EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.5.1.42 | additional information | the role played by the critical active site residue threonine residue is analyzed using mutant having an asparagine or alanine substitution at this position. The mutants show that having an alanine residue at this position lowers the activation barrier for this reaction, increasing the reaction rate | Rhodococcus erythropolis |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.5.1.42 | FMNH2 + NAD+ | Rhodococcus erythropolis | - |
FMN + NADH + H+ | - |
r | |
1.5.1.42 | FMNH2 + NAD+ | Rhodococcus erythropolis IGTS8 / ATCC 53968 | - |
FMN + NADH + H+ | - |
r |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.5.1.42 | Rhodococcus erythropolis | - |
- |
- |
1.5.1.42 | Rhodococcus erythropolis IGTS8 / ATCC 53968 | - |
- |
- |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
1.5.1.42 | FMNH2 + NAD+ = FMN + NADH + H+ | catalytic reaction mechanism with active site Thr residue, hybrid quantum mechanics/molecular mechanics simulation methods, overview | Rhodococcus erythropolis |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.5.1.42 | FMNH2 + NAD+ | - |
Rhodococcus erythropolis | FMN + NADH + H+ | - |
r | |
1.5.1.42 | FMNH2 + NAD+ | - |
Rhodococcus erythropolis IGTS8 / ATCC 53968 | FMN + NADH + H+ | - |
r |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.5.1.42 | DszD | - |
Rhodococcus erythropolis |
1.5.1.42 | NADH-FMN oxidoreductase | - |
Rhodococcus erythropolis |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.5.1.42 | NAD+ | - |
Rhodococcus erythropolis | |
1.5.1.42 | NADH | - |
Rhodococcus erythropolis |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.5.1.42 | additional information | the enzyme structure of DszD enzyme from Rhodococcus erythropolis strain IGTS8 complexed with both NADH and FMN is modeled using the crystal structure of the homologous enzyme 4-hydroxyphenylacetate hydroxylase component C of Sulfolobus tokodaii strain 7, HpaCst, PDB ID 2D37, with a resolution of 1.7 A | Rhodococcus erythropolis |
1.5.1.42 | physiological function | Rhodococcus erythropolis strain IGTS8 metabolizes organic sulfur compounds through a mechanism known as 4S pathway, which involves four enzymes, DszA, DszB, DszC, and DszD. NADH-FMN oxidoreductase DszD occupies a central place on the 4S pathway by catalyzing the formation of the FMNH2 that is used by the two monooxynases in the cycle, DszA and DszC | Rhodococcus erythropolis |