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Literature summary for 1.5.1.42 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
Search for more literature for 1.5.1.42

Protein Variants

Protein Variants Comment Organism
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)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
FMNH2 + NAD+ Rhodococcus erythropolis
-
 FMN + NADH + H+
-
 r
FMNH2 + NAD+ Rhodococcus erythropolis IGTS8 / ATCC 53968
-
 FMN + NADH + H+
-
 r

Organism

Organism UniProt Comment Textmining
Rhodococcus erythropolis
-
-
-
Rhodococcus erythropolis IGTS8 / ATCC 53968
-
-
-

Reaction

Reaction Comment Organism Reaction ID
FMNH2 + NAD+ = FMN + NADH + H+ catalytic reaction mechanism with active site Thr residue, hybrid quantum mechanics/molecular mechanics simulation methods, overview Rhodococcus erythropolis
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
FMNH2 + NAD+
-
 Rhodococcus erythropolis FMN + NADH + H+
-
 r
FMNH2 + NAD+
-
 Rhodococcus erythropolis IGTS8 / ATCC 53968 FMN + NADH + H+
-
 r

Synonyms

Synonyms Comment Organism
DszD
-
 Rhodococcus erythropolis
NADH-FMN oxidoreductase
-
 Rhodococcus erythropolis

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Rhodococcus erythropolis
NADH
-
 Rhodococcus erythropolis

General Information

General Information Comment Organism
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
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