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Literature summary for 1.1.3.17 extracted from

  • Su, D.; Smitherman, C.; Gadda, G.
    A metastable photoinduced protein-flavin adduct in choline oxidase, an enzyme not involved in light-dependent processes (2020), J. Phys. Chem. B, 124, 3936-3943 .
    View publication on PubMed
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Protein Variants

Protein Variants Comment Organism
H466Q the unusual fluorescence behavior of the enzyme is lost in the mutant Arthrobacter globiformis
S101A the unusual fluorescence behavior of the enzyme persists in the mutant Arthrobacter globiformis

Organism

Organism UniProt Comment Textmining
Arthrobacter globiformis Q7X2H8
-
-

Synonyms

Synonyms Comment Organism
codA
-
 Arthrobacter globiformis

Cofactor

Cofactor Comment Organism Structure
FMN the enzyme-bound flavin shows a progressive shift of the fluorescence excitation maximum (lambdaex) from 468 to 399 nm with increasing pH value between pH 6.0 and 10.0, consistent with a metastable photoinduced protein-flavin adduct. In contrast, the maximal lambdaem is independent of pH, with values of about 526 nm Arthrobacter globiformis

General Information

General Information Comment Organism
metabolism observation of an unusual fluorescence excitation spectrum in choline oxidase at alkaline pH. Physiologically, choline oxidase oxidizes choline to betaine through two FAD-associated reactions and is not a photoenzyme. The enzyme-bound flavin shows a progressive shift of the fluorescence excitation maximum (lambdaex) from 468 to 399 nm with increasing pH value between pH 6.0 and 10.0, consistent with a metastable photoinduced protein-flavin adduct. In contrast, the maximal lambdaem is independent of pH, with values of about 526 nm. The unusual behavior of the enzyme persists in the mutated S101A enzyme variant but is eliminated in the H466Q variant Arthrobacter globiformis