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Journal articles on the topic 'Isopenicillin N'

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Published: 4 June 2021
Last updated: 1 February 2022

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1

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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2

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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3

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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4

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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5

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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6

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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7

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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8

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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9

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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10

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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11

Loke, Paxton, Chee Pang Ng, and Tiow-Suan Sim. "PCR cloning, heterologous expression, and characterization of isopenicillin N synthase fromStreptomyces lipmaniiNRRL 3584." Canadian Journal of Microbiology 46, no. 2 (February 1, 2000): 166–70. http://dx.doi.org/10.1139/w99-127.

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A key step which involves the cyclization of δ-(L-α-aminoadipyl)-L-cysteinyl-D-valine to the bicyclic ring structure of isopenicillin N in the penicillin and cephalosporin biosynthetic pathway, is catalyzed by isopenicillin N synthase (IPNS). In this study, an IPNS gene from Streptomyces lipmanii NRRL 3584 (slIPNS) was cloned via PCR-based homology cloning, sequenced and expressed in Escherichia coli. Soluble slIPNS was overexpressed up to 21% of total soluble protein, and verified to be functionally active when in an IPNS enzymatic assay. Sequence comparison of the slIPNS gene obtained (excluding the consensus primer sequences) with another cloned IPNS from S. lipmanii 16884.3, revealed one three-nucleotide deletion and three closely-spaced single nucleotide deletions. Futhermore, this paper also reports the first instance of the usage of PCR as an alternative and rapid strategy for IPNS cloning using consensus primers. Key words: isopenicillin N synthase, β-lactam antibiotics, secondary metabolism, consensus primers.
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12

Lau, Rute Madeira, Jacques T. H. van Eupen, Dick Schipper, Godefridus I. Tesser, Jan Verweij, and Erik de Vroom. "ChemInform Abstract: Synthesis of Penicillin N and Isopenicillin N." ChemInform 32, no. 1 (January 2, 2001): no. http://dx.doi.org/10.1002/chin.200101229.

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13

Schenk, Wolfdieter A. "Isopenicillin N Synthase: An Enzyme at Work." Angewandte Chemie 39, no. 19 (October 2, 2000): 3409–11. http://dx.doi.org/10.1002/1521-3773(20001002)39:19<3409::aid-anie3409>3.0.co;2-t.

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14

BALDWIN, J. E., and M. BRADLEY. "ChemInform Abstract: Isopenicillin N Synthase: Mechanistic Studies." ChemInform 22, no. 8 (August 23, 2010): no. http://dx.doi.org/10.1002/chin.199108385.

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15

Ramos, F. R., M. J. Lopez-Nieto, and J. F. Martin. "Isopenicillin N Synthetase of Penicillium chrysogenum, an Enzyme That Converts -(L- -Aminoadipyl)-L-Cysteinyl-D-Valine to Isopenicillin N." Antimicrobial Agents and Chemotherapy 28, no. 3 (September 1, 1985): 464. http://dx.doi.org/10.1128/aac.28.3.464-a.

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16

Loke, Paxton, and Tiow-Suan Sim. "Site-Directed Mutagenesis of Proline-285 to Leucine in Cephalosporium acremonium Isopenicillin N - Synthase Affects Catalysis and Increases Soluble Expression at Higher Temperatures." Zeitschrift für Naturforschung C 56, no. 5-6 (June 1, 2001): 413–15. http://dx.doi.org/10.1515/znc-2001-5-615.

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The conversion of δ-(ʟ-α-aminoadipyl)-ʟ-cysteinyl-ᴅ-valine (ACV) to isopenicillin N is dependant on the catalytic action of isopenicillin N - synthase (IPNS), an important enzyme in the penicillin and cephalosporin biosynthetic pathway. One of the amino acid residues suggested by the Aspergillus nidulans IPNS crystal structure for interaction with the valine isopropyl group of ACV is proline-283. Site-directed mutagenesis of the corresponding proline- 285 to leucine in Cephalosporium acremonium IPNS resulted in non-measurable activity but an increased soluble expression at higher temperatures in a heterologous E. coli host.
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17

BALDWIN, JACK E., STEPHEN J. KILLIN, ANDREW J. PRATT, JOHN D. SUTHERLAND, NICHOLAS J. TURNER, M. JAMES C. CRABBE, EDWARD P. ABRAHAM, and ANTHONY C. WILLIS. "Purification and characterization of cloned isopenicillin N synthetase." Journal of Antibiotics 40, no. 5 (1987): 652–59. http://dx.doi.org/10.7164/antibiotics.40.652.

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18

Schenk, Wolfdieter A. "Isopenicillin-N-Synthase: ein Enzym bei der Arbeit." Angewandte Chemie 112, no. 19 (October 2, 2000): 3551–54. http://dx.doi.org/10.1002/1521-3757(20001002)112:19<3551::aid-ange3551>3.0.co;2-5.

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19

BALDWIN, J. E., M. BRADLEY, S. D. ABBOTT, and R. M. ADLINGTON. "ChemInform Abstract: New Penicillins from Isopenicillin N Synthase." ChemInform 22, no. 40 (August 22, 2010): no. http://dx.doi.org/10.1002/chin.199140254.

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20

Baldwin, Jack E., Gregory P. Lynch, and Christopher J. Schofield. "Isopenicillin N synthase: a new mode of reactivity." Journal of the Chemical Society, Chemical Communications, no. 10 (1991): 736. http://dx.doi.org/10.1039/c39910000736.

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21

Baldwin, Jack E., Robert M. Adlington, M. Bradley, N. J. Turner, and A. R. Pitt. "Evidence for epoxide formation from isopenicillin N synthase." Journal of the Chemical Society, Chemical Communications, no. 15 (1989): 978. http://dx.doi.org/10.1039/c39890000978.

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22

Baldwin, Jack E., Simon E. Moroney, and Hong-Hoi Ting. "A coupled enzyme assay for isopenicillin N synthetase." Analytical Biochemistry 145, no. 1 (February 1985): 183–87. http://dx.doi.org/10.1016/0003-2697(85)90345-8.

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23

Ramos, F. R., M. J. Lopez-Nieto, and J. F. Martin. "Isopenicillin N synthetase of Penicillium chrysogenum, an enzyme that converts delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine to isopenicillin N." Antimicrobial Agents and Chemotherapy 27, no. 3 (March 1, 1985): 380–87. http://dx.doi.org/10.1128/aac.27.3.380.

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24

Rabe, Patrick, Jos J. A. G. Kamps, Kyle D. Sutherlin, James D. S. Linyard, Pierre Aller, Cindy C. Pham, Hiroki Makita, et al. "X-ray free-electron laser studies reveal correlated motion during isopenicillin N synthase catalysis." Science Advances 7, no. 34 (August 2021): eabh0250. http://dx.doi.org/10.1126/sciadv.abh0250.

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Isopenicillin N synthase (IPNS) catalyzes the unique reaction of l-δ-(α-aminoadipoyl)-l-cysteinyl-d-valine (ACV) with dioxygen giving isopenicillin N (IPN), the precursor of all natural penicillins and cephalosporins. X-ray free-electron laser studies including time-resolved crystallography and emission spectroscopy reveal how reaction of IPNS:Fe(II):ACV with dioxygen to yield an Fe(III) superoxide causes differences in active site volume and unexpected conformational changes that propagate to structurally remote regions. Combined with solution studies, the results reveal the importance of protein dynamics in regulating intermediate conformations during conversion of ACV to IPN. The results have implications for catalysis by multiple IPNS-related oxygenases, including those involved in the human hypoxic response, and highlight the power of serial femtosecond crystallography to provide insight into long-range enzyme dynamics during reactions presently impossible for nonprotein catalysts.
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25

Krall, Jordan A., Peter J. Rutledge, and Jack E. Baldwin. "Design and synthesis of an isopenicillin N synthase mimic." Tetrahedron 61, no. 1 (January 2005): 137–43. http://dx.doi.org/10.1016/j.tet.2004.10.041.

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26

Roelofs, Dick, Martijn J. T. N. Timmermans, Paul Hensbergen, Hans van Leeuwen, Jessica Koopman, Anna Faddeeva, Wouter Suring, et al. "A Functional Isopenicillin N Synthase in an Animal Genome." Molecular Biology and Evolution 30, no. 3 (November 29, 2012): 541–48. http://dx.doi.org/10.1093/molbev/mss269.

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27

Bainbridge, Zoë A., Robert I. Scott, and David Perry. "Oxygen utilisation by isopenicillin n synthase from penicillium chrysogenum." Journal of Chemical Technology & Biotechnology 55, no. 3 (April 24, 2007): 233–38. http://dx.doi.org/10.1002/jctb.280550306.

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28

Baldwin, Jack E., William J. Norris, Richard T. Freeman, Mark Bradley, Robert M. Adlington, Sadie Long-Fox, and Christopher J. Schofield. "γ-Lactam formation from tripeptides with isopenicillin N synthase." J. Chem. Soc., Chem. Commun., no. 16 (1988): 1128–30. http://dx.doi.org/10.1039/c39880001128.

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29

Chen, V. J., C. A. Frolik, S. Samson, P. D. Gesellchen, A. M. Orville, M. R. Harpel, J. D. Lipscomb, K. K. Surerus, and E. Münck. "Mössbauer and EPR studies of isopenicillin n synthase (IPNS)." Journal of Inorganic Biochemistry 36, no. 3-4 (August 1989): 258. http://dx.doi.org/10.1016/0162-0134(89)84329-6.

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30

Fujishima, Y., C. J. Schofield, J. E. Baldwin, J. M. Charnock, and C. D. Garner. "Recent physical and mechanistic studies on isopenicillin N synthase." Journal of Inorganic Biochemistry 43, no. 2-3 (August 1991): 564. http://dx.doi.org/10.1016/0162-0134(91)84539-l.

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31

GRUMMITT, Annaleise R., Peter J. RUTLEDGE, Ian J. CLIFTON, and Jack E. BALDWIN. "Active-site-mediated elimination of hydrogen fluoride from a fluorinated substrate analogue by isopenicillin N synthase." Biochemical Journal 382, no. 2 (August 24, 2004): 659–66. http://dx.doi.org/10.1042/bj20040529.

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Isopenicillin N synthase (IPNS) is a non-haem iron oxidase that catalyses the formation of bicyclic isopenicillin N from δ-(L-α-aminoadipoyl)-L-cysteinyl-D-valine (ACV). In this study we report a novel activity for the iron of the IPNS active site, which behaves as a Lewis acid to catalyse the elimination of HF from the fluorinated substrate analogue, δ-(L-α-aminoadipoyl)-L-cysteinyl-D-β-fluorovaline (ACβFV). X-Ray crystallographic studies of IPNS crystals grown anaerobically with ACβFV reveal that the valinyl β-fluorine is missing from the active site region, and suggest the presence of the unsaturated tripeptide δ-(L-α-aminoadipoyl)-L-cysteinyl-D-isodehydrovaline in place of substrate ACβFV. 19F NMR studies confirm the release of fluoride from ACβFV in the presence of the active IPNS enzyme. These results suggest a new mode of reactivity for the IPNS iron centre, a mechanism of action that has not previously been reported for any of the iron oxidase enzymes.
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32

LONG, Alexandra J., Ian J. CLIFTON, Peter L. ROACH, Jack E. BALDWIN, Christopher J. SCHOFIELD, and Peter J. RUTLEDGE. "Structural studies on the reaction of isopenicillin N synthase with the substrate analogue delta-(l-alpha-aminoadipoyl)-l-cysteinyl-d-alpha-aminobutyrate." Biochemical Journal 372, no. 3 (June 15, 2003): 687–93. http://dx.doi.org/10.1042/bj20021627.

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Isopenicillin N synthase (IPNS) is a non-haem iron(II) oxidase which catalyses the biosynthesis of isopenicillin N from the tripeptide δ-(l-α-aminoadipoyl)-l-cysteinyl-d-valine (ACV). Herein we report crystallographic studies to investigate the reaction of IPNS with the truncated substrate analogue δ-(l-α-aminoadipoyl)-l-cysteinyl-d-α-aminobutyrate (ACAb). It has been reported previously that this analogue gives rise to three β-lactam products when incubated with IPNS: two methyl penams and a cepham. Crystal structures of the IPNS–Fe(II)–ACAb and IPNS–Fe(II)–ACAb–NO complexes have now been solved and are reported herein. These structures and modelling studies based on them shed light on the diminished product selectivity shown by IPNS in its reaction with ACAb and further rationalize the presence of certain key residues at the IPNS active site.
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33

Weber, Stefan S., Fabiola Polli, Rémon Boer, Roel A. L. Bovenberg, and Arnold J. M. Driessen. "Increased Penicillin Production in Penicillium chrysogenum Production Strains via Balanced Overexpression of Isopenicillin N Acyltransferase." Applied and Environmental Microbiology 78, no. 19 (August 3, 2012): 7107–13. http://dx.doi.org/10.1128/aem.01529-12.

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ABSTRACTIntense classical strain improvement has yielded industrialPenicillium chrysogenumstrains that produce high titers of penicillin. These strains contain multiple copies of the penicillin biosynthesis cluster encoding the three key enzymes: δ-(l-α-aminoadipyl)-l-cysteinyl-d-valine synthetase (ACVS), isopenicillin N synthase (IPNS), and isopenicillin N acyltransferase (IAT). The phenylacetic acid coenzyme A (CoA) ligase (PCL) gene encoding the enzyme responsible for the activation of the side chain precursor phenylacetic acid is localized elsewhere in the genome in a single copy. Since the protein level of IAT already saturates at low cluster copy numbers, IAT might catalyze a limiting step in high-yielding strains. Here, we show that penicillin production in high-yielding strains can be further improved by the overexpression of IAT while at very high levels of IAT the precursor 6-aminopenicillic acid (6-APA) accumulates. Overproduction of PCL only marginally stimulates penicillin production. These data demonstrate that in high-yielding strains IAT is the limiting factor and that this limitation can be alleviated by a balanced overproduction of this enzyme.
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34

Fernández-Aguado, M., J. F. Martín, R. Rodríguez-Castro, C. García-Estrada, S. M. Albillos, F. Teijeira, and R. V. Ullán. "New insights into the isopenicillin N transport in Penicillium chrysogenum." Metabolic Engineering 22 (March 2014): 89–103. http://dx.doi.org/10.1016/j.ymben.2014.01.004.

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35

Brown-Marshall, Christina D., Adrienne R. Diebold, and Edward I. Solomon. "Reaction Coordinate of Isopenicillin N Synthase: Oxidase versus Oxygenase Activity." Biochemistry 49, no. 6 (February 16, 2010): 1176–82. http://dx.doi.org/10.1021/bi901772w.

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36

Baldwin, J. E., J. B. Coates, J. B. Halpern, M. G. Moloney, and A. J. Pratt. "Photoaffinity labelling of isopenicillin N synthetase by laser-flash photolysis." Biochemical Journal 261, no. 1 (July 1, 1989): 197–204. http://dx.doi.org/10.1042/bj2610197.

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Isopenicillin N synthetase (IPNS) from Acremonium chrysogenum was photolabelled by laser-flash photolysis in the presence of a diazirinyl-containing substrate, 2-[3-(3-trifluoromethyl-3H-diazirin-3-yl)-phenoxy]acetyl-S- methyloxycarbonylsulphenyl-L-cysteinyl-D-valine (DCV). Labelling of IPNS by DCV is partially inhibited in the presence of an excess of L-alpha-aminoadipoyl-L-cysteinyl-D-valine (ACV), the natural substrate. In the absence of light, DCV is converted into the corresponding penicillin with comparable Km but significantly depressed Vmax relative to ACV. Selective incorporation of [14C]DCV into IPNS has been demonstrated by fluorography of IPNS analysed by SDS/polyacrylamide-gel electrophoresis. Scintillation counting of labelled IPNS purified on an ion-exchange f.p.l.c. column confirms this result. This methodology may be applicable for studies aimed at investigating the binding of substrates to IPNS.
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37

BALDWIN, J. E., G. P. LYNCH, and C. J. SCHOFIELD. "ChemInform Abstract: Isopenicillin N Synthase: A New Mode of Reactivity." ChemInform 24, no. 6 (August 21, 2010): no. http://dx.doi.org/10.1002/chin.199306060.

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38

Ge, W., R. Adlington, P. Rutledge, and J. Baldwin. "Crystallographic studies on the reaction cycle of isopenicillin N synthase." Acta Crystallographica Section A Foundations of Crystallography 60, a1 (August 26, 2004): s138. http://dx.doi.org/10.1107/s0108767304097284.

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39

Baldwin, Jack E., Robert M. Adlington, Mark Bradley, William J. Norris, Nicholas J. Turner, and Akira Yoshida. "Identification and characterisation of shunt metabolites from isopenicillin N synthase." Journal of the Chemical Society, Chemical Communications, no. 16 (1988): 1125. http://dx.doi.org/10.1039/c39880001125.

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40

Buades, Celia, and Andrés Moya. "Phylogenetic analysis of the isopenicillin-N-synthetase horizontal gene transfer." Journal of Molecular Evolution 42, no. 5 (May 1996): 537–42. http://dx.doi.org/10.1007/bf02352283.

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41

Usui, Shigeyuki, and Chang-An Yu. "Purification and properties of isopenicillin N epimerase from Streptomyces clavuligerus." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 999, no. 1 (November 1989): 78–85. http://dx.doi.org/10.1016/0167-4838(89)90033-2.

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42

COHEN, G., D. SHIFFMAN, M. MEVARECH, and Y. AHARONOWITZ. "Microbial isopenicillin N synthase genes: Structure, function, diversity and evolution." Trends in Biotechnology 8 (1990): 105–11. http://dx.doi.org/10.1016/0167-7799(90)90148-q.

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43

Kurzătkowski, W., H. Palissa, H. Van Liempt, H. von Döhren, H. Kleinkauf, W. P. Wolf, and W. Kuryłowicz. "Localization of isopenicillin N synthase in Penicillium chrysogenum PQ-96." Applied Microbiology and Biotechnology 35, no. 4 (July 1991): 517–20. http://dx.doi.org/10.1007/bf00169760.

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44

Durairaj, Micheal, Brenda K. Leskiw, and Susan E. Jensen. "Genetic and biochemical analysis of the cysteinyl residues of isopenicillin N synthase from Streptomyces clavuligerus." Canadian Journal of Microbiology 42, no. 8 (August 1, 1996): 870–75. http://dx.doi.org/10.1139/m96-112.

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Isopenicillin N synthase (IPNS) from Streptomyces clavuligerus catalyses the oxidative cyclization of the acyclic tripeptide δ-(L-α-aminoadipyl)-L-cysteinyl-D-valine into isopenicillin N. All four of the cysteine residues found in this enzyme were mutated individually into serine residues, either by the polymerase chain reaction or by single-strand site-directed mutagenesis. Functional analysis of these single mutants showed that the C104S mutant lost more than 96% of its activity, while the remaining C37S, C142S, and C251S mutants each lost 30–50% of their activity. Treatment with the thiol-group-specific reagent N-ethylmaleimide confirmed the importance of the cysteine 104 residue. Activity analysis of an IPNS triple mutant (C37S, C142S, and C251S), prepared by recombining fragments of the IPNS-encoding pcbC gene from each of the three single mutants, showed that it had lost more than 90% of its activity. Conformational analysis by circular dichroism spectroscopy indicated that the IPNS triple mutant was structurally different from the wild type, suggesting that the loss of activity may be due to conformational changes rather than active site modifications.Key words: penicillin, Streptomyces, site-directed mutagenesis, polymerase chain reaction, thiol groups.
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45

Liberek, Bogdan, and Regina Kasprzykowska. "An efficient synthesis of δ-(L-α-aminoadipyl)-L-seryl-D-valine (LLD ASV), a naturally occuring tripeptide from the fermentation of Penicillium chrysogenum." Collection of Czechoslovak Chemical Communications 53, no. 11 (1988): 2854–56. http://dx.doi.org/10.1135/cccc19882854.

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The synthesis of δ-(L-α-aminoadipyl)-L-seryl-D-valine (LLD ASV), a naturally occuring congener of the well known tripeptide δ-(L-α-aminoadipyl)-L-cysteinyl-D-valine (LLD ACV) which is the linear precursor of isopenicillin N, penicillin N, cephalosporin C is described. An efficient method for producing the requisite α-monobenzyl ester of N-benzyloxycarbonyl-L-homoglutamic acid for subsequent condesation at the side chain δ-carboxy group is presented.
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46

Baldwin, J. E., J. M. Blackburn, and C. J. Schofield. "The Enzymatic Synthesis of 3-Aceto-Penams Using Isopenicillin N Synthase." Biocatalysis 3, no. 1-2 (January 1990): 129–36. http://dx.doi.org/10.3109/10242429008992055.

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47

Ming, Li June, Lawrence Que, Aidas Kriauciunas, Charles A. Frolik, and Victor J. Chen. "Coordination chemistry of the metal binding site of isopenicillin N synthase." Inorganic Chemistry 29, no. 6 (March 1990): 1111–12. http://dx.doi.org/10.1021/ic00331a001.

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48

Ogle, James M., Ian J. Clifton, Peter J. Rutledge, Jonathan M. Elkins, Nicolai I. Burzlaff, Robert M. Adlington, Peter L. Roach, and Jack E. Baldwin. "Alternative oxidation by isopenicillin N synthase observed by X-ray diffraction." Chemistry & Biology 8, no. 12 (December 2001): 1231–37. http://dx.doi.org/10.1016/s1074-5521(01)00090-4.

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49

CASTRO, J. M., P. LIRAS, L. LAIZ, J. CORTES, and J. F. MARTIN. "Purification and Characterization of the Isopenicillin N Synthase of Streptomyces lactamdurans." Microbiology 134, no. 1 (January 1, 1988): 133–41. http://dx.doi.org/10.1099/00221287-134-1-133.

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50

Laiz, L., P. Liras, J. M. Castro, and J. F. Martin. "Purification and characterization of the isopenicillin N epimerase from Nocardia lactamdurans." Journal of General Microbiology 136, no. 4 (April 1, 1990): 663–71. http://dx.doi.org/10.1099/00221287-136-4-663.

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