Protein Variants | Comment | Organism |
---|---|---|
additional information | replacement of the wild-type spectator residue of the rate-limiting step of the reduction of FMN to FMNH2 catalysed by DszD and known to play an important role in the reaction energy profile. As replacements, all the naturally occurring amino acids are used, one at a time, using computational methodologies, determination of mutant activities, application of quantum mechanics/molecular mechanics (QM/MM) methods within an ONIOM scheme | Rhodococcus erythropolis |
N33A | site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type | Rhodococcus erythropolis |
N33C | site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type | Rhodococcus erythropolis |
N33D | site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type | Rhodococcus erythropolis |
N33E | site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type | Rhodococcus erythropolis |
N33F | site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type | Rhodococcus erythropolis |
N33G | site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type | Rhodococcus erythropolis |
N33HID | site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type | Rhodococcus erythropolis |
N33HIE | site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type | Rhodococcus erythropolis |
N33HIP | site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type | Rhodococcus erythropolis |
N33I | site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type | Rhodococcus erythropolis |
N33K | site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type | Rhodococcus erythropolis |
N33L | site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type | Rhodococcus erythropolis |
N33M | site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type | Rhodococcus erythropolis |
N33Q | site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type | Rhodococcus erythropolis |
N33R | site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type | Rhodococcus erythropolis |
N33S | site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type | Rhodococcus erythropolis |
N33T | site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type | Rhodococcus erythropolis |
N33V | site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type | Rhodococcus erythropolis |
N33W | site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type | Rhodococcus erythropolis |
N33Y | site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type | Rhodococcus erythropolis |
T62A | site-directed mutagenesis, the mutant shows 7fold increased activity compared to wild-type | Rhodococcus erythropolis |
T62N | site-directed mutagenesis, the mutant shows 5fold increased activity compared to wild-type | Rhodococcus erythropolis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | Gibbs activation and reaction free energies obtained for the hydride transfer by wild-type enzyme | Rhodococcus erythropolis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
FMN + NADH + H+ | Rhodococcus erythropolis | - |
FMNH2 + NAD+ | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rhodococcus erythropolis | Q7DI30 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
FMN + NADH + H+ | - |
Rhodococcus erythropolis | FMNH2 + NAD+ | - |
? |
Synonyms | Comment | Organism |
---|---|---|
DszD | - |
Rhodococcus erythropolis |
NADH-FMN oxidoreductase | - |
Rhodococcus erythropolis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADH | - |
Rhodococcus erythropolis |
General Information | Comment | Organism |
---|---|---|
malfunction | mutation of the critical residue Thr62, T62N and T62A, show a 5 and 7fold increase in catalytic rate, respectively | Rhodococcus erythropolis |
additional information | critical role of the residue in position 62 (threonine) of the DszD sequence in the enzymatic activity. This residue is located near the N5 atom of the isoalloxazine ring of FMN. Structure modelling of wild-type and mutants using quantum mechanics/molecular mechanics (QM/MM) method, and active site as well as substrate binding structure analysis, overview | Rhodococcus erythropolis |
physiological function | DszD from Rhodococcus erythropolis is a NADH-FMN oxidoreductase responsible for supplying FMNH2 to DszA and DszC in the biodesulfurization process of crude oil, the 4S pathway. The rate-limiting step of the reduction of FMN to FMNH2 is a process catalysed by DszD and known to play an important role in the reaction energy profile | Rhodococcus erythropolis |