title: Study of IspH, a key enzyme in the methylerythritol phosphate pathway using fluoro-substituted substrate analogues.
abstract: IspH, a [4Fe-4S]-cluster-containing enzyme, catalyzes the reductive dehydroxylation of 4-hydroxy-3-methyl-butenyl diphosphate (HMBPP) to isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP) in the methylerythritol phosphate pathway. Studies of IspH using fluoro-substituted substrate analogues to dissect the contributions of several factors to IspH catalysis, including the coordination of the HMBPP C(4)-OH group to the iron-sulfur cluster, the H-bonding network in the active site, and the electronic properties of the substrates, are reported.
authors: Department of Chemistry, Boston University, Boston, Massachusetts 02215, USA.
authors: Youli
authors: Y
authors: Xiao
authors: Wei-chen
authors: WC
authors: Chang
authors: Hung-wen
authors: HW
authors: Liu
authors: Pinghua
authors: P
authors: Liu
mesh_terms: D019883:Alkyl and Aryl Transferases / Q000378:metabolism*; D055162:Biocatalysis; D004896:Erythritol / Q000737:chemistry* / Q000378:metabolism; D017611:Fluorine Compounds / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D015394:Molecular Structure; D010084:Oxidation-Reduction; D013379:Substrate Specificity; D013403:Sugar Phosphates / Q000737:chemistry* / Q000378:metabolism
chemical_list: D017611:Fluorine Compounds; D013403:Sugar Phosphates; D019883:Alkyl and Aryl Transferases; D004896:Erythritol