IPR013118
Mannitol dehydrogenase, C-terminal
InterPro entry
Short name | Mannitol_DH_C |
Overlapping homologous superfamilies |
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 ~54kDa and include:
* Mannitol-1-phosphate 5-dehydrogenase (
1.1.1.17* Mannitol-1-phosphate 5-dehydrogenase (
)
[1]* Mannitol 2-dehydrogenase (
)
[2]* D-arabinitol 4-dehydrogenase (
)
[3]* Altronate oxidoreductase (
)
* D-mannonate oxidoreductase (
1.1.1.57* D-mannonate oxidoreductase (
)
These enzymes are mostly found in bacteria, though they are also present in some fungal species.
These enzymes are mostly found in bacteria, though they are also present in some fungal species.
References
1.Molecular analysis of the mannitol operon of Clostridium acetobutylicum encoding a phosphotransferase system and a putative PTS-modulated regulator. Behrens S, Mitchell W, Bahl H. Microbiology (Reading, Engl.) 147, 75-86, (2001). View articlePMID: 11160802
Further reading
4. Crystal structure of Pseudomonas fluorescens mannitol 2-dehydrogenase binary and ternary complexes. Specificity and catalytic mechanism. Kavanagh KL, Klimacek M, Nidetzky B, Wilson DK. J. Biol. Chem. 277, 43433-42, (2002). View articlePMID: 12196534
GO terms
Cross References
ENZYME
Genome Properties
Contributing Member Database Entry
- Pfam:PF08125