AN ADDITIONAL IONIC BOND SUGGESTED BY MOLECULAR MODELING OF TEM-2 MIGHT INDUCE A SLIGHT DISCREPANCY BETWEEN CATALYTIC PROPERTIES OF TEM-1 AND TEM-2 BETA-LACTAMASES
Eb. Chaibi et al., AN ADDITIONAL IONIC BOND SUGGESTED BY MOLECULAR MODELING OF TEM-2 MIGHT INDUCE A SLIGHT DISCREPANCY BETWEEN CATALYTIC PROPERTIES OF TEM-1 AND TEM-2 BETA-LACTAMASES, FEMS microbiology letters, 143(2-3), 1996, pp. 121-125
The plasmid-mediated TEM-1 and TEM-2 beta-lactamases are the most comm
only encountered among Gram-negative bacteria. They belong to molecula
r class A, and differ by one amino acid at position 39: TEM-1 have a g
lutamine and TEM-2 a lysine. Kinetic parameters (k(cat) and K-m) and c
atalytic efficiency (k(cat)/K-m) of TEM-1 and TEM-2 beta-lactamases ar
e slightly, but significantly different. For all antibiotics except me
thicillin and cefazolin, the catalytic efficiency values of TEM-2 are
clearly greater than that of TEM-1. Molecular modelling of TEM-2, when
compared to that of TEM-1, showed an additional ionic bond between Ly
s-39 and Glu-281.