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