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1uzw
From Proteopedia
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| - | [[Image:1uzw.gif|left|200px]]<br /> | + | [[Image:1uzw.gif|left|200px]]<br /><applet load="1uzw" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1uzw" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1uzw, resolution 1.30Å" /> | caption="1uzw, resolution 1.30Å" /> | ||
'''ISOPENICILLIN N SYNTHASE WITH L-D-(A-AMINOADIPOYL)-L-CYSTEINYL-D-ISODEHYDROVALINE'''<br /> | '''ISOPENICILLIN N SYNTHASE WITH L-D-(A-AMINOADIPOYL)-L-CYSTEINYL-D-ISODEHYDROVALINE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1UZW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Emericella_nidulans Emericella nidulans] with FE2, SO4 and CDH as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Isopenicillin-N_synthase Isopenicillin-N synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.21.3.1 1.21.3.1] | + | 1UZW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Emericella_nidulans Emericella nidulans] with FE2, SO4 and CDH as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Isopenicillin-N_synthase Isopenicillin-N synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.21.3.1 1.21.3.1] Known structural/functional Site: <scene name='pdbsite=AC1:So4 Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UZW OCA]. |
==Reference== | ==Reference== | ||
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[[Category: penicillin biosynthesis]] | [[Category: penicillin biosynthesis]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 18:19:53 2007'' |
Revision as of 16:10, 18 December 2007
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ISOPENICILLIN N SYNTHASE WITH L-D-(A-AMINOADIPOYL)-L-CYSTEINYL-D-ISODEHYDROVALINE
Overview
Isopenicillin N synthase (IPNS) is a non-haem iron oxidase that catalyses, the formation of bicyclic isopenicillin N from, delta-(L-alpha-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, delta-(L-alpha-aminoadipoyl)-L-cysteinyl-D-beta-fluorovaline (ACbetaFV)., X-Ray crystallographic studies of IPNS crystals grown anaerobically with, ACbetaFV reveal that the valinyl beta-fluorine is missing from the active, site region, and suggest the presence of the unsaturated tripeptide, delta-(L-alpha-aminoadipoyl)-L-cysteinyl-D-isodehydrovaline in place of, substrate ACbetaFV. (19)F NMR studies confirm the release of fluoride from, ACbetaFV 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.
About this Structure
1UZW is a Single protein structure of sequence from Emericella nidulans with FE2, SO4 and CDH as ligands. Active as Isopenicillin-N synthase, with EC number 1.21.3.1 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Active-site-mediated elimination of hydrogen fluoride from a fluorinated substrate analogue by isopenicillin N synthase., Grummitt AR, Rutledge PJ, Clifton IJ, Baldwin JE, Biochem J. 2004 Sep 1;382(Pt 2):659-66. PMID:15175003
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