Structural Characterization and Mapping of the Covalently Linked FAD Cofactor in Choline Oxidase from Arthrobacter globiformis

The flavoenzyme choline oxidase catalyzes the oxidation of choline and betaine aldehyde to betaine. Earlier studies have shown that the choline oxidase from Arthrobacter globiformis contains FAD covalently linked to a histidine residue. To identify the exact type of flavin binding, the FAD-carrying...

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Veröffentlicht in:	Biochemistry (Easton) 2003-06, Vol.42 (23), p.7188-7194
Hauptverfasser:	Rand, Thomas, Halkier, Torben, Hansen, Ole C.
Format:	Artikel
Sprache:	eng
Schlagworte:	Alcohol Oxidoreductases - chemistry Amino Acid Sequence Arthrobacter - enzymology Flavin-Adenine Dinucleotide - chemistry Histidine - chemistry Hydrogen-Ion Concentration Hydrolysis Oxidation-Reduction Peptide Fragments - analysis Spectrometry, Fluorescence - methods Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization - methods Trypsin - metabolism
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