R
René Floris
Researcher at University of Groningen
Publications - 5
Citations - 234
René Floris is an academic researcher from University of Groningen. The author has contributed to research in topics: Penicillin amidase & Binding site. The author has an hindex of 5, co-authored 5 publications receiving 227 citations.
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Journal ArticleDOI
Characterization of the β-lactam binding site of penicillin acylase of Escherichia coli by structural and site-directed mutagenesis studies
Wynand Alkema,Charles M.H. Hensgens,Els H. Kroezinga,Erik F. J. de Vries,René Floris,Jan-Metske van der Laan,Bauke W. Dijkstra,Dick B. Janssen +7 more
TL;DR: The combined results of the structural and kinetic studies show the importance of alphaF146 in the beta-lactam binding site and provide leads for engineering mutants with improved synthetic properties.
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The use of chromogenic reference substrates for the kinetic analysis of penicillin acylases
TL;DR: The use of chromogenic reference substrates appears to be a rapid and reliable method for determining kinetic constants with various substrates and enzymes.
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Kinetics of enzyme acylation and deacylation in the penicillin acylase-catalyzed synthesis of beta-lactam antibiotics
TL;DR: Values for the relevant kinetic constants for the synthesis and hydrolysis of beta-lactam antibiotics were obtained and 7-aminodesacetoxycephalosporanic acid was a better nucleophile than 6-aminopenicillanic acid, caused by a higher affinity of the enzyme for 7-ADCA and complete suppression of hydrolysed of the acyl-enzyme upon binding of 7- ADCA.
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Cloning, sequence analysis, and expression in Escherichia coli of the gene encoding an α-amino acid ester hydrolase from Acetobacter turbidans
Jolanda J. Polderman-Tijmes,Peter A. Jekel,Erik J. de Vries,Annet E. J. van Merode,René Floris,Jan-Metske van der Laan,Theo Sonke,Dick B. Janssen +7 more
TL;DR: The α-amino acid ester hydrolase from Acetobacter turbidans ATCC 9325 is capable of hydrolyzing and synthesizing β-lactam antibiotics, such as cephalexin and ampicillin, and belongs to a class of hydrolases that is different from the NtnHydrolase superfamily to which the well-characterized penicillin acylase from E. coli belongs.
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Thermodynamic analysis of halide binding to haloalkane dehalogenase suggests the occurrence of large conformational changes
TL;DR: Thermodynamic analysis of bromide binding and release showed that the slow unimolecular isomerization steps in the three‐step bromides export route have considerably larger transition state enthalpies and entropies than those in the other route, which suggests that the three-step route involves different and perhaps larger conformational changes than the two‐step export route.