Biosynthesis of terpenoids: 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase from tomato.

Content Provider	Semantic Scholar
Author	Rohdich, Felix Wungsintaweekul, Juraithip Luttgen, Holger Fischer, Markus K. R. Eisenreich, Wolfgang Schuhr, Christoph A. Fellermeier, Monika Schramek, Nicholas Zenk, Meinhart H. Bacher, Adelbert
Copyright Year	2000
Abstract	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 micromol small middle dotmg(-1) small middle dotmin(-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 Mg(2+), are required for activity. Neither the tomato enzyme nor the E. coli ortholog catalyzes the phosphorylation of isopentenyl monophosphate.
File Format	PDF HTM / HTML
DOI	10.1073/pnas.140209197
PubMed reference number	10880567
Journal	Medline
Volume Number	97
Issue Number	15
Alternate Webpage(s)	http://www.pnas.org/content/97/15/8251.full.pdf
Alternate Webpage(s)	https://doi.org/10.1073/pnas.140209197
Journal	Proceedings of the National Academy of Sciences of the United States of America
Language	English
Access Restriction	Open
Content Type	Text
Resource Type	Article