EC Number | Cloned (Comment) | Organism |
---|---|---|
1.1.3.17 | gene codA, expression of Strep-tagged wild-type and mutant enzymes in Escherichia coli strain BL21-Gold | Glutamicibacter nicotianae |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.1.3.17 | A21V | site-directed mutagenesis in the FAD binding site | Glutamicibacter nicotianae |
1.1.3.17 | A21V/G62D | site-directed mutagenesis, the mutant shows 1.93fold increased activity with tris-(2-hydroxyethyl)-methylammonium methylsulfate and slightly reduced activity with choline compared to the wild-type enzyme | Glutamicibacter nicotianae |
1.1.3.17 | A21V/G62D/I69V | site-directed mutagenesis, the mutant shows 1.68fold increased activity with tris-(2-hydroxyethyl)-methylammonium methylsulfate compared to the wild-type enzyme | Glutamicibacter nicotianae |
1.1.3.17 | A21V/G62D/I69V/S348L | site-directed mutagenesis, the mutant shows 3.45fold increased activity with tris-(2-hydroxyethyl)-methylammonium methylsulfate and highly reduced activity with choline compared to the wild-type enzyme | Glutamicibacter nicotianae |
1.1.3.17 | A21V/G62D/S348C | site-directed mutagenesis, the mutant shows 5.18fold increased activity with tris-(2-hydroxyethyl)-methylammonium methylsulfate and reduced activity with choline compared to the wild-type enzyme | Glutamicibacter nicotianae |
1.1.3.17 | A21V/G62D/S348L | site-directed mutagenesis, the mutant shows 3.72fold increased activity with tris-(2-hydroxyethyl)-methylammonium methylsulfate and highly reduced activity with choline compared to the wild-type enzyme | Glutamicibacter nicotianae |
1.1.3.17 | A21V/G62D/S348L/V349L | site-directed mutagenesis, the mutant shows 5.75fold increased activity with tris-(2-hydroxyethyl)-methylammonium methylsulfate and highly reduced activity with choline compared to the wild-type enzyme | Glutamicibacter nicotianae |
1.1.3.17 | A21V/K394R | site-directed mutagenesis, the mutant shows 85% activity with tris-(2-hydroxyethyl)-methylammonium methylsulfate compared to the wild-type enzyme | Glutamicibacter nicotianae |
1.1.3.17 | F351Y | site-directed mutagenesis in the substrate binding site, the mutant shows reduced activity with choline compared to the wild-type enzyme | Glutamicibacter nicotianae |
1.1.3.17 | G62D | site-directed mutagenesis in the FAD binding site, the mutant shows 2fold increased activity with tris-(2-hydroxyethyl)-methylammonium methylsulfate and reduced activity with choline compared to the wild-type enzyme | Glutamicibacter nicotianae |
1.1.3.17 | G62D/F351Y | site-directed mutagenesis, the mutant shows 2.14fold increased activity with tris-(2-hydroxyethyl)-methylammonium methylsulfate compared to the wild-type enzyme | Glutamicibacter nicotianae |
1.1.3.17 | G62D/R249H/F351Y | site-directed mutagenesis, the mutant shows 2.7fold increased activity with tris-(2-hydroxyethyl)-methylammonium methylsulfate and reduced activity with choline compared to the wild-type enzyme | Glutamicibacter nicotianae |
1.1.3.17 | I69V | site-directed mutagenesis in the FAD binding site, the mutant shows93% activity with tris-(2-hydroxyethyl)-methylammonium methylsulfate compared to the wild-type enzyme | Glutamicibacter nicotianae |
1.1.3.17 | P393Q/S530G | site-directed mutagenesis, the mutant shows 1.5fold increased activity with choline compared to the wild-type enzyme | Glutamicibacter nicotianae |
1.1.3.17 | S348L | site-directed mutagenesis in the substrate binding site | Glutamicibacter nicotianae |
1.1.3.17 | T116I/K128M | site-directed mutagenesis, the mutant shows unaltered activity with choline compared to the wild-type enzyme | Glutamicibacter nicotianae |
1.1.3.17 | T116I/K128M/P393Q/S530G | site-directed mutagenesis, the mutant shows 2.32fold increased activity with choline compared to the wild-type enzyme | Glutamicibacter nicotianae |
1.1.3.17 | V349L | site-directed mutagenesis in the substrate binding site | Glutamicibacter nicotianae |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.3.17 | choline + 2 O2 + H2O2 | Glutamicibacter nicotianae | - |
betaine + 2 H2O2 | - |
? | |
1.1.3.17 | choline + 2 O2 + H2O2 | Glutamicibacter nicotianae DSM Z-ID 96-878 | - |
betaine + 2 H2O2 | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.1.3.17 | Glutamicibacter nicotianae | - |
gene codA | - |
1.1.3.17 | Glutamicibacter nicotianae DSM Z-ID 96-878 | - |
gene codA | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.3.17 | choline + 2 O2 + H2O2 | - |
Glutamicibacter nicotianae | betaine + 2 H2O2 | - |
? | |
1.1.3.17 | choline + 2 O2 + H2O2 | - |
Glutamicibacter nicotianae DSM Z-ID 96-878 | betaine + 2 H2O2 | - |
? | |
1.1.3.17 | additional information | Phe351 is positioned right in the active site of An_CodA and very likely interacts with the bound substrate | Glutamicibacter nicotianae | ? | - |
? | |
1.1.3.17 | additional information | Phe351 is positioned right in the active site of An_CodA and very likely interacts with the bound substrate | Glutamicibacter nicotianae DSM Z-ID 96-878 | ? | - |
? | |
1.1.3.17 | tris-(2-hydroxyethyl)-methylammonium methylsulfate + 2 O2 + H2O2 | - |
Glutamicibacter nicotianae | ? + 2 H2O2 | - |
? | |
1.1.3.17 | tris-(2-hydroxyethyl)-methylammonium methylsulfate + 2 O2 + H2O2 | - |
Glutamicibacter nicotianae DSM Z-ID 96-878 | ? + 2 H2O2 | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.1.3.17 | An_CodA | - |
Glutamicibacter nicotianae |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.1.3.17 | 37 | - |
assay at | Glutamicibacter nicotianae |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.1.3.17 | 9 | - |
assay at | Glutamicibacter nicotianae |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.1.3.17 | FAD | Ala21 is part of an alpha-helix which interacts with the diphosphate moiety of the flavin cofactor and might influence the activity and specificity of the enzyme | Glutamicibacter nicotianae |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.1.3.17 | evolution | choline oxidases belong to the superfamily of glucose-methanol-choline (GMC) oxidoreductases. The three-dimensional structures of the GMC members are highly conserved while their primary sequences can strongly differ according to their different substrate specificities | Glutamicibacter nicotianae |
1.1.3.17 | additional information | enzyme structure modeling, overview | Glutamicibacter nicotianae |