Any feedback?
Literature summary extracted from
- Engineering of choline oxidase from Arthrobacter nicotianae for potential use as biological bleach in detergents (2010), Appl. Microbiol. Biotechnol., 87, 1743-1752.
Cloned(Commentary)
| 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 |
Protein Variants
| 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 |
Natural Substrates/ Products (Substrates)
| 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 | - |
? | |
Organism
| 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 | - |
Substrates and Products (Substrate)
| 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 | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.1.3.17 | An_CodA | - |
Glutamicibacter nicotianae |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.1.3.17 | 37 | - |
assay at | Glutamicibacter nicotianae |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.1.3.17 | 9 | - |
assay at | Glutamicibacter nicotianae |
Cofactor
| 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 | |
General Information
| 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 |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
