TY - JOUR
T1 - Current developments and challenges in the search for a naturally selected Diels-Alderase
AU - Kim, Hak Joong
AU - Ruszczycky, Mark W.
AU - Liu, Hung wen
N1 - Funding Information:
This work is supported partly by grants from the National Institutes of Health ( GM035906 , GM040541 , F32AI082906 ), the Texas Higher Education Coordination Board ( ARP-003658-0093-2007 ), and the Welch Foundation ( F-1511 ).
PY - 2012/4
Y1 - 2012/4
N2 - 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 Diels-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.
AB - 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 Diels-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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U2 - 10.1016/j.cbpa.2011.12.017
DO - 10.1016/j.cbpa.2011.12.017
M3 - Review article
C2 - 22260931
AN - SCOPUS:84862786646
VL - 16
SP - 124
EP - 131
JO - Current Opinion in Chemical Biology
JF - Current Opinion in Chemical Biology
SN - 1367-5931
IS - 1-2
ER -