IspH Protein of the Deoxyxylulose Phosphate Pathway: Mechanistic Studies with C 1 ‐Deuterium‐Labeled Substrate and Fluorinated Analogue | Zendy

Xiao Youli | Zendy; Liu Pinghua | Zendy

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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− .

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