8번째 carboxylesterase family에 속하는 EstU1의 beta-lactamase 활성에 대한 구조기반 연구

Abstract

EstU1 is a remarkable family VIII carboxylesterase in that it exhibits hydrolytic activity towards the amide bond of clinically-used b-lactam antibiotics as well as the ester bond of p-nitrophenyl esters. The crystal structures of EstU1 and the EstU1/cephalothin complex revealed the structural basis for the catalytic feature. Structural and sequential comparison of EstU1 with other family VIII carboxylesterases that cannot cleave clinically-used b-lactam antibiotics provides insights into an operative molecular strategy of family VIII carboxylesterases to extend their substrate spectrum. the EstU1/cephalothin complex revealed the structural basis for the catalytic feature. Structural and sequential comparison of EstU1 with other family VIII carboxylesterases that cannot cleave clinically-used b-lactam antibiotics provides insights into an operative molecular strategy of family VIII carboxylesterases to extend their substrate spectrum.