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Literature summary extracted from

  • Quaye, O.; Lountos, G.T.; Fan, F.; Orville, A.M.; Gadda, G.
    Role of Glu312 in binding and positioning of the substrate for the hydride transfer reaction in choline oxidase (2008), Biochemistry, 47, 243-256.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.3.17 expressed in Escherichia coli, strain Rosetta(DE3)pLysS, pET/codAmg plasmid, wild-type and Glu312 variants generated by site-directed mutagenesis Arthrobacter globiformis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.3.17 crystal structure determined by synchrotron X-ray radiation, refined to a resolution of 1.86 A, data collected at 100 K Arthrobacter globiformis

Protein Variants

EC Number Protein Variants Comment Organism
1.1.3.17 E312A generated for investigation of the negative charge on Glu312, enzyme inactive Arthrobacter globiformis
1.1.3.17 E312D generated for investigation of the negative charge on Glu312, kcat values about 230times lower and and kcat/Km values about 35times lower than in the wild-type, solvent viscosity and substrate kinetic isotope effects indicates presence of internal equilibrium prior to the hydride transfer reaction Arthrobacter globiformis
1.1.3.17 E312Q generated for investigation of the negative charge on Glu312, Kd value for choline about 500times larger than that of wild-type Arthrobacter globiformis

Natural Substrates/ Products (Substrates)

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
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.3.17 Arthrobacter globiformis Q7X2H8
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.3.17 wild-type and mutant variants Arthrobacter globiformis

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.3.17 additional information
-
 X-ray data collection and mutant analysis, steady-state kinetic parameters, pH profiles, substrate kinetic isotope effects for mutants and wild-type determined Arthrobacter globiformis

Substrates and Products (Substrate)

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 choline + O2 spatial location of the negative charge on residue 312 important for oxidation of alcohol substrate Arthrobacter globiformis betaine aldehyde + H2O2
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.3.17 25
-
 activity assay at, rate of oxygen consumption Arthrobacter globiformis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.1.3.17 5 10 pH profiles of kinetic parameters with choline as a substrate Arthrobacter globiformis

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.3.17 FAD covalent binding of FAD to purified proteins ascertained, rates of flavin reduction determined in wild-type and mutant variants Arthrobacter globiformis