Application | Comment | Organism |
---|---|---|
environmental protection | bacteria with Cld play significant roles in the bioremediation of industrially contaminated sites and also in wastewater treatment | Nitrospira defluvii |
Cloned (Comment) | Organism |
---|---|
phylogenetic analysis, expression of N-terminally His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) | Nitrospira defluvii |
Crystallization (Comment) | Organism |
---|---|
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 | Nitrospira defluvii |
Protein Variants | Comment | Organism |
---|---|---|
R173A | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme, structure determination and comparison to the wild-type enzyme | Nitrospira defluvii |
R173K | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme, structure determination and comparison to the wild-type enzyme | Nitrospira defluvii |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | steady-state, pre-steady-state, and transient-state kinetics, overview | Nitrospira defluvii | |
0.057 | - |
Chlorite | pH 7.0, 30°C, recombinant wild-type enzyme | Nitrospira defluvii | |
0.107 | - |
Chlorite | pH 7.0, 30°C, recombinant mutant R137A | Nitrospira defluvii | |
0.818 | - |
Chlorite | pH 7.0, 30°C, recombinant mutant R137K | Nitrospira defluvii |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
CN- | binding kinetics of wild-type and mutant enzymes, overview | Nitrospira defluvii | |
Fe2+ | heme protein | Nitrospira defluvii |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
chloride + O2 | Nitrospira defluvii | chlorite dismutase is a unique heme enzyme which transforms chlorite to chloride and molecular oxygen | chlorite | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Nitrospira defluvii | B3U4H7 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant N-terminally His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration | Nitrospira defluvii |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
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 | Nitrospira defluvii |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
chloride + O2 | chlorite dismutase is a unique heme enzyme which transforms chlorite to chloride and molecular oxygen | Nitrospira defluvii | chlorite | - |
r | |
chloride + O2 | 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 | Nitrospira defluvii | chlorite | - |
r |
Subunits | Comment | Organism |
---|---|---|
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 | Nitrospira defluvii |
Synonyms | Comment | Organism |
---|---|---|
chlorite dismutase | - |
Nitrospira defluvii |
CLD | - |
Nitrospira defluvii |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | 30 | assay at | Nitrospira defluvii |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
7.1 | - |
Chlorite | pH 7.0, 30°C, recombinant mutant R137A | Nitrospira defluvii | |
21 | - |
Chlorite | pH 7.0, 30°C, recombinant mutant R137K | Nitrospira defluvii | |
35 | - |
Chlorite | pH 7.0, 30°C, recombinant wild-type enzyme | Nitrospira defluvii |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
assay at | Nitrospira defluvii |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
heme | - |
Nitrospira defluvii |
General Information | Comment | Organism |
---|---|---|
evolution | active site conservation and evolution of Cld, overview | Nitrospira defluvii |
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 | Nitrospira defluvii |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
25000 | - |
Chlorite | pH 7.0, 30°C, recombinant mutant R137K | Nitrospira defluvii | |
66000 | - |
Chlorite | pH 7.0, 30°C, recombinant mutant R137A | Nitrospira defluvii | |
600000 | - |
Chlorite | pH 7.0, 30°C, recombinant wild-type enzyme | Nitrospira defluvii |