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Information on EC 1.13.11.49 - chlorite O2-lyase

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EC Tree
IUBMB 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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This record set is specific for:
UNIPROT: B8HNS6
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Word Map
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
chlorite dismutase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
chlorite dismutase
-
chlorite dismutase
-
-
-
-
dimutase, chlorite
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
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 hide
190208-21-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
chlorite
chloride + O2
show the reaction diagram
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
chlorite
chloride + O2
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
heme
resting ferric high-spin axially symmetric heme enzyme, standard reduction potential of the Fe(III)/Fe(II) couple of -126 mV at pH 7.0
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Chlorite
above 0.1 mM chlorite (5000fold excess) irreversible inactivation is observed
cyanide
mediates the formation of a low-spin complex
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0188 - 0.327
Chlorite
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
18.91 - 1144
Chlorite
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
560 - 7100
Chlorite
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
B8HNS6_CYAP4
Cyanothece sp. (strain PCC 7425 / ATCC 29141)
182
0
21220
TrEMBL
other Location (Reliability: 2)
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
mutant enzymes Q74V and Q74E, sitting drop vapor diffusion method, using 0.1 M MES (pH 6.5), 0.15 M MgSO4, 28% (w/v) polyethylene glycol 3350, and 3% (v/v) glycerol
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
His-trap affinity column chromatography and Superdex 200 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 Gold (DE3) cells
expression in Escherichia coli
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
thermal and chemical unfolding follows a non-twostate unfolding pathway with the first transition being related to the release of the prosthetic group
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schaffner, I.; Hofbauer, S.; Krutzler, M.; Pirker, K.F.; Bellei, M.; Stadlmayr, G.; Mlynek, G.; Djinovic-Carugo, K.; Battistuzzi, G.; Furtmueller, P.G.; Daims, H.; Obinger, C.
Dimeric chlorite dismutase from the nitrogen-fixing cyanobacterium Cyanothece sp. PCC7425
Mol. Microbiol.
96
1053-1068
2015
Cyanothece sp. PCC 7425 (B8HNS6)
Manually annotated by BRENDA team
Schmidt, D.; Serra, I.; Mlynek, G.; Pfanzagl, V.; Hofbauer, S.; Furtmueller, P.G.; Djinovic-Carugo, K.; Van Doorslaer, S.; Obinger, C.
Arresting the catalytic arginine in chlorite dismutases Impact on heme coordination, thermal stability, and catalysis
Biochemistry
60
621-634
2021
Cyanothece sp. PCC 7425 (B8HNS6)
Manually annotated by BRENDA team