کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
70761 | 48845 | 2009 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Investigation of the carboligase activity of thiamine diphosphate-dependent enzymes using kinetic modeling and NMR spectroscopy
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
مهندسی شیمی
کاتالیزور
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Investigation of the carboligase activity of thiamine diphosphate-dependent enzymes using kinetic modeling and NMR spectroscopy Investigation of the carboligase activity of thiamine diphosphate-dependent enzymes using kinetic modeling and NMR spectroscopy](/preview/png/70761.png)
چکیده انگلیسی
The benzoin condensation reaction catalyzed by the thiamine diphosphate (ThDP)-dependent enzymes benzaldehyde lyase (BAL) and benzoylformate decarboxylase variant His281Ala (BFDH281A) was studied via initial rate measurements, progress curve analysis and NMR-based analysis of reaction intermediates. Using a mechanistic kinetic model, the kinetic parameters and microscopic rate constants were determined, thus identifying the rate limiting steps of the reaction. In BAL, overall reaction is rate-limited by product release, whereas in BFDH281A substrate binding is the slowest step of catalysis. These results were further confirmed by analysis of covalent reaction intermediates using NMR spectroscopy after acid quench isolation.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Molecular Catalysis B: Enzymatic - Volume 61, Issues 1–2, November 2009, Pages 73–79
Journal: Journal of Molecular Catalysis B: Enzymatic - Volume 61, Issues 1–2, November 2009, Pages 73–79
نویسندگان
Mariya Kokova, Michael Zavrel, Kai Tittmann, Antje C. Spiess, Martina Pohl,