Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.1.3.17 extracted from

  • Ribitsch, D.; Winkler, S.; Gruber, K.; Karl, W.; Wehrschuetz-Sigl, E.; Eiteljoerg, I.; Schratl, P.; Remler, P.; Stehr, R.; Bessler, C.; Mussmann, N.; Sauter, K.; Maurer, K.H.; Schwab, H.
    Engineering of choline oxidase from Arthrobacter nicotianae for potential use as biological bleach in detergents (2010), Appl. Microbiol. Biotechnol., 87, 1743-1752.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene codA, expression of Strep-tagged wild-type and mutant enzymes in Escherichia coli strain BL21-Gold Glutamicibacter nicotianae

Protein Variants

Protein Variants Comment Organism
A21V site-directed mutagenesis in the FAD binding site Glutamicibacter nicotianae
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
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
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
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
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
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
A21V/K394R site-directed mutagenesis, the mutant shows 85% activity with tris-(2-hydroxyethyl)-methylammonium methylsulfate compared to the wild-type enzyme Glutamicibacter nicotianae
F351Y site-directed mutagenesis in the substrate binding site, the mutant shows reduced activity with choline compared to the wild-type enzyme Glutamicibacter nicotianae
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
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
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
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
P393Q/S530G site-directed mutagenesis, the mutant shows 1.5fold increased activity with choline compared to the wild-type enzyme Glutamicibacter nicotianae
S348L site-directed mutagenesis in the substrate binding site Glutamicibacter nicotianae
T116I/K128M site-directed mutagenesis, the mutant shows unaltered activity with choline compared to the wild-type enzyme Glutamicibacter nicotianae
T116I/K128M/P393Q/S530G site-directed mutagenesis, the mutant shows 2.32fold increased activity with choline compared to the wild-type enzyme Glutamicibacter nicotianae
V349L site-directed mutagenesis in the substrate binding site Glutamicibacter nicotianae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
choline + 2 O2 + H2O2 Glutamicibacter nicotianae
-
betaine + 2 H2O2
-
?
choline + 2 O2 + H2O2 Glutamicibacter nicotianae DSM Z-ID 96-878
-
betaine + 2 H2O2
-
?

Organism

Organism UniProt Comment Textmining
Glutamicibacter nicotianae
-
gene codA
-
Glutamicibacter nicotianae DSM Z-ID 96-878
-
gene codA
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
choline + 2 O2 + H2O2
-
Glutamicibacter nicotianae betaine + 2 H2O2
-
?
choline + 2 O2 + H2O2
-
Glutamicibacter nicotianae DSM Z-ID 96-878 betaine + 2 H2O2
-
?
additional information Phe351 is positioned right in the active site of An_CodA and very likely interacts with the bound substrate Glutamicibacter nicotianae ?
-
?
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 ?
-
?
tris-(2-hydroxyethyl)-methylammonium methylsulfate + 2 O2 + H2O2
-
Glutamicibacter nicotianae ? + 2 H2O2
-
?
tris-(2-hydroxyethyl)-methylammonium methylsulfate + 2 O2 + H2O2
-
Glutamicibacter nicotianae DSM Z-ID 96-878 ? + 2 H2O2
-
?

Synonyms

Synonyms Comment Organism
An_CodA
-
Glutamicibacter nicotianae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Glutamicibacter nicotianae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9
-
assay at Glutamicibacter nicotianae

Cofactor

Cofactor Comment Organism Structure
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

General Information Comment Organism
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
additional information enzyme structure modeling, overview Glutamicibacter nicotianae