EC Number |
Subunits |
Reference |
---|
1.5.5.2 | dimer |
- |
-, 743635 |
1.5.5.2 | dimer |
2 * 119000-124000, SDS-PAGE |
392560 |
1.5.5.2 | dimer |
2 * 137000, bifunctional enzyme: proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase, SDS-PAGE |
722591 |
1.5.5.2 | homodimer |
2 * 37000, SDS-PAGE |
724389 |
1.5.5.2 | dimer |
2 * 74401, recombinant MBP-tagged enzyme, sequence calculation, 2 * 71899, recombinant enzyme mutant DELTAABC, sequence calculation |
-, 743834 |
1.5.5.2 | heterooctamer |
4 * 55300 + 4 * 42700, calculated from amino acid sequence |
739932 |
1.5.5.2 | tetramer |
alpha,beta, 2 * 50000 + 2 * 40000, SDS-PAGE |
392570 |
1.5.5.2 | tetramer |
alphabetagammadelta, 1 * 54000 + 1 * 43000 + 1 * 19000 + 1 * 8000, the beta-subunit catalyzes the dye-linked L-proline dehydrogenase reaction by itself, the alpha-subunit exhibts dye-linked NADH dehydrogenase activity, SDS-PAGE |
658668 |
1.5.5.2 | dimer |
domain-swapped dimer with each subunit comprising three domains: a helical dimerization arm, a 120-residue domain containing a three-helix bundle similar to that in the helix-turn-helix superfamily of DNA-binding proteins and a beta/alpha-barrel PRODH domain with a bound lactate inhibitor |
659987 |
1.5.5.2 | More |
homology-based three-dimensional structural modeling of JcProDH, overview |
741642 |