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Literature summary extracted from

  • Blanc, B.; Rodgers, K.; Lukat-Rodgers, G.; Dubois, J.
    Understanding the roles of strictly conserved tryptophan residues in O2 producing chlorite dismutases (2013), Dalton Trans., 42, 3156-3169.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
1.13.11.49 W155F site-directed mutagenesis, mutation of a conserved residue on the proximal side of the heme causes a loss of the characteristic pentameric oligomerization state, secondary structure, and heme binding properties of the wild-type protein. Conversion to an inactive, heme-free form is accelerated by dilution Dechloromonas aromatica
1.13.11.49 W156F site-directed mutagenesis, mutation of a conserved residue on the proximal side of the heme causes a loss of the characteristic pentameric oligomerization state, secondary structure, and heme binding properties of the wild-type protein. Conversion to an inactive, heme-free form is accelerated by dilution Dechloromonas aromatica
1.13.11.49 W227F site-directed mutagenesis, mutation of a conserved residue on the proximal side of the heme, but W227F retains many properties of the wild-type protein, the mutant reacts with peracetic acid at pH 6.0-8.0, overview Dechloromonas aromatica

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.13.11.49 additional information suicide inactivation by oxidative heme destruction Dechloromonas aromatica

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.13.11.49 additional information
-
 additional information transient kinetic studies with wild-type and mutant enzymes, and steady-state kinetics, overview Dechloromonas aromatica

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.13.11.49 Fe2+ heme enzyme Dechloromonas aromatica

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.13.11.49 28400
-
 2 * 28400, recombinant mutant W155F, SDS-PAGE Dechloromonas aromatica
1.13.11.49 54000
-
 recombinant mutant W155F, gel filtration Dechloromonas aromatica

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.13.11.49 chlorite Dechloromonas aromatica
-
 chloride + O2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.13.11.49 Dechloromonas aromatica
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.11.49 chlorite
-
 Dechloromonas aromatica chloride + O2
-
 ?

Subunits

EC Number Subunits Comment Organism
1.13.11.49 homodimer 2 * 28400, recombinant mutant W155F, SDS-PAGE Dechloromonas aromatica

Synonyms

EC Number Synonyms Comment Organism
1.13.11.49 chlorite dismutase
-
 Dechloromonas aromatica
1.13.11.49 CLD
-
 Dechloromonas aromatica

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.13.11.49 20 25 assay at Dechloromonas aromatica

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.13.11.49 5.8 7.9 assay at Dechloromonas aromatica

Cofactor

EC Number Cofactor Comment Organism Structure
1.13.11.49 heme
-
 Dechloromonas aromatica

General Information

EC Number General Information Comment Organism
1.13.11.49 malfunction the W155F mutation of the enzyme appears to disturb both the relatively higher heme affinity and pentameric oligomerization state common to the wild-type enzyme, mutant W156F, and mutant W227F Dechloromonas aromatica