5eat
From Proteopedia
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[[Category: natural products biosynthesis]] | [[Category: natural products biosynthesis]] | ||
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Revision as of 16:44, 5 November 2007
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5-EPI-ARISTOLOCHENE SYNTHASE FROM NICOTIANA TABACUM WITH SUBSTRATE ANALOG FARNESYL HYDROXYPHOSPHONATE
Overview
Terpene cyclases catalyze the synthesis of cyclic terpenes with 10-, 15-, and 20-carbon acyclic isoprenoid diphosphates as substrates. Plants have, been a source of these natural products by providing a homologous set of, terpene synthases. The crystal structures of 5-epi-aristolochene synthase, a sesquiterpene cyclase from tobacco, alone and complexed separately with, two farnesyl diphosphate analogs were analyzed. These structures reveal an, unexpected enzymatic mechanism for the synthesis of the bicyclic product, 5-epi-aristolochene, and provide a basis for understanding the, stereochemical selectivity displayed by other cyclases in the biosynthesis, of pharmacologically important cyclic terpenes. As such, these structures, provide templates for the engineering of novel terpene cyclases.
About this Structure
5EAT is a Single protein structure of sequence from Nicotiana tabacum with MG and FHP as ligands. Structure known Active Sites: AVE, MGA, MGB and MGC. Full crystallographic information is available from OCA.
Reference
Structural basis for cyclic terpene biosynthesis by tobacco 5-epi-aristolochene synthase., Starks CM, Back K, Chappell J, Noel JP, Science. 1997 Sep 19;277(5333):1815-20. PMID:9295271
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