMID: 12196534]. Most of the residues implicated in substrate binding are located within this region, and a conserved lysine residue is thought to act as a proton acceptor during catalysis.
GO terms
Biological Process
GO:0055114 oxidation-reduction process
Molecular Function
GO:0050662 coenzyme binding
GO:0016491 oxidoreductase activity
Cellular Component
No terms assigned in this category.
Contributing signatures
- PF08125 (Mannitol_dh_C)