期刊
FEBS JOURNAL
卷 276, 期 9, 页码 2432-2446出版社
WILEY
DOI: 10.1111/j.1742-4658.2009.06964.x
关键词
1'; 4'-iminopyrimidine tautomeric form of thiamin; benzaldehyde lyase; benzoylformate decarboxylase; CD; enamine intermediate; pyruvate decarboxylase; pyruvate dehydrogenase; thiamin diphosphate
资金
- National Institutes of Health [GM050380]
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM050380] Funding Source: NIH RePORTER
We summarize the currently available information regarding the state of ionization and tautomerization of the 4'-aminopyrimidine ring of the thiamine diphosphate on enzymes requiring this coenzyme. This coenzyme forms a series of covalent intermediates with its substrates as an electrophilic catalyst, and the coenzyme itself also carries out intramolecular proton transfers, which is virtually unprecedented in coenzyme chemistry. An understanding of the state of ionization and tautomerization of the 4'-aminopyrimidine ring in each of these intermediates provides important details about proton movements during catalysis. CD spectroscopy, both steady-state and time-resolved, has proved crucial for obtaining this information because no other experimental method has provided such atomic detail so far.
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