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1.13.11.49: chlorite O2-lyase

This is an abbreviated version!
For detailed information about chlorite O2-lyase, go to the full flat file.

Word Map on EC 1.13.11.49

Reaction

chloride
+
O2
=
Chlorite

Synonyms

chlorite dismutase, CLD, Cyan7425_1434, dimutase, chlorite, HemQ, Pfam chlorite dismutase, PitA

ECTree

     1 Oxidoreductases
         1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)
             1.13.11 With incorporation of two atoms of oxygen
                1.13.11.49 chlorite O2-lyase

Engineering

Engineering on EC 1.13.11.49 - chlorite O2-lyase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R183a
the mutation results in the loss of the ability to bind acetate
Q74E
the catalytic efficiency (kcat/KM) of chlorite degradation of the variant is similar to that of the wild type protein
Q74V
the catalytic efficiency (kcat/KM) of chlorite degradation of the variant is similar to that of the wild type protein
R183Q
mutant does not bind OH- under conditions where the wild-type enzyme is completely converted to the heme hydroxide. Mutant does not bind F-
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
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
W227F
R183Q
-
mutant does not bind OH- under conditions where the wild-type enzyme is completely converted to the heme hydroxide. Mutant does not bind F-
-
W227F
-
mutant does not bind OH- under conditions where the wild-type enzyme is completely converted to the heme hydroxide. Mutant does not bind F-
-
R173A
R173K
additional information