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Literature summary for 1.1.3.17 extracted from

  • Rungsrisuriyachai, K.; Gadda, G.
    On the role of histidine 351 in the reaction of alcohol oxidation catalyzed by choline oxidase (2008), Biochemistry, 47, 6762-6769.
    View publication on PubMed
Search for more literature for 1.1.3.17

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli, wild-type and H351A variant, plasmid pET/codAmg1-H351A Arthrobacter globiformis

Crystallization (Commentary)

Crystallization (Comment) Organism
active site of wild-type choline oxidase, resolution of 1.86 A Arthrobacter globiformis

Protein Variants

Protein Variants Comment Organism
H351A generated by site-directed mutagenesis Arthrobacter globiformis

Inhibitors

Inhibitors Comment Organism Structure
glycine betaine pH dependence of the kcat and kcat/Km values for glycine betaine inhibition shown, inhibition of H351A enzyme maximal at low pH and reduced with increasing pH Arthrobacter globiformis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
choline + O2 Arthrobacter globiformis
-
 betaine aldehyde + H2O2
-
 ?

Organism

Organism UniProt Comment Textmining
Arthrobacter globiformis Q7X2H8 strain ATCC 8010
-

Purification (Commentary)

Purification (Comment) Organism
wild-type and mutant protein, purified enzymes have 50-70% of the enzyme-bound flavin cofactor as an air-stable anionic flavosemiquinone, converts slowly to oxidized state by extensive dialysis at pH 6 and 4°C Arthrobacter globiformis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 pH dependence of substrate deuterium isotope effects and of the kcat and kcat/Km values for choline in the mutant variant H351A determined, steady-state kinetic parameters compared between H351A mutant and wild-type, His351 important but not essential for the reductive half-reaction of choline oxidation, contributes to substrate binding and to the overall polarity of the active site Arthrobacter globiformis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
choline + O2
-
 Arthrobacter globiformis betaine aldehyde + H2O2
-
 ?
choline + O2 choline shown to be a slow substrate for H351A variant, His351 residue important for substrate binding and hydride transfer reaction Arthrobacter globiformis betaine aldehyde + H2O2
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 activity assay at Arthrobacter globiformis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
 additional information overall turnover of mutant variant about 60-fold decreased with choline compared to wild-type enzyme Arthrobacter globiformis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
10
-
 activity assay at, in 50 mM sodium pyrophosphate, neutral hydroquinone species of the flavin stabilized in the H351A enzyme at Arthrobacter globiformis

pH Range

pH Minimum pH Maximum Comment Organism
5 10 varying concentrations of both choline and oxygen, between pH 7 and pH 10, Km values for oxygen less than 15 microM Arthrobacter globiformis

Cofactor

Cofactor Comment Organism Structure
FAD His351 stabilizes transition state for hydride transfer reaction to flavin, is not involved in the activation of the reduced flavin for reaction with oxygen Arthrobacter globiformis