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
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perchlorate-reducing
- dismutases
- clo2
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dismutation
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high-spin
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low-spin
- dechloratans
- defluvii
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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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General Information
General Information on EC 1.13.11.49 - chlorite O2-lyase
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evolution
malfunction
metabolism
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the enzyme is the terminal enzyme involved in the perchlorate reduction pathway
physiological function
additional information
evolution
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The chlorite dismutases (C-family proteins) are a widespread family of heme-binding proteins
evolution
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The chlorite dismutases (C-family proteins) are a widespread family of heme-binding proteins
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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. The DELTAhemQ mutant accumulates coproporphyrin specifically under aerobic conditions. Phenotypes, overview
malfunction
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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
malfunction
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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. The DELTAhemQ mutant accumulates coproporphyrin specifically under aerobic conditions. Phenotypes, overview
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similar substrate role for heme or porphyrin, with possible sensor-regulator functions for the protein
physiological function
the enzyme detoxifies the chlorite that results from chlorate respiration in bacteria and would otherwise accumulate in the cell and kill the organism. Nitrobacter has a limited chlorite resistance, which enables it to persist and even oxidize nitrite in the presence of low concentrations of chlorate
physiological function
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the enzyme detoxifies the chlorite that results from chlorate respiration in bacteria and would otherwise accumulate in the cell and kill the organism. The reaction must be fast in order to serve its biological function: the homopentameric enzyme from Dechloromonas aromatica is one of the fastest and most efficient chlorite O2-lyases yet studied. The enzyme can support the generation of tens-of-millimolar O2 on the millisecond timescale
physiological function
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wild-type strains have a significant growth advantage in the presence of chlorate relative to a Cld knockout strain, specifically under nitrate-respiring conditions
physiological function
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wild-type strains have a significant growth advantage in the presence of chlorate relative to a Cld knockout strain, specifically under nitrate-respiring conditions
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physiological function
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similar substrate role for heme or porphyrin, with possible sensor-regulator functions for the protein
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active and inactive enzyme forms dependent on the protonation status, overview
additional information
Candidatus Nitrospira defluvii is a key nitrifier in biological wastewater treatment, molecular mechanism of chlorite detoxification, overview. The residue corresponding to Arg173 is conserved in all known active forms of Cld and propose it as a marker for Cld activity in yet uncharacterized Cld-like proteins
additional information
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Candidatus Nitrospira defluvii is a key nitrifier in biological wastewater treatment, molecular mechanism of chlorite detoxification, overview. The residue corresponding to Arg173 is conserved in all known active forms of Cld and propose it as a marker for Cld activity in yet uncharacterized Cld-like proteins
additional information
conformational and thermal stability of recombinant dimeric Cld from Nitrobacter winogradskyi, overview
additional information
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conformational and thermal stability of recombinant pentameric Cld from Nitrospira defluvii, overview
additional information
despite a truncated N-terminal domain in each subunit, the dimeric enzyme is a highly efficient chlorite dismutase. Subunit interface and active site structures, structure modeling, overview
additional information
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despite a truncated N-terminal domain in each subunit, the dimeric enzyme is a highly efficient chlorite dismutase. Subunit interface and active site structures, structure modeling, overview
additional information
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the enzyme is capable of approximately 17000 turnovers per heme before undergoing irreversible inactivation due to oxidative damage to the heme