High impact information on IDI1

• Expression of IPP isomerase, and of two enzymes specific to the carotenoid pathway (lycopene beta-cyclase and beta-carotene-C-4-oxygenase), was followed in the green unicellular alga Haematococcus pluvialis after exposure to high illumination [1].
• This review covers the biosynthesis of the starter units of terpenoids, isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP) via the nonmevalonate pathway together with a new enzyme involved in the conversion of IPP and DMAPP, i.e type 2 IPP isomerase [2].
• Nucleotide sequence of a Clarkia breweri cDNA clone of Ipi1, a gene encoding isopentenyl pyrophosphate isomerase [3].
• We have investigated the docking of a variety of inhibitors and substrates to the isoprene biosynthesis pathway enzymes farnesyl diphosphate synthase (FPPS), isopentenyl diphosphate/dimethylallyl diphosphate isomerase (IPPI) and deoxyxylulose-5-phosphate reductoisomerase (DXR) using the Lamarckian genetic alogorithm program, AutoDock [4].
• These genes encode gelsolin, isopentenyl-diphosphate delta isomerase (IDI1), and 1,25-dihydroxyvitamin D-3 up-regulated protein 1 (VDUP1), the last two of which were identified by DD [5].

Anatomical context of IDI1

• A human promyelocyte mRNA transiently induced by TPA is homologous to yeast IPP isomerase [6].
• In both cell lines, the statins (atorvastatin, cerivastatin and pitavastatin) induced the expression of four genes, which relate to cholesterol metabolism, namely, HMG-CoA synthase 1, HMG-CoA reductase, farnesyl diphosphate synthase and isopentenyl-diphosphate delta isomerase [7].
• Isopentenyl pyrophosphate isomerase and prenyltransferase from tomato fruit plastids [8].

Associations of IDI1 with chemical compounds

• Among these enzymes, MK, IPPI and FPPS activities in the YM-16638-treated group significantly decreased by 38%, 56% and 30%, respectively, when compared to those from control animals receiving no drug treatment [9].
• Isopentenyl pyrophosphate isomerase could also be totally inactivated by 1 X 10(-3) M iodoacetamide, and this property was utilized in the assay of prenyltransferase activity in the presence of contaminating isomerase [8].
• The inactivation of isomerase by iodoacetamide is consistent with the stabilization of isopentenyl pyrophosphate isomerase by dithiothreitol [8].
• Isopentenyl pyrophosphate isomerase has been isolated from an extract of tomato fruit plastids and purified 245-fold by fractionation with ammonium sulfate, gel filtration on Bio-Gel A 1.5m, ion-exchange chromatography on DEAE-cellulose, gel filtration on Sephadex G-100, and chromatofocusing [8].
• Isopentenyl pyrophosphate isomerase, two prenyltransferases, and a number of terpene cyclases (synthases) were readily adsorbed to Matrex Gel Red A (a dimeric triazine dye coupled to cross-linked agarose beads), and desorbed in good yield with relatively high concentrations of KCl and increasing pH [10].

Analytical, diagnostic and therapeutic context of IDI1

• Gel filtration on Sephadex G-100 separated the isopentenyl pyrophosphate isomerase from a prenyltransferase fraction that catalyzed the conversion of isopentenyl pyrophosphate to acid-labile compounds in the presence of dimethylallyl, geranyl, or farnesyl pyrophosphates [8].

References