1.1.1.138: mannitol 2-dehydrogenase (NADP+)
This is an abbreviated version!
For detailed information about mannitol 2-dehydrogenase (NADP+), go to the full flat file.
Word Map on EC 1.1.1.138
-
1.1.1.138
-
spindle
-
checkpoint
-
d-fructose
-
kinetochore
-
anaphase
-
cladosporium
-
bub3
-
kinetochore-microtubule
-
1.1.1.67
-
herbarum
-
l-xylulose
-
d-arabinitol
-
gluconobacter
-
jecorina
-
mad3
-
ige-binding
-
hypocrea
-
unattached
-
synthesis
-
analysis
-
biotechnology
- 1.1.1.138
- spindle
-
checkpoint
- d-fructose
- kinetochore
-
anaphase
- cladosporium
- bub3
-
kinetochore-microtubule
-
1.1.1.67
- herbarum
- l-xylulose
- d-arabinitol
- gluconobacter
- jecorina
- mad3
-
ige-binding
- hypocrea
-
unattached
- synthesis
- analysis
- biotechnology
Reaction
Synonyms
Cla h 8, Cla h 8 allergen, D-mannitol 2-dehydrogenase, D-mannitol dehydrogenase, D-mannitol dehydrogenase, NADP-dependent, Gox1432, LRMDH, LXR1, MAD1p, mannitol 2-dehydrogenase, Mannitol 2-dehydrogenase [NADP+], mannitol dehydrogenase, mannitol dehydrogenase (NADP+), mannitol dehydrogenase (nicotinamide dinucleotide phosphate), mannitol dehydrogenase 1, MDH, More, MtDH, NADP+-dependent mannitol dehydrogenase, NADP-dependent mannitol dehydrogenase, NADP-dependent MtDH, NADP-mannitol dehydrogenase, PIG8p, PSLDR, TbMDH
ECTree
Advanced search results
Subunits
Subunits on EC 1.1.1.138 - mannitol 2-dehydrogenase (NADP+)
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
dimer
heterotetramer
-
2 * 43000 + 2 * 34500, SDS-PAGE, both subunits have the same amino-terminal amino acid sequence
homodimer
monomer
tetramer
additional information
-
structure-function analysis of enzyme and the family of polyol-specific long-chain dehydrogenases/reductases. G33 is in the N-terminal coenzyme-binding domain, D230 and K295 are at an interdomain segment contributing to the active site in which K295 likely functions as the catalytic general acid/base
MtDH co-exists as monomer, dimer, and tetramer in solution as detected in Blue native PAGE
dimer
-
2 * 40000, recombinant enzyme, SDS-PAGE, 2 * 37279, recombinant His6-tagged enzyme, mass spectrometry
MtDH co-exists as monomer, dimer, and tetramer in solution as detected in Blue native PAGE
tetramer
-
crystallization data, residues Ser149, Tyr169, Lys173 form a catalytic triad
tetramer
MtDH co-exists as monomer, dimer, and tetramer in solution as detected in Blue native PAGE. Tetramer is rather unstable and easily dissociates and reassociates