EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.1.3.17 | H466A | site-directed mutagenesis, comparison of midpoint reduction-oxidation potentials of the enzyme-FAD form with mutant H466D and the wild-type enzyme | Arthrobacter globiformis |
1.1.3.17 | H466D | site-directed mutagenesis, the mutation alters the flavin binding to the enzyme, while substrate choline is normally bound, binding og glycine btaine is inhibited, spectrometrical analysis, the mutant shows a different flavin-binding stoichiometry of 0.29:1, compared to 1:1 for the wild-type enzyme, stabilized at pH 6.0-10.0, overview, comparison of midpoint reduction-oxidation potentials of the enzyme-FAD form with mutant H466A and the wild-type enzyme, the mutant shows no catalytic activity | Arthrobacter globiformis |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.1.3.17 | additional information | - |
additional information | kinetics and redox potentiometric analysis of liganded and unliganded wild-type and mutant enzymes, comparison of spectral parameters of wild-type and mutant enzymes, overview | 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 | - |
? | |
1.1.3.17 | FADH2 + O2 | Arthrobacter globiformis | - |
FAD + H2O2 | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.1.3.17 | Arthrobacter globiformis | - |
strain ATCC 8010 | - |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
1.1.3.17 | choline + O2 = betaine aldehyde + H2O2 | reaction mechanism, the enzyme catalyzes the four-electron-oxidation of choline to glycine betaine via the intermediate betaine aldehyde in two sequential FAD-dependent reaction steps, His466 is a catalytic residue involved in flavin-binding | Arthrobacter globiformis |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.3.17 | choline + O2 | - |
Arthrobacter globiformis | betaine aldehyde + H2O2 | - |
? | |
1.1.3.17 | FADH2 + O2 | - |
Arthrobacter globiformis | FAD + H2O2 | - |
? |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.1.3.17 | FAD | dependent on, covalently bound to the enzyme, involving His466, in an 1:1 stoichiometry, spectrometrical analysis, effects of pH, mutant enzyme H466D shows a 0.29:1 stoichiometry, overview, comparison of midpoint reduction-oxidation potentials of the enzyme-FAD form with mutants H466D and H466A | Arthrobacter globiformis |