Literature summary for 1.14.14.21 extracted from

Guan, L.J.; Lee, W.C.; Wang, S.; Ohshiro, T.; Izumi, Y.; Ohtsuka, J.; Tanokura, M.
Crystal structures of apo-DszC and FMN-bound DszC from Rhodococcus erythropolis D-1 (2015), FEBS J., 282, 3126-3135.

Search for more literature for 1.14.14.21

Cloned(Commentary)

Cloned (Comment)	Organism
gene dszC, recombinant expression of His-tagged enzyme in Escherichia coli strain Rosetta(DE3)	Rhodococcus erythropolis

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant His-tagged enzyme in apoform and as FMN-bound enzyme DszC, two distinct conformations occur in the loop region (residues 131-142) adjacent to the active site, sitting drop vapor diffusion method, mixing of 0.001 ml protein solution with 0.001 ml of reservoir solution consisting of 0.2 M malonate, pH 6.0, 24% w/v PEG 3350, and 50 mM NaF, at 20°C, with or without 1 mM FMN, X-ray diffraction structure determination and analysis at 2.11 A an 2.3 A resolution, respectively, Each crystal contains two tetramers in the asymmetric unit, formed by two homodimers	Rhodococcus erythropolis

Crystallization (Comment)

Organism

purified recombinant His-tagged enzyme in apoform and as FMN-bound enzyme DszC, two distinct conformations occur in the loop region (residues 131-142) adjacent to the active site, sitting drop vapor diffusion method, mixing of 0.001 ml protein solution with 0.001 ml of reservoir solution consisting of 0.2 M malonate, pH 6.0, 24% w/v PEG 3350, and 50 mM NaF, at 20°C, with or without 1 mM FMN, X-ray diffraction structure determination and analysis at 2.11 A an 2.3 A resolution, respectively, Each crystal contains two tetramers in the asymmetric unit, formed by two homodimers

Rhodococcus erythropolis

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
dibenzothiophene + 2 FMNH2 + 2 O2	Rhodococcus erythropolis	-	dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O	-	?
dibenzothiophene + 2 FMNH2 + 2 O2	Rhodococcus erythropolis D-1	-	dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O	-	?

Organism

Organism	UniProt	Comment	Textmining
Rhodococcus erythropolis	A0A0C6DRW4	gene dszC	-
Rhodococcus erythropolis D-1	A0A0C6DRW4	gene dszC	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant His-tagged enzyme from Escherichia coli strain Rosetta(DE3) by nickel affinity and anion exchange chromatography, followed by ultrafiltration	Rhodococcus erythropolis

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
dibenzothiophene + 2 FMNH2 + 2 O2	-	Rhodococcus erythropolis	dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O	-	?
dibenzothiophene + 2 FMNH2 + 2 O2	-	Rhodococcus erythropolis D-1	dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O	-	?

Subunits

Subunits	Comment	Organism
More	in the crystal, the homodimeric enzyme forms tetramers from two homodimers, overview	Rhodococcus erythropolis

Synonyms

Synonyms	Comment	Organism
DBT monooxygenase	-	Rhodococcus erythropolis
dszC	-	Rhodococcus erythropolis

Cofactor

Cofactor	Comment	Organism	Structure
FMNH2	enzyme DszC-FMN crystal structure analysis, FMN-binding site, binding structure and mechanism, modeling, overview	Rhodococcus erythropolis

General Information

General Information	Comment	Organism
metabolism	the DBT monooxygenase from Rhodococcus erythropolis D-1 is involved in the first two steps of the 4S pathway. The 4S metabolic pathway catalyzes the sequential conversion of DBT to 2'-hydroxybiphenyl via three enzymes encoded by the dsz operon in several bacterial species	Rhodococcus erythropolis
additional information	C-terminal DBT-binding site by using a molecular docking simulation that simultaneously docks the FMN cofactor and DBT substrate to an apo-DszC structure, role of the C terminus in catalysis	Rhodococcus erythropolis