EC Number   |
General Information |
Reference |
|---|
  1.5.99.B4 | evolution |
opine dehydrogenase (OpnDH) belongs to a group of so-called dye-linked dehydrogenases that catalyze the oxidation of various organic acids, amino acids, and alcohols in the presence of an artificial electron acceptor, such as 2,6-dichloroindophenol, in which FAD and/or FMN is commonly contained as a prosthetic group(s). This enzyme is phylogenetically related to hydrogen cyanide synthase, EC 1.4.99.5, from bacteria, D-hydroxyproline dehydrogenase from bacteria, and L-proline dehydrogenase, EC 1.5.5.2, from archaea. In contrast to Agrobacterium species, PpOpnDH and BjOpnDH genes are located on the chromosome. Flavin-containing OpnDH (the beta-subunit) belongs to the D-amino acid oxidase (DAD) superfamily (pfam01266). An ancestor of this protein family may inherently possess FMN between the alpha- and beta-subunits, and OpnDHtype-1 and OpnDHtype-2 may have acquired the same substrate specificity independently, convergent evolution of OpnDH |
-, 743588 |
| 1.5.99.B4 | evolution |
opine dehydrogenase (OpnDH) belongs to a group of so-called dye-linked dehydrogenases that catalyze the oxidation of various organic acids, amino acids, and alcohols in the presence of an artificial electron acceptor, such as 2,6-dichloroindophenol, in which FAD and/or FMN is commonly contained as a prosthetic group(s). This enzyme is phylogenetically related to hydrogen cyanide synthase, EC 1.4.99.5, from bacteria, D-hydroxyproline dehydrogenase from bacteria, and L-proline dehydrogenase, EC 1.5.5.2, from archaea. In contrast to Agrobacterium species, PpOpnDH and BjOpnDH, genes are located on the chromosome. Pseudomonas putida strain KT2440 very recently acquired this ability by horizontal gene transfer (not plasmid transfer). Convergent evolution of OpnDH |
-, 743588 |
| 1.5.99.B4 | evolution |
two types of ProDHs, alphabetagammadelta, and alpha4beta4 complexes, have been identified from hyperthermophilic archaea, and their alpha-subunits commonly correspond to the gamma-subunit of OpnDH. OpnDH belongs to a group of so-called dye-linked dehydrogenases that catalyze the oxidation of various organic acids, amino acids, and alcohols in the presence of an artificial electron acceptor, such as 2,6-dichloroindophenol, in which FAD and/or FMN is commonly contained as a prosthetic group(s) |
-, 742120 |
| 1.5.99.B4 | malfunction |
loss of the [4Fe-4S] cluster and/or gamma-subunit by itself has no effect on the binding of FAD and FMN. A marked decrease in the activity of the alphabeta mutant appears to be due to the (partial) degradation of the [2Fe-2S] cluster |
-, 742120 |
| 1.5.99.B4 | more |
a poor phylogenetic relationship exists between OdhB1 and OdhB2 in spite of them both functioning as octopine dehydrogenases, which provided clear evidence for the acquisition of novel functions by subunit exchange |
-, 743588 |
| 1.5.99.B4 | more |
the beta-subunit functions as a catalytic subunit by itself |
-, 743588 |
| 1.5.99.B4 | more |
the gamma-subunit by itself is necessary for the adequate binding of FMN and [2Fe-2S], particularly the latter. The removal of the [4Fe-4S] cluster may result in the easier formation of a disulfide bond between the remaining three cysteine residues in [Fe-S]site 1 of the alphabetagammaC61S mutant than in alphabetagamma-wild-type for structural stabilization |
-, 742120 |
| 1.5.99.B4 | physiological function |
a potential physiological role in opine catabolism may be limited to (active) BjOpnDH2 because the OdhA and OdhC proteins preferentially associate with OdhB2 over OdhB1 |
-, 743588 |
