Summary
The stereoselectivity of penicillin amidase (PA, EC 3.5.1.11) from E coli and homologeous enzymes from other sources has been determined as a function of temperature and substrate for hydrolysis and kinetically controlled synthesis. The stereoselectivity of these reactions decreased almost by one order of magnitude from 5 to 45°C. It increased with the substrate (k cat/K m) and nucleophile (k T/k H) specificity, and was found to differ in the S1- (R-specific) and S′1-(S-specific)-binding subsites of the active site. The S1-stereoselectivity was determined mainly by differences in the activation energy, i.e. the turnover number. The stereoselectivity of PA from different sources differed by almost an order of magnitude for the same substrate.
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Kasche, V., Galunsky, B., Nurk, A. et al. The dependency of the stereoselectivity of penicillin amidases-enzymes with R-specific S1- and S-specific S′1-subsites- on temperature and primary structure. Biotechnol Lett 18, 455–460 (1996). https://doi.org/10.1007/BF00143470
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DOI: https://doi.org/10.1007/BF00143470