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
-
1.13.11.49
-
perchlorate
-
chlorate
-
dechloromonas
-
perchlorate-reducing
-
dismutases
-
clo2
-
dismutation
-
high-spin
-
low-spin
-
dechloratans
-
defluvii
-
chlorate-reducing
-
nitrospira
-
ideonella
-
aromatica
-
azospira
-
hemqs
-
environmental protection
-
molecular biology
-
biotechnology
- 1.13.11.49
- perchlorate
- chlorate
- dechloromonas
-
perchlorate-reducing
- dismutases
- clo2
-
dismutation
-
high-spin
-
low-spin
- dechloratans
- defluvii
-
chlorate-reducing
- nitrospira
- ideonella
- aromatica
- azospira
-
hemqs
- environmental protection
- molecular biology
- biotechnology
Reaction
Synonyms
chlorite dismutase, CLD, Cyan7425_1434, dimutase, chlorite, HemQ, Pfam chlorite dismutase, PitA
ECTree
Advanced search results
Crystallization
Crystallization on EC 1.13.11.49 - chlorite O2-lyase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
thiocyanate inhibited enzyme with incorporated heme, crystals grown from well solution containing 100 mM Mes buffer (pH 5.5), 25% polyethylene glycol monomethyl ether 2000, 0.3 M KSCN, 5% glycerol, 160-260 mM (NH4)2SO4, before data collection crystals are soaked in a solution of the mother liquor including 16% glycerol, crystal is flash-frozen and kept at -173°C (100 K) for multiple anomalous dispersion (MAD) with synchrotron radiation
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
recombinant protein, buffer-exchanged into 20 mM HEPES, pH 7.0, hanging-drop vapor diffusion, 16% PEG 8000, 0.2 M calcium acetate, 90 mM MES, pH 6.5, 293 K, chrystals appear after 2 h, co-crystals with substrate analogues sodium nitrite and sodium cyanide under same conditions
-
enzyme is a homopentamer, with presence of one b-type heme per monomer
in complex with thiocyanate and azide, to 0.976 and 1.0 A resolution, respectively. The crystal structure of the Cld-azide complex reveals a single well-defined orientation of the azide molecule in the heme pocket. EPR shows a pH-dependent heme structure, probably due to acid-base transitions of the surrounding amino-acid residues stabilizing azide
purified recombinant His-tagged enzyme, sitting-drop vapor diffusion technique and a nanodropdispensing robot, from 1.0 M Na2HPO4-NaH2PO4, pH 8.2, at 22°C, 1 week, X-ray diffraction structure determination and analysis at 2.10 A resolution
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