TY - JOUR
T1 - Enantioselective oxidation of amphetamine by copper-containing quinoprotein amine oxidases from Escherichia coli and Klebsiella oxytoca
AU - Hacisalihoglu, Ayse
AU - Jongejan, Aldo
AU - Jongejan, Jaap A.
AU - Duine, Johannis A.
PY - 2000/12/12
Y1 - 2000/12/12
N2 - The enantioselective properties of copper-containing quinoprotein amine oxidase (EC 1.4.3.6) from Escherichia coli K12 and Klebsiella oxytoca in the kinetic resolution of (R,S)-1-phenyl-2-aminopropane, amphetamine, have been determined. Determination of the enantiomeric ratio, E = (k(cat)/K(M))(R)/(k(cat)/K(M))(S), the ratio of specificity constants for the enantiomeric substrates, can be accomplished in several ways. For practical reasons, we calculated E using non-linear regression analysis of initial rate data obtained at a fixed overall concentration of amphetamine mixtures of chiral composition ranging from 0 to 50% (R)-(-)-amphetamine [Jongejan et al., Recl. Trav. Chim. Pays-Bas 110 (1990) 247]. It is found that both enzymes catalyze the enantioselective oxidation of amphetamine with E-values of sufficient magnitude (E ≃ 15) which may open the possibility for future application of amine oxidase-catalyzed kinetic resolutions of racemic amphetamine. The preference for the (R)-enantiomer of amphetamine is in agreement with the pro-S specificity that has been observed for the conversion of 2-phenylethylamine. Rationalization of this observation, based on the structure of the E. coli amine oxidase, is discussed. (C) 2000 Elsevier Science B.V.
AB - The enantioselective properties of copper-containing quinoprotein amine oxidase (EC 1.4.3.6) from Escherichia coli K12 and Klebsiella oxytoca in the kinetic resolution of (R,S)-1-phenyl-2-aminopropane, amphetamine, have been determined. Determination of the enantiomeric ratio, E = (k(cat)/K(M))(R)/(k(cat)/K(M))(S), the ratio of specificity constants for the enantiomeric substrates, can be accomplished in several ways. For practical reasons, we calculated E using non-linear regression analysis of initial rate data obtained at a fixed overall concentration of amphetamine mixtures of chiral composition ranging from 0 to 50% (R)-(-)-amphetamine [Jongejan et al., Recl. Trav. Chim. Pays-Bas 110 (1990) 247]. It is found that both enzymes catalyze the enantioselective oxidation of amphetamine with E-values of sufficient magnitude (E ≃ 15) which may open the possibility for future application of amine oxidase-catalyzed kinetic resolutions of racemic amphetamine. The preference for the (R)-enantiomer of amphetamine is in agreement with the pro-S specificity that has been observed for the conversion of 2-phenylethylamine. Rationalization of this observation, based on the structure of the E. coli amine oxidase, is discussed. (C) 2000 Elsevier Science B.V.
KW - (R,S)-1-phenyl-2-aminopropane
KW - Amphetamine
KW - Copper-containing quinoprotein amine oxidase
KW - Enantiomeric ratio
KW - Escherichia coli
KW - Kinetic resolution
KW - Klebsiella oxytoca
UR - http://www.scopus.com/inward/record.url?scp=0034642366&partnerID=8YFLogxK
U2 - https://doi.org/10.1016/S1381-1177(00)00216-2
DO - https://doi.org/10.1016/S1381-1177(00)00216-2
M3 - Article
SN - 1381-1177
VL - 11
SP - 81
EP - 88
JO - Journal of Molecular Catalysis - B Enzymatic
JF - Journal of Molecular Catalysis - B Enzymatic
IS - 2-3
ER -