EC Tree |
1. Oxidoreductases |
1.1 Acting on the CH-OH group of donors |
1.1.1 With NAD+ or NADP+ as acceptor |
ID: | 1.1.1.67 | ||
---|---|---|---|
Description: | Mannitol 2-dehydrogenase. | ||
Alternative Name: |
Mannitol dehydrogenase. | ||
Prosite: | PDOC00751; | ||
PDB: |
|
||
Cath: | 1.10.1040.10; 3.40.50.720; |
Click one PDB to see exact 3D structure provided by NGL.
Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.UniProtKB Enzyme Link: | UniProtKB 1.1.1.67 |
BRENDA Enzyme Link: | BRENDA 1.1.1.67 |
KEGG Enzyme Link: | KEGG1.1.1.67 |
BioCyc Enzyme Link: | BioCyc 1.1.1.67 |
ExPASy Enzyme Link: | ExPASy1.1.1.67 |
EC2PDB Enzyme Link: | EC2PDB 1.1.1.67 |
ExplorEnz Enzyme Link: | ExplorEnz 1.1.1.67 |
PRIAM enzyme-specific profiles Link: | PRIAM 1.1.1.67 |
IntEnz Enzyme Link: | IntEnz 1.1.1.67 |
MEDLINE Enzyme Link: | MEDLINE 1.1.1.67 |
RHEA:12084 | D-mannitol + NAD(+) = D-fructose + H(+) + NADH |
RULE(radius=1) | ([*:1]-[CH;+0:2](-[*:3])-[*:4].[*:5]-[OH;+0:6]).[*:7]-[n+;H0:8]1:[cH;+0:9]:[cH;+0:10]:[cH;+0:11]:[c;H0;+0:12](-[*:13]):[cH;+0:14]:1>>[*:7]-[N;H0;+0:8]1-[CH;+0:9]=[CH;+0:10]-[CH2;+0:11]-[C;H0;+0:12](-[*:13])=[CH;+0:14]-1.[*:5]-[O;H0;+0:6]-[C;H0;+0:2](-[*:1])(-[*:3])-[*:4] |
Reaction | ![]() |
Core-to-Core |
Title | Authors | Date | PubMed ID |
---|---|---|---|
Enzymes of mannitol metabolism in the human pathogenic fungus Aspergillus fumigatus--kinetic properties of mannitol-1-phosphate 5-dehydrogenase and mannitol 2-dehydrogenase, and their physiological implications. | Krahulec S, Armao GC, Klimacek M, Nidetzky B | 2011 Apr | 21299839 |
The oxyanion hole of Pseudomonas fluorescens mannitol 2-dehydrogenase: a novel structural motif for electrostatic stabilization in alcohol dehydrogenase active sites. | Klimacek M, Nidetzky B | 2009 Dec 23 | 19857201 |