1357580-68-7Relevant academic research and scientific papers
Mechanistic studies of an isph-catalyzed reaction: Implications for substrate binding and protonation in the biosynthesis of isoprenoids
Chang, Wei-Chen,Xiao, Youli,Liu, Hung-Wen,Liu, Pinghua
, p. 12304 - 12307 (2012/02/02)
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.
