1aev
From Proteopedia
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==About this Structure== | ==About this Structure== | ||
| - | 1AEV is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]] with HEM and AMT as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ | + | 1AEV is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]] with HEM and AMT as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Cytochrome-c_peroxidase Cytochrome-c peroxidase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.5 1.11.1.5]]. Structure known Active Site: AVE. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AEV OCA]]. |
==Reference== | ==Reference== | ||
Introduction of novel substrate oxidation into cytochrome c peroxidase by cavity complementation: oxidation of 2-aminothiazole and covalent modification of the enzyme., Musah RA, Goodin DB, Biochemistry. 1997 Sep 30;36(39):11665-74. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9305956 9305956] | Introduction of novel substrate oxidation into cytochrome c peroxidase by cavity complementation: oxidation of 2-aminothiazole and covalent modification of the enzyme., Musah RA, Goodin DB, Biochemistry. 1997 Sep 30;36(39):11665-74. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9305956 9305956] | ||
| + | [[Category: Cytochrome-c peroxidase]] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transit peptide]] | [[Category: transit peptide]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:38:39 2007'' |
Revision as of 08:33, 30 October 2007
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INTRODUCTION OF NOVEL SUBSTRATE OXIDATION INTO CYTOCHROME C PEROXIDASE BY CAVITY COMPLEMENTATION: OXIDATION OF 2-AMINOTHIAZOLE AND COVALENT MODIFICATION OF THE ENZYME (2-AMINOTHIAZOLE)
Overview
The binding and oxidation of an artificial substrate, 2-aminothiazole, by, an engineered cavity of cytochrome c peroxidase is described. The W191G, mutant has been shown to create a buried cavity into which a number of, small heterocyclic compounds will bind [Fitzgerald, M. M., Churchill, M., J., McRee, D. E., & Goodin, D. B. (1994) Biochemistry 33, 3807-3818], providing a specific site near the heme from which substrates might be, oxidized. In this study, we show by titration calorimetry that, 2-aminothiazole binds to W191G with a Kd of 0.028 mM at pH 6. A crystal, structure at 2.3 A resolution of W191G in the presence of 2-aminothiazole, reveals the occupation of this compound in the cavity, and indicates that, it is in van der Waals contact with the heme. The WT enzyme reacts with, ... [(full description)]
About this Structure
1AEV is a [Single protein] structure of sequence from [Saccharomyces cerevisiae] with HEM and AMT as [ligands]. Active as [Cytochrome-c peroxidase], with EC number [1.11.1.5]. Structure known Active Site: AVE. Full crystallographic information is available from [OCA].
Reference
Introduction of novel substrate oxidation into cytochrome c peroxidase by cavity complementation: oxidation of 2-aminothiazole and covalent modification of the enzyme., Musah RA, Goodin DB, Biochemistry. 1997 Sep 30;36(39):11665-74. PMID:9305956
Page seeded by OCA on Tue Oct 30 10:38:39 2007
