Isopentenyl pyrophosphate isomerase:dimethylallyl pyrophosphate isomerase: Isolation from Claviceps sp. SD 58 and comparison to the mammalian enzyme

Bruenger, Eveline; Chayet, L.; Rilling, Hans C.

doi:10.1016/0003-9861(86)90516-3

Cited by 23 publications

(24 citation statements)

References 10 publications

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“…Slightly larger sizes were reported for the Claviceps enzyme (39 kDa; Bruenger et al, 1986) and the yeast isopentenyl-POP isomerases (39 -40 kDa; Reardon and Abeles, 1986;Anderson et al, 1989). In animal cells, the enzyme seems to be prone to proteolysis and modifications, which is probably the reason for the broad range (22-82 kDa) of the molecular masses reported (Bmenger et al, 1986;Banthorpe et al, 1977).…”

Section: Discussionmentioning

confidence: 93%

“…The combination of ion exchange, hydroxyapatite, and HIC used in our purification protocol, was based on the procedures described for the purification of isopentenyl-POP isomerases and prenyltransferases from other sources (Ogura et al, 1971 ;Bruenger et al, 1986;Hugueney and Camara, 1990). Separation of two isopentenyl-POP isomerase isoforms by hydroxyapatite chromatography was also observed for pumpkin (Ogura, et al, 1971) and C. unnuum protein extracts (Camara, B., Hugueney, P. and van der Heijden, R., unpublished results).…”

Section: Discussionmentioning

confidence: 93%

“…A further complicating factor during the purification procedure was the instability of the C. robustu isopentenyl-POP isomerase, especially at high salt concentrations necessary for HIC. It has previously been reported that isopentenyl-POP isomerases from plants and animals were less stable than the microbial enzyme (Bruenger et a]., 1986, Fujisaki et al, 1986. Glycerol and leupeptin showed a protective effect on the activity of the C. robustu enzyme and were used during the extraction procedure and during purification.…”

Section: Discussionmentioning

confidence: 99%

“…A regulatory role of this enzyme has been postulated to occur in the biosynthesis of sterols in yeast (Anderson et al, 1989) and mammalian liver cells (Bruenger et al, 1986), in prenylated protein metabolism in human promyelocytes (Xuan et al, 1994), and in the biosynthesis of carotenoids in fungi and plants (El-Jack et al, 1988;Albrecht and Sandmann, 1994). In plants, it is assumed that the isomerisation takes place within three subcellular compartments : in the plastids, in the cytosol, and in the mitochondria (Gray, 1987;Kleinig, 1989).…”

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confidence: 99%

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Purification and Characterization of two Isoforms of Isopentenyl‐Diphosphate Isomerase from Elicitor‐Treated Cinchona Robusta Cells

Ramos-Valdivlv¹,

Heijden²,

Verpoorte³

et al. 1997

European Journal of Biochemistry

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In Cinchona robusta (Rubiaceae) cell suspension cultures, the activity of the enzyme isopentenyldiphosphate isomerase (isopentenyl-POP isomerase) is transiently induced after addition of a homogenate of the phytopathogenic fungus Phytophthora cinnamomi. The enzyme catalyses the interconversion of isopentenyl-POP and dimethylallyl diphosphate (dimethylallyl-POP) and may be involved in the biosynthesis of anthrayuinone phytoalexins that accumulate rapidly after elicitation of Cinchona cells. From elicitor-treated C. robusta cells, two isoforms of isopentenyl-POP isomerase have been purified to apparent homogeneity in four chromatographic steps. The purified forms are monomeric enzymes of 34 kDa (isoform I) and 29 kDa (isoform 11), with K, values for isopentenyl-POP of 5.1 pM and 1.0 pM, respectively. Both isoforms require MnZ+ or Mg2+ as cofactor, isoform I1 showing a preference for Mn2+ with maximum activity at 1.5-2 mM. Isoform I was most active in the presence of 0.5-1.5 mM Mg" or in the presence of 0.5 mM MnZ+. A pH optimum of 7-7.8 was found for both forms and both were competitively inhibited by geranyl diphosphate (K, 96 pM for isoform I) and the transition state analogue 2-(dimethy1amino)ethyl diphosphate. Rechromatography of purified isoforms did not indicate any interconversion of both forms. Western blot analysis, using antibodies raised against isopentenyl-POP isomerase purified from Capsicum annuum, showed the presence of both isoforms in the crude protein extracts from C. robustu cells. Isoform I1 was specifically induced by elicitation, non-treated cells contained low activity of this isoform. The possible role of isopentenyl-POP isomerase in the biosynthesis of anthraquinones is discussed.

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Section: Discussionmentioning

confidence: 93%

Section: Discussionmentioning

confidence: 93%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

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Purification and Characterization of two Isoforms of Isopentenyl‐Diphosphate Isomerase from Elicitor‐Treated Cinchona Robusta Cells

Ramos-Valdivlv¹,

Heijden²,

Verpoorte³

et al. 1997

European Journal of Biochemistry

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“…Additionally, multiple isozymes of IDI have been identified in higher eukaryotes Sus domesticus and Gallus gallus. In all cases the isozymes maintain specialized functions by different expression patterns, subcellular localization, and susceptibility to inhibitors (8,9).…”

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confidence: 99%

IDI2, a Second Isopentenyl Diphosphate Isomerase in Mammals

Clizbe

Owens

Masuda

et al. 2007

Journal of Biological Chemistry

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We recently described the identification of a novel isopentenyl diphosphate isomerase, IDI2 in humans and mice. Our current data indicate that, in humans, IDI2 is expressed only in skeletal muscle. Isoprenoids and isoprenoid-derived compounds play an essential role in all living systems. They provide a necessary function in the organization of many biological systems including membrane structure, signal transduction, and redox chemistry. Several of the important end products of the isoprenoid biosynthetic pathway include: prenylated proteins, dolichols, vitamins A, D, E, and K, steroid hormones, carotenoids, bile acids, and cholesterol (1). In addition, this complex pathway also produces farnesyl diphosphate (FPP) 2 and geranyl-geranyl diphosphate (GGPP), compounds required for the isoprenylation of various G proteins (2).All isoprenoids are derived from the 5-carbon isoprene defined by isopentenyl diphosphate (IPP) and its highly electrophilic isomer dimethylallyl diphosphate (DMAPP). The enzyme isopentenyl diphosphate isomerase (IDI1; EC 5.3.3.2) transforms unreactive IPP into its reactive isomer DMAPP by the concerted addition and abstraction of protons at C-4. These two isomers are the building blocks for the successive head-to-tail condensation reactions that result in the synthesis of geranyl diphosphate (GPP, C 10 ) FPP (C 15 ) and ultimately, non-sterol products and cholesterol (3).IDI1 first identified in Saccharomyces cerevisiae (4) has since been characterized in numerous organisms including humans. Most recently, IDI1 has been identified in hamster and rat where it was shown to localize to the peroxisome by a Pex-5p-dependent PTS1 mechanism (5).Analysis of IDI1 in S. cerevisiae revealed two catalytically active amino acids, Cys 139 and Glu 207 . Mutagenesis analysis in the yeast enzyme demonstrated that a C139S mutation resulted in a significant reduction in isomerase activity whereas a Cys to Val or Ala change at this site abolished activity completely (6).Several examples of multiple IDI isozymes have been reported in plants and algae. In Nicotiana tobacum, the two IDI isozymes are regulated at the transcriptional level under a variety of environmental conditions (7). Similar duplications exist in Cinchona robusta and the green alga Hematococcus pluvialis. Additionally, multiple isozymes of IDI have been identified in higher eukaryotes Sus domesticus and Gallus gallus. In all cases the isozymes maintain specialized functions by different expression patterns, subcellular localization, and susceptibility to inhibitors (8, 9).We previously reported a detailed phylogenetic and structural analysis of IDI2 (10). Molecular modeling suggested that IDI2 is likely to perform functionally as an isomerase despite a Ser to Cys change within the putative active site. In the current study we present the biochemical and functional characterization of IDI2 in mammals. Our data illustrate that IDI2 has a distinct tissue expression pattern, has functional isomerase activity in vivo, a unique kinetic profile, and is...

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Involvement of Farnesyl Protein Transferase (FPTase) in FcεRI-Induced Activation of RBL-2H3 Mast Cells

Chen

Mehan

Gupta

et al. 1999

Archives of Biochemistry and Biophysics

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Isopentenyl pyrophosphate isomerase:dimethylallyl pyrophosphate isomerase: Isolation from Claviceps sp. SD 58 and comparison to the mammalian enzyme

Cited by 23 publications

References 10 publications

Purification and Characterization of two Isoforms of Isopentenyl‐Diphosphate Isomerase from Elicitor‐Treated Cinchona Robusta Cells

Purification and Characterization of two Isoforms of Isopentenyl‐Diphosphate Isomerase from Elicitor‐Treated Cinchona Robusta Cells

IDI2, a Second Isopentenyl Diphosphate Isomerase in Mammals

Involvement of Farnesyl Protein Transferase (FPTase) in FcεRI-Induced Activation of RBL-2H3 Mast Cells

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