EC Number | Cloned (Comment) | Organism |
---|---|---|
1.6.2.2 | wild type and mutant enzyme expressed in Escherichia coli BL21-CodonPlus (DE3)-RIL | Rattus norvegicus |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
1.6.2.2 | sitting drop method | Rattus norvegicus |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.6.2.2 | S127P | caused methemoglobinemia type II, FAD is displaced from its binding site by NADH, Km for NADH is strongly increased | Rattus norvegicus |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.6.2.2 | 0.003 | - |
NADH | pH 7.0, wild type enzyme with cytochrome b5 as substrate | Rattus norvegicus | |
1.6.2.2 | 0.006 | - |
NADH | pH 7.0, wild type enzyme with ferricyanide as substrate | Rattus norvegicus | |
1.6.2.2 | 0.007 | - |
ferricyanide | pH 7.0, wild type enzyme | Rattus norvegicus | |
1.6.2.2 | 0.008 | - |
ferricyanide | pH 7.0, S127P mutant enzyme | Rattus norvegicus | |
1.6.2.2 | 0.013 | - |
ferricytochrome b5 | pH 7.0, wild type enzyme | Rattus norvegicus | |
1.6.2.2 | 0.014 | - |
ferricytochrome b5 | pH 7.0, S127P mutant enzyme | Rattus norvegicus | |
1.6.2.2 | 0.025 | - |
NADH | pH 7.0, S127P mutant enzyme with cytochrome b5 as substrate | Rattus norvegicus | |
1.6.2.2 | 0.055 | - |
NADH | pH 7.0, S127P mutant enzyme with ferricyanide as substrate | Rattus norvegicus |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
1.6.2.2 | membrane | full length form contains a 3 kDa membrane anchoring domain | Rattus norvegicus | 16020 | - |
1.6.2.2 | microsome | - |
Rattus norvegicus | - |
- |
1.6.2.2 | soluble | truncated form lacking the membrane anchoring domain | Rattus norvegicus | - |
- |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.6.2.2 | 2 ferricytochrome b5 + NADH | Rattus norvegicus | involved in the synthesis of fatty acids and cholesterol, and in the oxidation of xenobiotics, mutations can cause methemoglobinemia type I or II | 2 ferrocytochrome b5 + NAD+ + H+ | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.6.2.2 | Rattus norvegicus | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.6.2.2 | recombinant enzymes purified from Escherichia coli | Rattus norvegicus |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.6.2.2 | 2 ferricytochrome b5 + NADH | - |
Rattus norvegicus | 2 ferrocytochrome b5 + NAD+ + H+ | - |
? | |
1.6.2.2 | 2 ferricytochrome b5 + NADH | involved in the synthesis of fatty acids and cholesterol, and in the oxidation of xenobiotics, mutations can cause methemoglobinemia type I or II | Rattus norvegicus | 2 ferrocytochrome b5 + NAD+ + H+ | - |
? |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.6.2.2 | 106 | - |
ferricytochrome b5 | pH 7.0, S127P mutant enzyme | Rattus norvegicus | |
1.6.2.2 | 300 | - |
ferricyanide | pH 7.0, S127P mutant enzyme | Rattus norvegicus | |
1.6.2.2 | 367 | - |
ferricytochrome b5 | pH 7.0, wild type enzyme | Rattus norvegicus | |
1.6.2.2 | 800 | - |
ferricyanide | pH 7.0, wild type enzyme | Rattus norvegicus |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.6.2.2 | FAD | tightly bound prosthetic group | Rattus norvegicus | |
1.6.2.2 | NADH | - |
Rattus norvegicus |