A lysine conserved in the monoamine oxidase family is involved in oxidation of the reduced flavin in mouse polyamine oxidase

Archives of Biochemistry and Biophysics

Volumn 498, Issue 2, 2010, Pages 83-88

  Henderson Pozzi, Michelle ^a   Fitzpatrick, Paul F ^b  

^a TEXAS A AND M UNIVERSITY   (United States)

^b Mays Cancer Center at UT Health San Antonio   (United States)

Author keywords

Enzyme kinetics; Enzyme mechanisms; Flavoproteins; Isotope effects

Indexed keywords

AMINE OXIDASE (FLAVIN CONTAINING); FLAVOPROTEIN; HYDROGEN; LYSINE; METHIONINE; OXYGEN; POLYAMINE OXIDASE; PROTON; QUERCETIN; SOLVENT; WATER;

ARTICLE; CONTROLLED STUDY; ENZYME KINETICS; ENZYME MECHANISM; GENE MUTATION; GENETIC CONSERVATION; HYDROGEN BOND; MOUSE; NONHUMAN; OXIDATION; PH; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN STRUCTURE; STEADY STATE; WILD TYPE;

ANIMALS; HYDROGEN BONDING; HYDROGEN-ION CONCENTRATION; KINETICS; LYSINE; MICE; MONOAMINE OXIDASE; MUTATION, MISSENSE; OXIDATION-REDUCTION; OXIDOREDUCTASES ACTING ON CH-NH GROUP DONORS;

EID: 77953538248     PISSN: 00039861     EISSN: 10960384     Source Type: Journal    
DOI: 10.1016/j.abb.2010.04.015     Document Type: Article

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