EC Number   |
Subunits |
Reference |
|---|
    1.4.1.18 | ? |
x * 42239, deduced from nucleotide sequence |
654286 |
| 1.4.1.18 | dimer |
2 * 39000, gel filtration, SDS-PAGE |
391527 |
| 1.4.1.18 | dimer |
2 * 42600, recombinant enzyme, SDS-PAGE, 2 * 42089, amino acid sequence |
-, 712491 |
| 1.4.1.18 | dimer |
after preincubation with NAD+ without L-lysine |
391532, 391533 |
| 1.4.1.18 | hexamer |
6 * 40000 Da, gel filtration, enzyme elutes as a hexamer when a high concentration of L-lysine (10 mM) is supplemented to both the enzyme and the elution buffer |
702864 |
| 1.4.1.18 | homodimer |
2 * 40000 Da, gel filtration |
702864 |
| 1.4.1.18 | More |
each monomer consists of a Rossmann fold domain and a C-terminal catalytic domain, and the fold of the catalytic domain showed similarity to that of saccharopine reductase, three-dimensional structure of the enzyme, structure comparisons, overview. Subunit A active site contains a sulfate ion not seen in subunit B. Consequently, subunit A adopts a closed conformation, whereas subunit B adopts an open one. In each subunit, one NAD molecule was bound to the active site in an anti-conformation, indicating that the enzyme makes use of pro-R-specific hydride transfer between the two hydrides at C-4 of NADH with type A specificity |
-, 712491 |
| 1.4.1.18 | tetramer |
gel filtration and centrifugation in presence of L-lysine |
391532, 391533 |
