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Literature summary extracted from

  • Ferreira, P.; Sousa, S.F.; Fernandes, P.A.; Ramos, M.J.
    Improving the catalytic power of the DszD enzyme for the biodesulfurization of crude oil and derivatives (2017), Chemistry, 23, 17231-17241 .
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.5.1.42 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
1.5.1.42 N33A site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type Rhodococcus erythropolis
1.5.1.42 N33C site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type Rhodococcus erythropolis
1.5.1.42 N33D site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type Rhodococcus erythropolis
1.5.1.42 N33E site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type Rhodococcus erythropolis
1.5.1.42 N33F site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type Rhodococcus erythropolis
1.5.1.42 N33G site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type Rhodococcus erythropolis
1.5.1.42 N33HID site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type Rhodococcus erythropolis
1.5.1.42 N33HIE site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type Rhodococcus erythropolis
1.5.1.42 N33HIP site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type Rhodococcus erythropolis
1.5.1.42 N33I site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type Rhodococcus erythropolis
1.5.1.42 N33K site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type Rhodococcus erythropolis
1.5.1.42 N33L site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type Rhodococcus erythropolis
1.5.1.42 N33M site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type Rhodococcus erythropolis
1.5.1.42 N33Q site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type Rhodococcus erythropolis
1.5.1.42 N33R site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type Rhodococcus erythropolis
1.5.1.42 N33S site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type Rhodococcus erythropolis
1.5.1.42 N33T site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type Rhodococcus erythropolis
1.5.1.42 N33V site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type Rhodococcus erythropolis
1.5.1.42 N33W site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type Rhodococcus erythropolis
1.5.1.42 N33Y site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type Rhodococcus erythropolis
1.5.1.42 T62A site-directed mutagenesis, the mutant shows 7fold increased activity compared to wild-type Rhodococcus erythropolis
1.5.1.42 T62N site-directed mutagenesis, the mutant shows 5fold increased activity compared to wild-type Rhodococcus erythropolis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.5.1.42 additional information
-
 additional information Gibbs activation and reaction free energies obtained for the hydride transfer by wild-type enzyme Rhodococcus erythropolis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.5.1.42 FMN + NADH + H+ Rhodococcus erythropolis
-
 FMNH2 + NAD+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.5.1.42 Rhodococcus erythropolis Q7DI30
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.1.42 FMN + NADH + H+
-
 Rhodococcus erythropolis FMNH2 + NAD+
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.5.1.42 DszD
-
 Rhodococcus erythropolis
1.5.1.42 NADH-FMN oxidoreductase
-
 Rhodococcus erythropolis

Cofactor

EC Number Cofactor Comment Organism Structure
1.5.1.42 NADH
-
 Rhodococcus erythropolis

General Information

EC Number General Information Comment Organism
1.5.1.42 malfunction mutation of the critical residue Thr62, T62N and T62A, show a 5 and 7fold increase in catalytic rate, respectively Rhodococcus erythropolis
1.5.1.42 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
1.5.1.42 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