A lysine conserved in the monoamine oxidase family is involved in oxidation of the reduced flavin in mouse polyamine oxidase
MH Pozzi, PF Fitzpatrick
Index: Henderson Pozzi, Michelle; Fitzpatrick, Paul F. Archives of Biochemistry and Biophysics, 2010 , vol. 498, # 2 p. 83 - 88
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Citation Number: 23
Abstract
Lysine 315 of mouse polyamine amine oxidase corresponds to a lysine residue that is conserved in the flavoprotein amine oxidases of the monoamine oxidase structural family. In several structures, this lysine residue forms a hydrogen bond to a water molecule that is hydrogen-bonded to the flavin N (5). Mutation of Lys315 in polyamine oxidase to methionine was previously shown to have no effect on the kinetics of the reductive half-reaction of the ...
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