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Mechanistic Studies of an IspH‐Catalyzed Reaction: Implications for Substrate Binding and Protonation in the Biosynthesis of Isoprenoids
Author(s) -
Chang Weichen,
Xiao Youli,
Liu Hungwen,
Liu Pinghua
Publication year - 2011
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201104124
Subject(s) - protonation , substrate (aquarium) , chemistry , catalysis , biosynthesis , stereochemistry , enzyme , terpenoid , double bond , biochemistry , biology , organic chemistry , ecology , ion
Chosen handle : Mechanistic studies of the IspH‐catalyzed reductive dehydroxylation of 4‐hydroxy‐3‐methyl‐2‐( E )‐1‐diphosphate (HMBPP) to isopentenyl diphosphate and dimethylallyl diphosphate suggest that both the 4‐OH group and the double bond of HMBPP may contribute to the formation of substrate–IspH complex. Labeling studies now show that the 4‐hydroxy group of the substrate plays the dominant role in positioning the substrate in the enzyme active site.