Abstract:
:Terpenoid cyclases catalyze remarkably complex cyclization cascades that are initiated by the formation of a highly reactive carbocation in a polyisoprene substrate. Recent crystal structures of terpenoid cyclases show how these enzymes provide a template for binding and stabilizing the flexible substrate in the precise orientation required for catalysis, trigger carbocation formation, chaperone the conformations of the reactive carbocation intermediates through a unique cyclization sequence, and sequester and stabilize carbocations from premature quenching. Notably, terpenoid cyclases and catalytic antibodies have converged to similar chemical and structural strategies for managing highly reactive carbocations in polyisoprene cyclization cascades.
journal_name
Curr Opin Struct Bioljournal_title
Current opinion in structural biologyauthors
Lesburg CA,Caruthers JM,Paschall CM,Christianson DWdoi
10.1016/s0959-440x(98)80088-2subject
Has Abstractpub_date
1998-12-01 00:00:00pages
695-703issue
6eissn
0959-440Xissn
1879-033Xpii
S0959-440X(98)80088-2journal_volume
8pub_type
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journal_title:Current opinion in structural biology
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abstract::A selection of World Wide Web sites relevant to papers published in this issue of Current Opinion in Structural Biology. ...
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