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IspH Protein of the Deoxyxylulose Phosphate Pathway: Mechanistic Studies with C 1 ‐Deuterium‐Labeled Substrate and Fluorinated Analogue
Author(s) -
Xiao Youli,
Liu Pinghua
Publication year - 2008
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.200803452
Subject(s) - nicotinamide adenine dinucleotide phosphate , flavodoxin , chemistry , substrate (aquarium) , enzyme , reductase , biochemistry , biosynthesis , nicotinamide adenine dinucleotide , cofactor , phosphate , deuterium , stereochemistry , nad+ kinase , biology , ferredoxin , ecology , oxidase test , physics , quantum mechanics
The last step of the deoxylxylulose phosphate pathway is catalyzed by IspH to synthesize two precursors for isoprenoid biosynthesis. The lack of a primary kinetic isotope effect at C 1 and enzymatic evaluation with a fluorinated analogue (see scheme) suggest that the C 1 ‐position is not involved in the IspH‐catalyzed reaction. FldA=flavodoxin, Fpr=flavodoxin reductase, NADPH=nicotinamide adenine dinucleotide phosphate, PPi=P 2 O 6 3− .