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Information on EC 1.13.11.49 - chlorite O2-lyase and Organism(s) Nitrospira defluvii and UniProt Accession B3U4H7
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1.13.11.49 chlorite O2-lyaseIUBMB Comments
Reaction occurs in the reverse direction in chlorate- and perchlorate-reducing bacteria. There is no activity when chlorite is replaced by hydrogen peroxide, perchlorate, chlorate or nitrite. The term 'chlorite dismutase' is misleading as the reaction does not involve dismutation/disproportionation. Contains iron and protoheme IX.
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Word Map
- 1.13.11.49
- perchlorate
- chlorate
- dechloromonas
-
perchlorate-reducing
- dismutases
- clo2
-
dismutation
-
high-spin
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low-spin
- dechloratans
- defluvii
-
chlorate-reducing
- nitrospira
- ideonella
- aromatica
- azospira
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hemqs
- environmental protection
- molecular biology
- biotechnology
The taxonomic range for the selected organisms is: Nitrospira defluvii
The expected taxonomic range for this enzyme is: Bacteria, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
chlorite dismutase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
chlorite dismutase
dimutase, chlorite
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chlorite dismutase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
chloride + O2 = chlorite
reaction mechanism and active site structure, Arg173 plays a key role in (i) controlling of ligand and substrate access and binding and (ii) in chlorite dismutation reaction, overview
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
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oxidation
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reduction
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SYSTEMATIC NAME
IUBMB Comments
chloride:oxygen oxidoreductase
Reaction occurs in the reverse direction in chlorate- and perchlorate-reducing bacteria. There is no activity when chlorite is replaced by hydrogen peroxide, perchlorate, chlorate or nitrite. The term 'chlorite dismutase' is misleading as the reaction does not involve dismutation/disproportionation. Contains iron and protoheme IX.
CAS REGISTRY NUMBER
COMMENTARY
190208-21-0
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
chloride + O2
chlorite
chlorite dismutase is a unique heme enzyme which transforms chlorite to chloride and molecular oxygen
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-
r
chloride + O2
chlorite
Arg173 plays a key role in (i) controlling of ligand and substrate access and binding and (ii) in chlorite dismutation reaction, mechanism, overview. The flexible residue modulates the electrostatic potential and size of the active site entrance and might be involved in keeping transiently formed hypochlorite in place for final molecular oxygen and chloride formation
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r
additional information
?
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upon reduction of chlorite, hypochlorite is formed and kept in the reaction sphere for recombination with the oxoiron(IV) group of Compound I. Approximately one molecule of HOCl per 100 full cycles escapes and reacts with both the prosthetic group and the protein moiety, leading to irreversible inactivation of Cld is observed which is more pronounced with an increase in pH. HOCl traps like methionine can rescue the enzyme from inactivation
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?
additional information
?
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chlorite binding to ferric Cld occurs spontaneously and residue Arg173 is important for recognition and to impair hypochlorite leakage from the reaction sphere
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?
additional information
?
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chlorite binding to ferric Cld occurs spontaneously and residue Arg173 is important for recognition and to impair hypochlorite leakage from the reaction sphere
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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
chloride + O2
chlorite
chlorite dismutase is a unique heme enzyme which transforms chlorite to chloride and molecular oxygen
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-
r
additional information
?
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upon reduction of chlorite, hypochlorite is formed and kept in the reaction sphere for recombination with the oxoiron(IV) group of Compound I. Approximately one molecule of HOCl per 100 full cycles escapes and reacts with both the prosthetic group and the protein moiety, leading to irreversible inactivation of Cld is observed which is more pronounced with an increase in pH. HOCl traps like methionine can rescue the enzyme from inactivation
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
presence of methionine can partly rescue inactivation during the reaction
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
steady-state, pre-steady-state, and transient-state kinetics, overview
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additional information
additional information
-
steady-state, pre-steady-state, and transient-state kinetics, overview
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additional information
additional information
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steady-state kinetics, overview
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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
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conformational and thermal stability of recombinant pentameric Cld from Nitrospira defluvii, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PDB
SCOP
CATH
UNIPROT
ORGANISM
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homopentamer
each monomer of NdCld is characterized by two topologically equivalent four-stranded antiparallel beta-sheets forming a beta-barrel, flanked on both sides by six alpha-helices, overview
pentamer
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conformational and thermal stability of recombinant pentameric Cld from Nitrospira defluvii, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
molecular dynamics simulations for binding of cyanide, chlorite, and hypochlorite with the enzyme in the ferrous, ferric, and compound I state. During reaction, a large portion of hypochlorite escapes from the heme cavity and enters the bulk phase. Leakage of hypochlorite in the mutant R173A is higher than that in the wild-type protein
purified recombinant His-tagged wild-type and mutant enzymes with bound cyanide, 22°C, sitting drop vapour diffusion method, X-ray diffraction structure determination and analysis at 1.85-2.70 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R173A
R173K
R173A
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
R173K
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 10
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the pentameric enzyme is very stable between pH 3 and 10 with Tm=92°C at pH 7.0
724448
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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conformational and thermal stability of recombinant pentameric Cld from Nitrospira defluvii, overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant N-terminally His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
recombinant Strep-tagged enzyme from Escherichia coli strain Tuner (DE3) by affinity chromatography, the Strep-II-tag is fully cleaved off using TEV-protease, followed by gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
phylogenetic analysis, expression of N-terminally His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
recombinant expression of the enzyme without the N-terminal signal, but with N-terminal TEV-cleavable Strep-II tag in Escherichia coli strain Tuner (DE3)
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
environmental protection
bacteria with Cld play significant roles in the bioremediation of industrially contaminated sites and also in wastewater treatment
environmental protection
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the enzyme from Nitrospira defluvii is an interesting candidate for bioremediation of chlorite
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Maixner, F.; Wagner, M.; Luecker, S.; Pelletier, E.; Schmitz-Esser, S.; Hace, K.; Spieck, E.; Konrat, R.; Le Paslier, D.; Daims, H.
Environmental genomics reveals a functional chlorite dismutase in the nitrite-oxidizing bacterium Candidatus Nitrospira defluvii
Environ. Microbiol.
10
3043-3056
2008
Nitrospira defluvii
Kostan, J.; Sjoeblom, B.; Maixner, F.; Mlynek, G.; Furtmueller, P.G.; Obinger, C.; Wagner, M.; Daims, H.; Djinovic-Carugo, K.
Structural and functional characterisation of the chlorite dismutase from the nitrite-oxidizing bacterium Candidatus Nitrospira defluvii: identification of a catalytically important amino acid residue
J. Struct. Biol.
172
331-342
2010
Nitrospira defluvii (B3U4H7), Nitrospira defluvii
Hofbauer, S.; Gysel, K.; Mlynek, G.; Kostan, J.; Hagmueller, A.; Daims, H.; Furtmueller, P.; Djinovic-Carugo, K.; Obinger, C.
Impact of subunit and oligomeric structure on the thermal and conformational stability of chlorite dismutases
Biochim. Biophys. Acta
1824
1031-1038
2012
Nitrospira defluvii, Nitrobacter winogradskyi (Q3SPU6)
Hofbauer, S.; Gruber, C.; Pirker, K.F.; Suendermann, A.; Schaffner, I.; Jakopitsch, C.; Oostenbrink, C.; Furtmueller, P.G.; Obinger, C.
Transiently produced hypochlorite is responsible for the irreversible inhibition of chlorite dismutase
Biochemistry
53
3145-3157
2014
Nitrospira defluvii (B3U4H7)
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