期刊名称:Proceedings of the National Academy of Sciences
印刷版ISSN:0027-8424
电子版ISSN:1091-6490
出版年度:2000
卷号:97
期号:15
页码:8251-8256
DOI:10.1073/pnas.140209197
语种:English
出版社:The National Academy of Sciences of the United States of America
摘要:The putative catalytic domain (residues 81-401) of a predicted tomato protein with similarity to 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase of Escherichia coli was expressed in a recombinant E. coli strain. The protein was purified to homogeneity and was shown to catalyze the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2-C-methyl-D-erythritol at a rate of 33 {micro}mol*mg-1*min-1. The structure of the reaction product, 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate, was established by NMR spectroscopy. Divalent metal ions, preferably Mg2+, are required for activity. Neither the tomato enzyme nor the E. coli ortholog catalyzes the phosphorylation of isopentenyl monophosphate.