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
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1.13.11.49
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perchlorate
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chlorate
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dechloromonas
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perchlorate-reducing
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dismutases
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clo2
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dismutation
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high-spin
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low-spin
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dechloratans
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defluvii
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chlorate-reducing
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nitrospira
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ideonella
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aromatica
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azospira
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hemqs
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environmental protection
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molecular biology
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biotechnology
- 1.13.11.49
- perchlorate
- chlorate
- dechloromonas
-
perchlorate-reducing
- dismutases
- clo2
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dismutation
-
high-spin
-
low-spin
- dechloratans
- defluvii
-
chlorate-reducing
- nitrospira
- ideonella
- aromatica
- azospira
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hemqs
- environmental protection
- molecular biology
- biotechnology
Reaction
Synonyms
chlorite dismutase, CLD, Cyan7425_1434, dimutase, chlorite, HemQ, Pfam chlorite dismutase, PitA
ECTree
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Engineering
Engineering on EC 1.13.11.49 - chlorite O2-lyase
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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
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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
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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
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mutant does not bind OH- under conditions where the wild-type enzyme is completely converted to the heme hydroxide. Mutant does not bind F-
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W227F
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mutant does not bind OH- under conditions where the wild-type enzyme is completely converted to the heme hydroxide. Mutant does not bind F-
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R173A
R173K
additional information
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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
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-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme, structure determination and comparison to the wild-type enzyme
R173A
leakage of hypochlorite during the reaction is higher than that in the wild-type protein
R173A
mutation increases the extent of irreversible inactivation. In the presence of the hypochlorite traps methionine, monochlorodimedone, and 2-[6-(4-aminophenoxy)-3-oxo-3H-xanthen-9-yl]benzoic acid, the extent of chlorite degradation and release of molecular oxygen is significantly increased, whereas heme bleaching and oxidative modifications of the protein are suppressed
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme, structure determination and comparison to the wild-type enzyme
R173K
mutation increases the extent of irreversible inactivation. In the presence of the hypochlorite traps methionine, monochlorodimedone, and 2-[6-(4-aminophenoxy)-3-oxo-3H-xanthen-9-yl]benzoic acid, the extent of chlorite degradation and release of molecular oxygen is significantly increased, whereas heme bleaching and oxidative modifications of the protein are suppressed
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a Staphylococcus aureus strain with an inactivated hemQ gene is generated and shown to be a slow growing small colony variant under aerobic but not anaerobic conditions
additional information
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a Staphylococcus aureus strain with an inactivated hemQ gene is generated and shown to be a slow growing small colony variant under aerobic but not anaerobic conditions
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