The trimethylammonium headgroup of choline is a major determinant for substrate binding and specificity in choline oxidase

Archives of Biochemistry and Biophysics

Volumn 430, Issue 2, 2004, Pages 264-273

  Gadda, Giovanni ^a   Powell, Nichole L N ^a   Menon, Prashanthi ^a  

^a GEORGIA STATE UNIVERSITY   (United States)

Author keywords

Binding energy; Choline oxidase; Competitive inhibitor; Covalent FAD; Difference spectrum; Flavoprotein; N,N Dimethylethanolamine; N Methylethanolamine; Substrate specificity; Trimethylammonium

Indexed keywords

2 METHYLAMINOETHANOL; AMINE; BETAINE DERIVATIVE; CARBOXYLIC ACID; CHOLINE DERIVATIVE; LIGAND; METHYL GROUP; OXIDOREDUCTASE; SARCOSINE; TRIMETHYLAMMONIUM SALT DERIVATIVE;

BINDING AFFINITY; COMPETITIVE INHIBITION; CONFERENCE PAPER; ENZYME SPECIFICITY; ENZYME SUBSTRATE COMPLEX; PH; PRIORITY JOURNAL;

ALCOHOL OXIDOREDUCTASES; BETAINE; CHOLINE; HYDROGEN-ION CONCENTRATION; KINETICS; RECOMBINANT PROTEINS; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY;

EID: 4444281751     PISSN: 00039861     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.abb.2004.07.011     Document Type: Conference Paper

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