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Literature summary extracted from

  • Sousa, S.F.; Sousa, J.F.; Barbosa, A.C.; Ferreira, C.E.; Neves, R.P.; Ribeiro, A.J.; Fernandes, P.A.; Ramos, M.J.
    Improving the biodesulfurization of crude oil and derivatives a QM/MM investigation of the catalytic mechanism of NADH-FMN oxidoreductase (DszD) (2016), J. Phys. Chem. A, 120, 5300-5306 .
    View publication on PubMed

Protein Variants

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

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
1.5.1.42 Rhodococcus erythropolis
-
-
-
1.5.1.42 Rhodococcus erythropolis IGTS8 / ATCC 53968
-
-
-

Reaction

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

Substrates and Products (Substrate)

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

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 NAD+
-
Rhodococcus erythropolis
1.5.1.42 NADH
-
Rhodococcus erythropolis

General Information

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