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Title of Journal: Biotechnol Lett

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Abbravation: Biotechnology Letters

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Springer Netherlands

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DOI

10.1016/0010-8545(83)80019-8

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1573-6776

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Changing the specificity of αamino acid ester hyd

Authors: LiJuan Ye Lu Wang Yue Pan Yi Cao
Publish Date: 2012/05/22
Volume: 34, Issue: 9, Pages: 1719-1724
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Abstract

αAmino acid ester hydrolases AEHs catalyze the synthesis of βlactam antibiotics containing an αamino group with decreased activity toward antibiotics with a phydroxyl group The AEH gene from Xanthomonas rubrillineans was cloned and expressed in Escherichia coli Based on the crystal structure of the AEH and cefprozil complex 13 residues not directly involved in substrate recognition were mutated individually The resulting ~1300 mutants were screened for activity using cefprozil as a model product based on spectrophotometric assay in a 96well format Mutants with improved cefprozil synthetic activity revealed the particular importance of positions 87 131 and 175 for specificity The mutant V131S with the highest initial rates of synthesis toward three phydroxyl cephalosporins showed 23  17  and 64  increase in maximum product accumulation of cefadroxil cefprozil and cefatrizine respectively

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