1aev
INTRODUCTION OF NOVEL SUBSTRATE OXIDATION INTO CYTOCHROME C PEROXIDASE BY CAVITY COMPLEMENTATION: OXIDATION OF 2-AMINOTHIAZOLE AND COVALENT MODIFICATION OF THE ENZYME (2-AMINOTHIAZOLE)
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OverviewOverview
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 StructureAbout 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].
ReferenceReference
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
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