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Gene Review:

ECs3761 - isopentenyl-diphosphate delta-isomerase

Escherichia coli O157:H7 str. Sakai

Ershov, Y. et al., Hoeffler, J.F. et al., Yoon, S.H. et al., de Ruyck, J. et al., Nishida, Y. et al., et al.

de Ruyck, Durisotti, Oudjama, Wouters,

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Disease relevance of ECs3761

The crystal structures of free and metal-bound Escherichia coli IPP isomerase reveal critical active site features underlying its catalytic mechanism [1].
It is shown that Synechocystis PCC6803 is deficient in IPP isomerase activity, consistent with the absence in its genome of an obvious homologue for the enzyme [2].
Open reading frame 176 in the photosynthesis gene cluster of Rhodobacter capsulatus encodes idi, a gene for isopentenyl diphosphate isomerase [3].

High impact information on ECs3761

The Escherichia coli plasmid expressing orfD could complement the disrupted IPP isomerase gene in E. coli [4].
This labelling pattern represents direct evidence for the presence of the DMAPP branch of the MEP pathway in a higher plant, and shows that IPP can be synthesized from DMAPP in plant plastids, most probably via a plastidial IPP isomerase [5].
A sequence analysis revealed this cluster to contain 12 open reading frames (ORFs), including the 7 known genes, crtW, crtY, crtI, crtB, crtE, idi, and crtZ [6].
The mevalonate lower pathway, composed of mvaK1, mvaK2, mvaD, and idi, was engineered to produce pSSN12Didi for an efficient supply of the lycopene building blocks, isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP) [7].
The addition of Triton X-100 enhanced OPP synthetase, but it did not affect IPP isomerase and FPP synthetase [8].

Associations of ECs3761 with chemical compounds

Isopentenyl diphosphate isomerase (IPP isomerase) in many organisms and in plastids is central to isoprenoid synthesis and involves the conversion between IPP and dimethylallyl diphosphate (DMAPP) [2].

Analytical, diagnostic and therapeutic context of ECs3761

Multiple sequence alignments and geometrical features observed in crystal structures of complexes with IPP isomerase suggest that Tyr-104 could play an important role during catalysis [9].

References

Crystal structure of isopentenyl diphosphate:dimethylallyl diphosphate isomerase. Durbecq, V., Sainz, G., Oudjama, Y., Clantin, B., Bompard-Gilles, C., Tricot, C., Caillet, J., Stalon, V., Droogmans, L., Villeret, V. EMBO J. (2001) [Pubmed]
Isopentenyl diphosphate isomerase deficiency in Synechocystis sp. strain PCC6803. Ershov, Y., Gantt, R.R., Cunningham, F.X., Gantt, E. FEBS Lett. (2000) [Pubmed]
Open reading frame 176 in the photosynthesis gene cluster of Rhodobacter capsulatus encodes idi, a gene for isopentenyl diphosphate isomerase. Hahn, F.M., Baker, J.A., Poulter, C.D. J. Bacteriol. (1996) [Pubmed]
An unusual isopentenyl diphosphate isomerase found in the mevalonate pathway gene cluster from Streptomyces sp. strain CL190. Kaneda, K., Kuzuyama, T., Takagi, M., Hayakawa, Y., Seto, H. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
Isoprenoid biosynthesis in higher plants and in Escherichia coli: on the branching in the methylerythritol phosphate pathway and the independent biosynthesis of isopentenyl diphosphate and dimethylallyl diphosphate. Hoeffler, J.F., Hemmerlin, A., Grosdemange-Billiard, C., Bach, T.J., Rohmer, M. Biochem. J. (2002) [Pubmed]
Elucidation of a carotenoid biosynthesis gene cluster encoding a novel enzyme, 2,2'-beta-hydroxylase, from Brevundimonas sp. strain SD212 and combinatorial biosynthesis of new or rare xanthophylls. Nishida, Y., Adachi, K., Kasai, H., Shizuri, Y., Shindo, K., Sawabe, A., Komemushi, S., Miki, W., Misawa, N. Appl. Environ. Microbiol. (2005) [Pubmed]
Enhanced lycopene production in Escherichia coli engineered to synthesize isopentenyl diphosphate and dimethylallyl diphosphate from mevalonate. Yoon, S.H., Lee, Y.M., Kim, J.E., Lee, S.H., Lee, J.H., Kim, J.Y., Jung, K.H., Shin, Y.C., Keasling, J.D., Kim, S.W. Biotechnol. Bioeng. (2006) [Pubmed]
Isoprenoid synthesis in Escherichia coli. Separation and partial purification of four enzymes involved in the synthesis. Fujisaki, S., Nishino, T., Katsuki, H. J. Biochem. (1986) [Pubmed]
Structural role for Tyr-104 in Escherichia coli isopentenyl-diphosphate isomerase: site-directed mutagenesis, enzymology, and protein crystallography. de Ruyck, J., Durisotti, V., Oudjama, Y., Wouters, J. J. Biol. Chem. (2006) [Pubmed]

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