Protein Variants | Comment | Organism |
---|---|---|
W155F | site-directed mutagenesis, mutation of a conserved residue on the proximal side of the heme causes a loss of the characteristic pentameric oligomerization state, secondary structure, and heme binding properties of the wild-type protein. Conversion to an inactive, heme-free form is accelerated by dilution | Dechloromonas aromatica |
W156F | site-directed mutagenesis, mutation of a conserved residue on the proximal side of the heme causes a loss of the characteristic pentameric oligomerization state, secondary structure, and heme binding properties of the wild-type protein. Conversion to an inactive, heme-free form is accelerated by dilution | Dechloromonas aromatica |
W227F | site-directed mutagenesis, mutation of a conserved residue on the proximal side of the heme, but W227F retains many properties of the wild-type protein, the mutant reacts with peracetic acid at pH 6.0-8.0, overview | Dechloromonas aromatica |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
additional information | suicide inactivation by oxidative heme destruction | Dechloromonas aromatica |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | transient kinetic studies with wild-type and mutant enzymes, and steady-state kinetics, overview | Dechloromonas aromatica |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | heme enzyme | Dechloromonas aromatica |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
28400 | - |
2 * 28400, recombinant mutant W155F, SDS-PAGE | Dechloromonas aromatica |
54000 | - |
recombinant mutant W155F, gel filtration | Dechloromonas aromatica |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
chlorite | Dechloromonas aromatica | - |
chloride + O2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Dechloromonas aromatica | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
chlorite | - |
Dechloromonas aromatica | chloride + O2 | - |
? |
Subunits | Comment | Organism |
---|---|---|
homodimer | 2 * 28400, recombinant mutant W155F, SDS-PAGE | Dechloromonas aromatica |
Synonyms | Comment | Organism |
---|---|---|
chlorite dismutase | - |
Dechloromonas aromatica |
CLD | - |
Dechloromonas aromatica |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
20 | 25 | assay at | Dechloromonas aromatica |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
5.8 | 7.9 | assay at | Dechloromonas aromatica |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
heme | - |
Dechloromonas aromatica |
General Information | Comment | Organism |
---|---|---|
malfunction | 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 | Dechloromonas aromatica |