Academic literature on the topic 'Isopenicillin N'

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Journal articles on the topic "Isopenicillin N"

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Baldwin, Jack E., and Mark Bradley. "Isopenicillin N synthase: mechanistic studies." Chemical Reviews 90, no. 7 (November 1990): 1079–88. http://dx.doi.org/10.1021/cr00105a001.

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Chapman, Nicole C., and Peter J. Rutledge. "Isopenicillin N Synthase: Crystallographic Studies." ChemBioChem 22, no. 10 (March 25, 2021): 1687–705. http://dx.doi.org/10.1002/cbic.202000743.

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Lau, Rute Madeira, Jacques T. H. van Eupen, Dick Schipper, Godefridus I. Tesser, Jan Verweij, and Erik de Vroom. "Synthesis of Penicillin N and Isopenicillin N." Tetrahedron 56, no. 38 (September 2000): 7601–6. http://dx.doi.org/10.1016/s0040-4020(00)00673-6.

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Chen, V. J., A. M. Orville, M. R. Harpel, C. A. Frolik, K. K. Surerus, E. Münck, and J. D. Lipscomb. "Spectroscopic Studies of Isopenicillin N Synthase." Journal of Biological Chemistry 264, no. 36 (December 1989): 21677–81. http://dx.doi.org/10.1016/s0021-9258(20)88239-8.

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Baldwin, Jack E., Mark Bradley, Shaun D. Abbott, and Robert M. Adlington. "New penicillins from isopenicillin N synthase." Tetrahedron 47, no. 28 (January 1991): 5309–28. http://dx.doi.org/10.1016/s0040-4020(01)87142-8.

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Huffman, George W., Paul D. Gesellchen, Jan R. Turner, Robert B. Rothenberger, Harold E. Osborne, F. Dean Miller, Jerry L. Chapman, and Stephen W. Queener. "Substrate specificity of isopenicillin N synthase." Journal of Medicinal Chemistry 35, no. 10 (May 1992): 1897–914. http://dx.doi.org/10.1021/jm00088a028.

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Sim, T. S., and P. Loke. "Molecular studies on isopenicillin N synthases." Applied Microbiology and Biotechnology 54, no. 1 (July 14, 2000): 1–8. http://dx.doi.org/10.1007/s002530000347.

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Huffman, George W. "IMPROVED PREPARATION OF PENICILLIN N AND ISOPENICILLIN N." Organic Preparations and Procedures International 20, no. 5 (October 1988): 497–503. http://dx.doi.org/10.1080/00304948809356295.

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Jensen, Susan E., Brenda K. Leskiw, Leo C. Vining, Yair Aharonowitz, Donald W. S. Westlake, and Saul Wolfe. "Purification of isopenicillin N synthetase from Streptomyces clavuligerus." Canadian Journal of Microbiology 32, no. 12 (December 1, 1986): 953–58. http://dx.doi.org/10.1139/m86-176.

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Isopenicillin N synthetase was purified from Streptomyces clavuligerus by sequential salt precipitation, ion-exchange and gel-filtration chromatography using both conventional open column and high-performance liquid chromatographic techniques. Material from the final purification step had a specific activity of 204.1 × 10−3 units/mg of protein which represented a 130-fold purification over the cell-free extract. The purified isopenicillin N synthetase was determined to have a molecular weight of 33 000 by sodium dodecyl sulfate – polyacrylamide gel electrophoresis and to have a Km of 0.32 mM with respect to its substrate δ-(L-α-aminoadipyl)-L-cysteinyl-D-valine. The enzyme showed a sensitivity to thiol-specific inhibitors with N-ethylmaleimide giving the strongest inhibitory effect.
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Loke, Paxton, and Tiow-Suan Sim. "Mutational analysis of conserved glycines 42 and 256 in Cephalosporium acremonium isopenicillin N synthase." Canadian Journal of Microbiology 47, no. 10 (October 1, 2001): 961–64. http://dx.doi.org/10.1139/w01-101.

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Isopenicillin N synthase (IPNS) is critical for the catalytic conversion of δ -(L-α-aminoadipoyl)-L-cysteinyl-D-valine to isopenicillin N in the penicillin and cephalosporin biosynthetic pathway. Two conserved glycine residues in Cephalosporium acremonium IPNS (cIPNS), namely glycine-42 and glycine-256, were identified by multiple sequence alignment and investigated by site-directed mutagenesis to study the effect of the substitution on catalysis. Our study showed that both the mutations from glycine to alanine or to serine reduced the catalytic activity of cIPNS and affected its soluble expression in a heterologous host at 37°C. Soluble expression was restored at a reduced temperature of 25°C, and thus, it is possible that these glycine residues may have a role in maintaining the local protein structure and are critical for the soluble expression of cIPNS.Key words: isopenicillin N synthase, site-directed mutagenesis, glycine, Cephalosporium acremonium.
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Dissertations / Theses on the topic "Isopenicillin N"

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Fujishima, Yoshiyuki. "Studies on isopenicillin N synthase." Thesis, University of Oxford, 1992. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.305979.

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Bradley, Mark. "Mechanism of isopenicillin N synthase." Thesis, University of Oxford, 1989. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.236117.

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Furuse, Reiko. "Mechanistic investigations into isopenicillin N synthase." Thesis, University of Oxford, 1992. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.305450.

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Daruzzaman, Adam. "Mechanistic studies on isopenicillin N synthase." Thesis, University of Oxford, 2002. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.289399.

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Turner, N. J. "Mechanistic studies on isopenicillin N synthase." Thesis, University of Oxford, 1985. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.355820.

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Abbott, Shaun Douglas. "Mechanistic studies on isopenicillin N synthase." Thesis, University of Oxford, 1991. https://ora.ox.ac.uk/objects/uuid:0124fa37-2d7a-43b5-a3e9-c49be4125be2.

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The mechanism of penicillin formation through the action of the enzyme isopenicillin N synthase (IPNS) on the substrate δ-(L-α-aminoadipoyl)-L-cysteinyl-D-valine and synthetic analogues, still raises many unresolved questions, despite many years' extensive investigation. In order to investigate the stereochemistry of formation of the second ring in the product, N-δ-(L-α-aminoadipoyl)-3α-hydroxymethylpenicillin, resulting from incubation of δ-(L-α-aminoadipoyl)- L-cysteinyl-D-vinylglycine with IPNS, the deuterium labelled tripeptides δ-(L-α-aminoadipoyl)- L-cysteinyl-E-[3,4-2H2]-D-vinylglycine and δ-(L-α-aminoadipoyl)-L-cysteinyl- Z-[3,4-2H2]-D-vinylglycine were synthesised and incubated with recombinant IPNS. The pattern of deuterium labelling was retained in the penam products, indicating stereospecific ring closure. The unlabelled and labelled penicillins were converted to their corresponding γ-lactones, and the 1H NMR coupling constants for the C(3)H-C(8)H2 system used to assign the 8-Pro/? and 8-ProS resonances of the unlabelled lactone. Comparison with the labelled lactones indicated that the parent penicillins had been formed via syn addition of sulphur and oxygen across the double bonds of the respective tripeptides. This stereochemistry is consistent with a mechanism involving [2πs + 2π] cycloaddition of an Fe=O species to the olefln.
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Fung, Kwok Wing. "Models and mimics of Isopenicillin N Synthase." Thesis, University of Oxford, 1993. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.335777.

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Pitt, A. R. "Stereochemistry and mechanism of isopenicillin N synthase." Thesis, University of Oxford, 1988. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.235052.

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Brown, Toby James Neville. "Analytical studies of some amino acid secondary metabolism." Thesis, University of Oxford, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.300806.

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Fletcher, Clare Alison. "Studies on the mechanism of isopenicillin-n-synthase." Thesis, University of Oxford, 1993. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.239289.

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Book chapters on the topic "Isopenicillin N"

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Martín, Juan F., Ricardo V. Ullán, and Javier Casqueiro. "Novel Genes Involved in Cephalosporin Biosynthesis: The Three-component Isopenicillin N Epimerase System." In Molecular Biotechnolgy of Fungal beta-Lactam Antibiotics and Related Peptide Synthetases, 91–109. Berlin, Heidelberg: Springer Berlin Heidelberg, 2004. http://dx.doi.org/10.1007/b99258.

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"Isopenicillin-N epimerase." In Class 4–6 Lyases, Isomerases, Ligases, 481–85. Berlin, Heidelberg: Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-540-85707-5_98.

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