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Isoprenoid biosynthesis in plants - 2C-methyl-d-erythritol-4-phosphate synthase (IspC protein) of Arabidopsis thaliana.

The ispC gene of Arabidopsis thaliana was expressed in pseudomature form without the putative plastid-targeting sequence in a recombinant Escherichia coli strain. The recombinant protein was purified by affinity chromatography and was shown to catalyze the formation of 2C-methyl-d-erythritol 4-phosphate from 1-deoxy-d-xylulose 5-phosphate at a rate of 5.6 micromol.min(-1).mg(-1) (k(cat) 4.4 s(-1)). The Michaelis constants for 1-deoxy-d-xylulose 5-phosphate and the cosubstrate NADPH are 132 and 30 microm, respectively. The enzyme has an absolute requirement for divalent metal ions, preferably Mn(2+) and Mg(2+), and is inhibited by fosmidomycin with a K(i) of 85 nm. The pH optimum is 8. 0. NADH can substitute for NADPH, albeit at a low rate (14% as compared to NADPH). The enzyme catalyzes the reverse reaction at a rate of 2.1 micromol.min(-1).mg(-1).[1]

References

  1. Isoprenoid biosynthesis in plants - 2C-methyl-d-erythritol-4-phosphate synthase (IspC protein) of Arabidopsis thaliana. Rohdich, F., Lauw, S., Kaiser, J., Feicht, R., Köhler, P., Bacher, A., Eisenreich, W. FEBS J. (2006) [Pubmed]
 
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