Mevalonate-independent methylerythritol phosphate pathway for isoprenoid biosynthesis. Elucidation and distribution

Rohmer, Michel

doi:10.1351/pac200375020375

Cited by 144 publications

(109 citation statements)

References 72 publications

Supporting

Mentioning

103

Contrasting

Unclassified

Order By: Relevance

“…In plants, both IDP and DMADP are synthesized via two parallel pathways, the mevalonate (MVA) pathway, which is active in the cytosol, and the methylerythritol 4-phosphate (MEP) pathway, which is active in the plastids (Lichtenthaler, 1999;Rodriguez-Concepció n and Boronat, 2002;Rohdich et al, 2002;Rohmer, 2003). It is generally recognized that the cytosolic pathway is responsible for the synthesis of sesquiterpenes, phytosterols and ubiquinone, whereas monoterpenes, gibberellins, abscisic acid, carotenoids and the prenyl moiety of chlorophylls, plastoquinone and tocopherol are produced in plastids (Lichtenthaler, 1999;Rodriguez-Concepció n and Boronat, 2002;Rohdich et al, 2002;Rohmer, 2003), but indications of cross-talk between the plastidic and cytosolic pathways have been found in tobacco, Arabidopsis and snapdragon petals Dudareva et al, 2005;Ohara et al, 2003). The direct precursors of terpenoids, linear geranyl diphosphate (GDP, C 10 ), farnesyl diphosphate (FDP, C 15 ) and geranylgeranyl diphosphate (GGDP,C 20 ), are produced by the activities of Biosynthesis of plant-derived flavor compounds 717 three prenyl transferases.…”

Section: Carbohydrate-derived Flavor Compoundsmentioning

confidence: 99%

Biosynthesis of plant‐derived flavor compounds

Schwab¹,

Davidovich‐Rikanati²,

Lewinsohn³

2008

The Plant Journal

968

704

View full text Add to dashboard Cite

SummaryPlants have the capacity to synthesize, accumulate and emit volatiles that may act as aroma and flavor molecules due to interactions with human receptors. These low-molecular-weight substances derived from the fatty acid, amino acid and carbohydrate pools constitute a heterogenous group of molecules with saturated and unsaturated, straight-chain, branched-chain and cyclic structures bearing various functional groups (e.g. alcohols, aldehydes, ketones, esters and ethers) and also nitrogen and sulfur. They are commercially important for the food, pharmaceutical, agricultural and chemical industries as flavorants, drugs, pesticides and industrial feedstocks. Due to the low abundance of the volatiles in their plant sources, many of the natural products had been replaced by their synthetic analogues by the end of the last century. However, the foreseeable shortage of the crude oil that is the source for many of the artifical flavors and fragrances has prompted recent interest in understanding the formation of these compounds and engineering their biosynthesis. Although many of the volatile constituents of flavors and aromas have been identified, many of the enzymes and genes involved in their biosynthesis are still not known. However, modification of flavor by genetic engineering is dependent on the knowledge and availability of genes that encode enzymes of key reactions that influence or divert the biosynthetic pathways of plant-derived volatiles. Major progress has resulted from the use of molecular and biochemical techniques, and a large number of genes encoding enzymes of volatile biosynthesis have recently been reported.

show abstract

Section: Carbohydrate-derived Flavor Compoundsmentioning

confidence: 99%

Biosynthesis of plant‐derived flavor compounds

Schwab¹,

Davidovich‐Rikanati²,

Lewinsohn³

2008

The Plant Journal

968

704

View full text Add to dashboard Cite

show abstract

“…While most biochemical reactions leading to tocopherol biosynthesis were identified more than two decades ago Soll et al, , 1983Soll et al, , 1985, genes encoding enzymes for tocopherol biosynthesis were identified relatively recently (Shintani and DellaPenna, 1998;Collakova and DellaPenna, 2001;Porfirova et al, 2002;Savidge et al, 2002;Cheng et al, 2003;Rohmer, 2003;Van Eenennaam et al, 2003). Homogentisic acid and phytyldiphosphate (PDP) serve as precursors for tocopherol biosynthesis (Figure 1).…”

Section: Introductionmentioning

confidence: 99%

TheArabidopsis vitamin E pathway gene5-1Mutant Reveals a Critical Role for Phytol Kinase in Seed Tocopherol Biosynthesis

Lincoln²,

et al. 2005

View full text Add to dashboard Cite

We report the identification and characterization of a low tocopherol Arabidopsis thaliana mutant, vitamin E pathway gene5-1 (vte5-1), with seed tocopherol levels reduced to 20% of the wild type. Map-based identification of the responsible mutation identified a G!A transition, resulting in the introduction of a stop codon in At5g04490, a previously unannotated gene, which we named VTE5. Complementation of the mutation with the wild-type transgene largely restored the wild-type tocopherol phenotype. A knockout mutation of the Synechocystis sp PCC 6803 VTE5 homolog slr1652 reduced Synechocystis tocopherol levels by 50% or more. Bioinformatic analysis of VTE5 and slr1652 indicated modest similarity to dolichol kinase. Analysis of extracts from Arabidopsis and Synechocystis mutants revealed increased accumulation of free phytol. Heterologous expression of these genes in Escherichia coli supplemented with free phytol and in vitro assays of recombinant protein produced phytylmonophosphate, suggesting that VTE5 and slr1652 encode phytol kinases. The phenotype of the vte5-1 mutant is consistent with the hypothesis that chlorophyll degradation-derived phytol serves as an important intermediate in seed tocopherol synthesis and forces reevaluation of the role of geranylgeranyl diphosphate reductase in tocopherol biosynthesis.

show abstract

“…found in most eubacteria, green algae, and the chloroplasts of higher plants (1,5,6). In the MVA pathway, DMAPP must be generated from IPP by an isopentenyl diphophate/ dimethylallyl diphosphate isomerase (IDI, Scheme 1) (1).…”

mentioning

confidence: 99%

Evidence for the Involvement of Acid/Base Chemistry in the Reaction Catalyzed by the Type II Isopentenyl Diphosphate/Dimethylallyl Diphosphate Isomerase from Staphylococcus aureus

et al. 2008

View full text Add to dashboard Cite

The type II isopentenyl diphosphate/dimethylallyl diphosphate isomerase (IDI-2) is a flavin mononucleotide (FMN)-dependent enzyme that catalyzes the reversible isomerization of isopentenyl pyrophosphate (IPP) to dimethylallyl pyrophosphate (DMAPP), a reaction with no net change in redox state of the coenzyme or substrate. Here, UV-vis spectral analysis of the IDI-2 reaction revealed the accumulation of a reduced neutral dihydroflavin intermediate when the reduced enzyme was incubated with IPP or DMAPP. When IDI-2 was reconstituted with 1-deazaFMN and 5-deazaFMN, similar reduced neutral forms of the deazaflavin analogues were observed in the presence of IPP. Single turnover stopped-flow absorbance experiments indicated that this flavin intermediate formed and decayed at kinetically competent rates in the pre-steadystate and, thus, most likely represents a true intermediate in the catalytic cycle. UV-vis spectra of the reaction mixtures reveal trace amounts of a neutral semiquinone, but evidence for the presence of IPP-based radicals could not be obtained by EPR spectroscopy. Rapid-mix chemical quench experiments show no burst in DMAPP formation, suggesting that the rate determining step in the forward direction (IPP to DMAPP) occurs prior to DMAPP formation. A solvent deuterium kinetic isotope effect ( D 2 O V max = 1.5) was measured on v o in steady-state kinetic experiments at saturating substrate concentrations. A substrate deuterium kinetic isotope effect was also measured on the initital velocity ( D V max = 1.8) and on the decay rate of the flavin intermediate ( D k s = 2.3) in single-turnover stopped-flow experiments using (R)-[2-2 H]-IPP. Taken together, these data suggest that the C2-H bond of IPP is cleaved in the rate determining step and that general acid/ base catalysis may be involved during turnover. Possible mechanisms for the IDI-2 catalyzed reaction are presented and discussed in terms of the available X-ray crystal structures.Isoprenoids comprise a large and ubiquitous class of metabolites that participate in numerous physiological processes (1-4). All isoprenoids are derived initially from the condensation of two isoprene units, isopentenyl pyrophosphate (IPP, 1)1 and dimethylallyl pyrophosphate (DMAPP, 2). Two biosynthetic pathways for the production of IPP and DMAPP are known, the mevalonate (MVA) pathway found in animals, fungi, and archaebacteria, and the non-mevalonate or methyl erythritol phosphate (MEP) pathway † This work was supported in part by a Welch Foundation Grant (F-1511), a National Institutes of Health Grant (GM40541), and a NIH-PA Author ManuscriptNIH-PA Author Manuscript NIH-PA Author Manuscript found in most eubacteria, green algae, and the chloroplasts of higher plants (1,5,6). In the MVA pathway, DMAPP must be generated from IPP by an isopentenyl diphophate/ dimethylallyl diphosphate isomerase (IDI, Scheme 1) (1). In the MEP pathway, both IPP and DMAPP are coproduced from 4-hydroxy-3-methyl-2-butenyl diphosphate in the same enzymatic reaction (catalyzed by IspH)...

show abstract

Mevalonate-independent methylerythritol phosphate pathway for isoprenoid biosynthesis. Elucidation and distribution

Cited by 144 publications

References 72 publications

Biosynthesis of plant‐derived flavor compounds

Biosynthesis of plant‐derived flavor compounds

TheArabidopsis vitamin E pathway gene5-1Mutant Reveals a Critical Role for Phytol Kinase in Seed Tocopherol Biosynthesis

Evidence for the Involvement of Acid/Base Chemistry in the Reaction Catalyzed by the Type II Isopentenyl Diphosphate/Dimethylallyl Diphosphate Isomerase from Staphylococcus aureus

Contact Info

Product

Resources

About