EC Number   |
Subunits |
Reference |
|---|
   1.1.1.138 | ? |
x * 29000, SDS-PAGE |
285854 |
| 1.1.1.138 | dimer |
2 * 40000, recombinant enzyme, SDS-PAGE, 2 * 37279, recombinant His6-tagged enzyme, mass spectrometry |
667280 |
| 1.1.1.138 | dimer |
MtDH co-exists as monomer, dimer, and tetramer in solution as detected in Blue native PAGE |
724481 |
| 1.1.1.138 | heterotetramer |
2 * 43000 + 2 * 34500, SDS-PAGE, both subunits have the same amino-terminal amino acid sequence |
655118 |
| 1.1.1.138 | homodimer |
2 * 54600, calculated from amino acid sequence |
739923 |
| 1.1.1.138 | homodimer |
2 * 54900, SDS-PAGE |
739923 |
| 1.1.1.138 | monomer |
1 * 36400, SDS-PAGE |
655114 |
| 1.1.1.138 | monomer |
1 * 50000, SDS-PAGE |
-, 285855 |
| 1.1.1.138 | monomer |
MtDH co-exists as monomer, dimer, and tetramer in solution as detected in Blue native PAGE |
724481 |
| 1.1.1.138 | More |
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 |
655224 |
