An additional ionic bond suggested by molecular modelling of TEM-2 might induce a slight discrepancy between catalytic properties of TEM-1 and TEM-2 β-lactamases
Open Access
- 1 October 1996
- journal article
- research article
- Published by Oxford University Press (OUP) in FEMS Microbiology Letters
- Vol. 143 (2-3) , 121-125
- https://doi.org/10.1111/j.1574-6968.1996.tb08470.x
Abstract
The plasmid-mediated TEM-1 and TEM-2 β-lactamases are the most commonly encountered among Gram-negative bacteria. They belong to molecular class A, and differ by one amino acid at position 39: TEM-1 have a glutamine and TEM-2 a lysine. Kinetic parameters (kcat and Km) and catalytic efficiency (kcat/Km) of TEM-1 and TEM-2 β-lactamases are slightly, but significantly different. For all antibiotics except methicillin 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 Lys-39 and Glu-281.Keywords
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