Prenyltransferase from Gossypium hirsutum

Widmaier, Robert; Howe, Jean M.; Heinstein, Peter

doi:10.1016/0003-9861(80)90394-x

Cited by 23 publications

(10 citation statements)

References 23 publications

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“…A similar high affinity for isopentenyl-POP was also reported for the isopentenyl-POP isomerase isoforms from avian liver (Sagami and Ogura, 1983). High K , values in the range of 22-74 pM have been reported for partially purified isopentenyl-POP isomerase from cotton (Widmaier et al, 1980), pumpkin fruit (Ogura et al, 1968(Ogura et al, , 1971, rubber latex (Koyama et al, 1996), and the purified yeast enzyme (Reardon and Abeles, 1986).…”

Section: Discussionmentioning

confidence: 48%

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: 48%

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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“…Widmaier et al 86 purified a protein fraction from Gossypium hirsutum roots. This fraction was able to produce the four different isomers of FPP with IPP as single substrate.…”

Section: Biosynthetic Pathways Leading To the Formation Of C 5 -Unitsmentioning

confidence: 99%

Isopentenyl diphosphate isomerase: a core enzyme in isoprenoid biosynthesis. A review of its biochemistry and function

Ramos-Valdivia¹,

Heijden²,

Verpoorte³

1997

Nat. Prod. Rep.

143

124

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“…FPP, GGPP, and PPP, either labeled or unlabeled, were synthesized from the corresponding alcohol as described in Ref. 26. Chlide a was prepared from Chl a with chlorophyllase as described in Ref.…”

Section: Methodsmentioning

confidence: 99%

Hydrogenation of Geranylgeraniol

Soll¹,

Schultz²,

Rüdiger³

et al. 1983

Plant Physiol.

116

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The reduction of geranylgeranylpyrophosphate to phytylpyrophosphate in spinach chloroplasts is described for the first time. The reductase is localized in the chloroplast envelope. By Refs. 8,23,22,5,and 24, respectively). GG is known to occur as the side chain in bacteriochlorophyll of purple bacteria (7), and it was later found in trace amounts esterified to Chl a in greening etiolated tissue (12,25). Rudiger et al. (17) showed that an enzyme different from chlorophyllase, i.e., Chl synthetase, was responsible for the esterification of Chlide in etiolated tissue. Subsequently, this enzyme was demonstrated in spinach chloroplasts (6,20) and Chl-free chromoplasts from daffodil (1 1). Further examination of the last steps ofChl biosynthesis in greening etiolated oat seedlings showed a stepwise reduction of the initial product, ChiGG, via Chl dihydrogeranylgeraniol and Chl tetrahydrogeranylgeraniol to Chiph (2,18). In a preliminary report (20), we showed that this sequence also exists in the natural green system. Very little is known about the regulation of this important final step in Chl synthesis in chloroplasts.In studies of tocopherol and phylloquinone synthesis, we found that GGPP could not substitute for PPP in the enzymic prenylation of the aromatic precursor of either vitamin (19,21). This is in contrast to Chl synthetase which uses GGPP and PPP and to a ' This work was aided by grants from the Deutsche Forschungsgemeinschaft.2Abbreviations: Ph, phytol; GG, geranylgeraniol; IPP, isopentenylpyrophosphate; ChlGG.DHGG,THGG,Ph, Chi esterified with GG, dihydro-GG, tetrahydro-GG, and Ph; GGPP and PPP, GG-and Ph-pyrophosphate; Phae, phaeophytin; FPP, farnesol-PP; Chl aF, Chl afarnesoi.lesser extent even FPP in the etioplast system (17). In a recent short communication (20), we showed for the first time that GGPP was directly incorporated into Ph. No data were available for the localization and regulation of this reductase activity. The data presented below further characterize the reduction of GGPP and show that two distinct sites and two distinct pathways exist for the conversion of the geranylgeranyl moiety to the phytyl moiety in spinach chloroplasts: the chloroplast envelope for the hydrogenation of GGPP to PPP, and the thylakoids for the esterification of chlide with GGPP and stepwise reduction of Chlc0 to ChlPh. MATERIALS AND METHODSReagents. The reagents were from commercial sources and were of the highest purity available.

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Prenyltransferase from Gossypium hirsutum

Cited by 23 publications

References 23 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

Isopentenyl diphosphate isomerase: a core enzyme in isoprenoid biosynthesis. A review of its biochemistry and function

Hydrogenation of Geranylgeraniol

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