期刊
CURRENT OPINION IN CHEMICAL BIOLOGY
卷 16, 期 1-2, 页码 124-131出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.cbpa.2011.12.017
关键词
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资金
- National Institutes of Health [GM035906, GM040541, F32AI082906]
- Texas Higher Education Coordination Board [ARP-003658-0093-2007]
- Welch Foundation [F-1511]
Only a very few examples of enzymes known to catalyze pericyclic reactions have been reported, and presently no enzyme has been demonstrated unequivocally to catalyze a Die Is-Alder reaction. Nevertheless, research into secondary metabolism has led to the discovery of numerous natural products exhibiting the structural hallmarks of [4 + 2] cycloadditions, prompting efforts to characterize the responsible enzymatic processes. These efforts have resulted in a growing collection of enzymes believed to catalyze pericyclic [4 + 2] cycloaddition reactions; however, in each case the complexity of the substrates and catalytic properties of these enzymes poses significant challenges in substantiating these hypotheses. Herein we consider the principles motivating these efforts and the enzymological systems currently under investigation.
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