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Literature summary extracted from

  • Driggers, C.M.; Hartman, S.J.; Karplus, P.A.
    Structures of Arg- and Gln-type bacterial cysteine dioxygenase homologs (2015), Protein Sci., 24, 154-161 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.13.11.20 gene cdoA, recombinant enzyme expression in Escherichia coli strain BL21(DE3), subcloning in Escherichia cli strain DH5alpha Bacillus subtilis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.13.11.20 purified recombinant enzyme free or with bound substrate L-Cys, hanging drop vapour diffusion method, mixing of 0.004 ml of 10 mg/ml protein solution with 0.004 ml of reservoir solution containing 18% w/v PEG 4000, 0.1 M potassium acetate, 0.05 M 2-(N-morpholino)ethanesulfonic acid, pH 6.0, 25°C, 2-7 days, X-ray diffraction structure determination and analysis at 2.38-2.82 A resolution Bacillus subtilis
1.13.11.91 structural comparison with cysteine dioxygenase homologs that conserve an active site Gln residue, cf. EC 1.13.11.20 Variovorax paradoxus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.13.11.20 Fe2+ a catalytic a non-heme iron is coordinated by three conserved residues His75, His77, and His125 Bacillus subtilis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.13.11.20 L-cysteine + O2 Bacillus subtilis
-
 3-sulfinoalanine
-
 ?
1.13.11.20 L-cysteine + O2 Bacillus subtilis 168
-
 3-sulfinoalanine
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.13.11.20 Bacillus subtilis O32085
-
-
1.13.11.20 Bacillus subtilis 168 O32085
-
-
1.13.11.91 Variovorax paradoxus B9U5L8
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.13.11.20 recombinant enzyme from Escherichia coli strain BL21(DE3) Bacillus subtilis

Reaction

EC Number Reaction Comment Organism Reaction ID
1.13.11.20 L-cysteine + O2 = 3-sulfinoalanine reaction mechanism and structure-function analysis Bacillus subtilis
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.11.20 L-cysteine + O2
-
 Bacillus subtilis 3-sulfinoalanine
-
 ?
1.13.11.20 L-cysteine + O2
-
 Bacillus subtilis 168 3-sulfinoalanine
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.13.11.20 Arg-type CDO
-
 Bacillus subtilis
1.13.11.20 BsCDO
-
 Bacillus subtilis
1.13.11.20 CDO
-
 Bacillus subtilis
1.13.11.91 3MP dioxygenase
-
 Variovorax paradoxus
1.13.11.91 MDO
-
 Variovorax paradoxus

General Information

EC Number General Information Comment Organism
1.13.11.20 evolution analysis of examples for two structural genomics groups of CDOs: a Bacillus subtilis Arg-type enzyme that has cysteine dioxygenase activity (BsCDO), and a Ralstonia eutropha Gln-type CDO homologue of uncharacterized activity (ReCDOhom), overview. The BsCDO active site is well conserved with mammalian CDO, and a cysteine complex captured in the active site confirms that the cysteine binding mode is also similar. The Arg position is not compatible with the mode of Cys binding seen in both Rattus norvegicus CDO and Bacillus subtilis CDO. Gln-type CDO homologues are not authentic CDOs but have substrate specificity more similar to 3-mercaptopropionate dioxygenases Bacillus subtilis
1.13.11.20 additional information the BsCDO active site has a non-heme iron coordinated by three conserved residues His75, His77, and His125. Ser137, His139, andTyr141 form the catalytic triad. The bound L-Cys coordinates the iron in a bidentate fashion via its Sgamma and N atoms. Structure comparisons, overview Bacillus subtilis