TY - JOUR
T1 - Mechanism of inactivation of monoamine oxidase by trans-2-phenylcyclopropylamine and the structure of the enzyme-inactivator adduct
AU - Silverman, R. B.
N1 - Copyright:
Copyright 2004 Elsevier B.V., All rights reserved.
PY - 1983
Y1 - 1983
N2 - Mitochondrial monoamine oxidase was inactivated with 2-[2-14C]phenylcyclopropylamine, dialyzed, and treated with acidic 2,4-dinitrophenylhydrazine. Contrary to the report of Paech et al. (Paech, C., Salach, J.I., and Singer, T.P. (1980) J. Biol. Chem. 255, 2700-2704), the 2,4-dinitrophenylhydrazone obtained was not that of 2-phenylcyclopropanone, but rather of cinnamaldehyde. Furthermore, denaturation of the labeled enzyme in the presence of sodium borohydride resulted in retention of 5.6 times more radioactivity than in its absence. Based on these results, a mechanism of inactivation of monoamine oxidase by 2-phenylcyclopropylamine and the structure of the enzyme-inactivator adduct are proposed.
AB - Mitochondrial monoamine oxidase was inactivated with 2-[2-14C]phenylcyclopropylamine, dialyzed, and treated with acidic 2,4-dinitrophenylhydrazine. Contrary to the report of Paech et al. (Paech, C., Salach, J.I., and Singer, T.P. (1980) J. Biol. Chem. 255, 2700-2704), the 2,4-dinitrophenylhydrazone obtained was not that of 2-phenylcyclopropanone, but rather of cinnamaldehyde. Furthermore, denaturation of the labeled enzyme in the presence of sodium borohydride resulted in retention of 5.6 times more radioactivity than in its absence. Based on these results, a mechanism of inactivation of monoamine oxidase by 2-phenylcyclopropylamine and the structure of the enzyme-inactivator adduct are proposed.
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M3 - Article
C2 - 6654891
AN - SCOPUS:0021025072
SN - 0021-9258
VL - 258
SP - 14766
EP - 14769
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 24
ER -