EC Number | Cloned (Comment) | Organism |
---|---|---|
1.1.3.17 | expression of wild-type and mutant enzymes in Escherichia coli | Arthrobacter globiformis |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.1.3.17 | H466A | decrease in kcat and kcat/Km-value for choline, but not for oxygen, partial rescue of activity in presence of imidazolium | Arthrobacter globiformis |
1.1.3.17 | H466A | site-directed mutagenesis, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme, the enzyme activity in the mutant strain can partially be rescued by addition of exogenous imidazolium, but not by imidazole, overview | Arthrobacter globiformis |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.1.3.17 | glycine betaine | binds to the active site, different binding of wild-type and mutant enzymes, overview | Arthrobacter globiformis |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.1.3.17 | additional information | - |
additional information | steady-state kinetics of wild-type and mutant enzymes at different pH and in presence or absence of imidazole, kinetic isotope effects | Arthrobacter globiformis | |
1.1.3.17 | 1.7 | - |
choline | pH 7.0, 25°C, wild type | Arthrobacter globiformis | |
1.1.3.17 | 21 | - |
O2 | pH 7.0, 25°C, mutant H466A | Arthrobacter globiformis | |
1.1.3.17 | 29 | - |
choline | pH 7.0, 25°C mutant H466A | Arthrobacter globiformis | |
1.1.3.17 | 703 | - |
O2 | pH 7.0, 25°C, wild type | Arthrobacter globiformis |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.3.17 | choline + O2 | Arthrobacter globiformis | - |
betaine aldehyde + H2O2 | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.1.3.17 | Arthrobacter globiformis | - |
strain ATCC 8010 | - |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.1.3.17 | recombinant wild-type enzyme in oxidized state to homogeneity | Arthrobacter globiformis |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
1.1.3.17 | betaine aldehyde + O2 + H2O = betaine + H2O2 | His466 is a catalytic residue involved in the oxidation but not the reduction, reaction mechanism | Arthrobacter globiformis | |
1.1.3.17 | choline + O2 = betaine aldehyde + H2O2 | His466 is a catalytic residue involved in the oxidation but not the reduction, reaction mechanism | Arthrobacter globiformis |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.3.17 | choline + O2 | - |
Arthrobacter globiformis | betaine aldehyde + H2O2 | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.1.3.17 | CHO | - |
Arthrobacter globiformis |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.1.3.17 | 25 | - |
assay at | Arthrobacter globiformis |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.1.3.17 | 0.03 | - |
choline | pH 5.5, 25°C, mutant H466A | Arthrobacter globiformis | |
1.1.3.17 | 0.03 | - |
choline | pH 5.5, 25°C, recombinant mutant H466A | Arthrobacter globiformis | |
1.1.3.17 | 0.07 | - |
choline | pH 6.0, 25°C, recombinant mutant H466A | Arthrobacter globiformis | |
1.1.3.17 | 0.21 | - |
choline | pH 5.5, 25°C, mutant H466A, presence of imidazole | Arthrobacter globiformis | |
1.1.3.17 | 0.37 | - |
choline | pH 7.0, 25°C, recombinant mutant H466A | Arthrobacter globiformis | |
1.1.3.17 | 0.52 | - |
choline | pH 7.0, 25°C, mutant H466A, presence of imidazole | Arthrobacter globiformis | |
1.1.3.17 | 0.7 | - |
choline | pH 10.0, 25°C, mutant H466A, presence of imidazole | Arthrobacter globiformis | |
1.1.3.17 | 0.72 | - |
choline | pH 8.0, 25°C, recombinant mutant H466A | Arthrobacter globiformis | |
1.1.3.17 | 0.73 | - |
choline | pH 10.0, 25°C, mutant H466A | Arthrobacter globiformis | |
1.1.3.17 | 0.73 | - |
choline | pH 10.0, 25°C, recombinant mutant H466A | Arthrobacter globiformis | |
1.1.3.17 | 1.1 | - |
choline | pH 7.0, 25°C, mutant H466A | Arthrobacter globiformis | |
1.1.3.17 | 61 | - |
choline | pH 7.0, 25°C, wild type | Arthrobacter globiformis |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.1.3.17 | 7 | - |
assay at | Arthrobacter globiformis |
EC Number | pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|---|
1.1.3.17 | 5.5 | 10 | - |
Arthrobacter globiformis |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.1.3.17 | FAD | covalently bound to the enzyme, spectral analysis of denatured wild-type and mutant enzymes, overview | Arthrobacter globiformis |
EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.1.3.17 | additional information | - |
additional information | inhibition kinetics | Arthrobacter globiformis |