scholarly journals Biosynthesis of the labdane diterpene marrubiin in Marrubium vulgare via a non-mevalonate pathway

1997 ◽  
Vol 326 (2) ◽  
pp. 449-454 ◽  
Author(s):  
Werner KNÖSS ◽  
Bernd REUTER ◽  
Josef ZAPP
Keyword(s):  
Mevalonate Pathway ◽  
Alternative Pathway ◽  
Mevalonic Acid ◽  
13C Nmr Spectroscopy ◽  
Shoot Cultures ◽  
Isopentenyl Diphosphate ◽  
Glucose Incorporation ◽  
Labdane Diterpene ◽  
Marrubium Vulgare ◽  
Putative Precursor

The biosynthesis of the furanic labdane diterpene marrubiin has been studied in plantlets and shoot cultures of Marrubium vulgare(Lamiaceae). The use of [2-14C]acetate, [2-14C]pyruvate, [2-14C]mevalonic acid and [U-14C]glucose incorporation experiments showed that the labelling of sterols in etiolated shoot cultures of M. vulgare was in accordance with their biosynthesis via the acetate–mevalonate pathway. In contrast, the incorporation rates of these precursors into the diterpene marrubiin could not be explained by biosynthesis of this compound via the acetate–mevalonate pathway. Cultivation of etiolated shoot cultures of M. vulgare on medium containing [1-13C]glucose and subsequent 13C-NMR spectroscopy of marrubiin led to the conclusion that the biosynthesis of marrubiin follows a non-mevalonate pathway. All isoprenic units of 13C-labelled marrubiin were enriched in those carbons that correspond to positions 1 and 5 of a putative precursor isopentenyl diphosphate. This labelling pattern from [1-13C]glucose is consistent with an alternative pathway via trioses, which has already been shown to occur in Eubacteria and Gymnospermae. The labdane skeleton is a precursor of many other skeletal types of diterpenes. Therefore it becomes obvious that in connection with the few known examples of a non-mevalonate pathway to isoprenoids the formation of some isoprenoids in plants via a non-mevalonate pathway might be quite common.

scholarly journals Biosynthesis of isoprenoids (carotenoids, sterols, prenyl side-chains of chlorophylls and plastoquinone) via a novel pyruvate/glyceraldehyde 3-phosphate non-mevalonate pathway in the green alga Scenedesmus obliquus*

1996 ◽  
Vol 316 (1) ◽  
pp. 73-80 ◽  
Author(s):  
Jörg SCHWENDER ◽  
Myriam SEEMANN ◽  
Hartmut K. LICHTENTHALER ◽  
Michel ROHMER
Keyword(s):  
Green Alga ◽  
13C Nmr ◽  
Mevalonate Pathway ◽  
Scenedesmus Obliquus ◽  
13C Nmr Spectroscopy ◽  
Side Chains ◽  
Isopentenyl Diphosphate ◽  
The Novel ◽  
13C Labelling ◽  
Β Carotene

Isoprenoid biosynthesis was investigated in the green alga Scenedesmus obliquus grown heterotrophically on 13C-labelled glucose and acetate. Several isoprenoid compounds were isolated and investigated by 13C-NMR spectroscopy. According to the 13C-labelling pattern indicated by the 13C-NMR spectra, the biosynthesis of all plastidic isoprenoids investigated (prenyl side-chains of chlorophylls and plastoquinone-9, and the carotenoids β-carotene and lutein), as well as of the non-plastidic cytoplasmic sterols, does not proceed via the classical acetate/mevalonate pathway (which leads from acetyl-CoA via mevalonate to isopentenyl diphosphate), but via the novel glyceraldehyde 3-phosphate/pyruvate route recently detected in eubacteria. Formation of isopentenyl diphosphate involves the condensation of a C2 unit derived from pyruvate decarboxylation with glyceraldehyde 3-phosphate and a transposition yielding the branched C5 skeleton of isoprenic units.

Inhibition of the mevalonate pathway enhances carvacrol biosynthesis and DXR gene expression in shoot cultures of Satureja khuzistanica Jamzad

2013 ◽  
Vol 170 (13) ◽  
pp. 1187-1193 ◽  
Author(s):  
Parvin Ramak ◽  
Shahrokh Kazempour Osaloo ◽  
Hassan Ebrahimzadeh ◽  
Mozafar Sharifi ◽  
Mehrdad Behmanesh
Keyword(s):  
Gene Expression ◽  
Mevalonate Pathway ◽  
Shoot Cultures

Mevalonic acid partially restores chloroplast and etioplast development in Arabidopsis lacking the non-mevalonate pathway

Planta ◽  
2002 ◽  
Vol 216 (2) ◽  
pp. 345-350 ◽  
Author(s):  
Noriko Nagata ◽  
Masashi Suzuki ◽  
Shigeo Yoshida ◽  
Toshiya Muranaka
Keyword(s):  
Mevalonate Pathway ◽  
Mevalonic Acid

scholarly journals Identification, Evolution, and Essentiality of the Mevalonate Pathway for Isopentenyl Diphosphate Biosynthesis in Gram-Positive Cocci

2000 ◽  
Vol 182 (15) ◽  
pp. 4319-4327 ◽  
Author(s):  
E. Imogen Wilding ◽  
James R. Brown ◽  
Alexander P. Bryant ◽  
Alison F. Chalker ◽  
David J. Holmes ◽  
...  
Keyword(s):  
Mevalonate Pathway ◽  
Genomic Analysis ◽  
Eukaryotic Cell ◽  
Infection Model ◽  
Isopentenyl Diphosphate ◽  
Gram Positive ◽  
Hmg Coa Reductase ◽  
Coa Reductase ◽  
Gram Positive Cocci

ABSTRACT The mevalonate pathway and the glyceraldehyde 3-phosphate (GAP)–pyruvate pathway are alternative routes for the biosynthesis of the central isoprenoid precursor, isopentenyl diphosphate. Genomic analysis revealed that the staphylococci, streptococci, and enterococci possess genes predicted to encode all of the enzymes of the mevalonate pathway and not the GAP-pyruvate pathway, unlike Bacillus subtilis and most gram-negative bacteria studied, which possess only components of the latter pathway. Phylogenetic and comparative genome analyses suggest that the genes for mevalonate biosynthesis in gram-positive cocci, which are highly divergent from those of mammals, were horizontally transferred from a primitive eukaryotic cell. Enterococci uniquely encode a bifunctional protein predicted to possess both 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase and acetyl-CoA acetyltransferase activities. Genetic disruption experiments have shown that five genes encoding proteins involved in this pathway (HMG-CoA synthase, HMG-CoA reductase, mevalonate kinase, phosphomevalonate kinase, and mevalonate diphosphate decarboxylase) are essential for the in vitro growth of Streptococcus pneumoniae under standard conditions. Allelic replacement of the HMG-CoA synthase gene rendered the organism auxotrophic for mevalonate and severely attenuated in a murine respiratory tract infection model. The mevalonate pathway thus represents a potential antibacterial target in the low-G+C gram-positive cocci.

scholarly journals 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

2002 ◽  
Vol 366 (2) ◽  
pp. 573-583 ◽  
Author(s):  
Jean-François HOEFFLER ◽  
Andréa HEMMERLIN ◽  
Catherine GROSDEMANGE-BILLIARD ◽  
Thomas J. BACH ◽  
Michel ROHMER
Keyword(s):  
Escherichia Coli ◽  
Higher Plants ◽  
Mevalonic Acid ◽  
Cell Suspension Cultures ◽  
Mep Pathway ◽  
Isopentenyl Diphosphate ◽  
Higher Plant ◽  
Methylerythritol Phosphate Pathway ◽  
Dimethylallyl Diphosphate ◽  
Deuterium Retention

In the bacterium Escherichia coli, the mevalonic-acid (MVA)-independent 2-C-methyl-d-erythritol 4-phosphate (MEP) pathway is characterized by two branches leading separately to isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). The signature of this branching is the retention of deuterium in DMAPP and the deuterium loss in IPP after incorporation of 1-[4-2H]deoxy-d-xylulose ([4-2H]DX). Feeding tobacco BY-2 cell-suspension cultures with [4-2H]DX resulted in deuterium retention in the isoprene units derived from DMAPP, as well as from IPP in the plastidial isoprenoids, phytoene and plastoquinone, synthesized via the MEP pathway. 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.

scholarly journals Peroxisomal Localization of Arabidopsis Isopentenyl Diphosphate Isomerases Suggests That Part of the Plant Isoprenoid Mevalonic Acid Pathway Is Compartmentalized to Peroxisomes

2008 ◽  
Vol 148 (3) ◽  
pp. 1219-1228 ◽  
Author(s):  
Maya Sapir-Mir ◽  
Anahit Mett ◽  
Eduard Belausov ◽  
Shira Tal-Meshulam ◽  
Ahuva Frydman ◽  
...  
Keyword(s):  
Mevalonic Acid ◽  
Isopentenyl Diphosphate ◽  
Mevalonic Acid Pathway ◽  
Acid Pathway

The deoxyxylulose phosphate pathway of isoprenoid biosynthesis. Discovery and function of the ispDEFGH genes and their cognate enzymes

2003 ◽  
Vol 75 (2-3) ◽  
pp. 393-405 ◽  
Author(s):  
F. Rohdich ◽  
Stefan Hecht ◽  
Adelbert Bacher ◽  
Wolfgang Eisenreich
Keyword(s):  
Biosynthetic Pathway ◽  
Mevalonate Pathway ◽  
Isoprenoid Biosynthesis ◽  
Catalytic Action ◽  
Isopentenyl Diphosphate ◽  
Dimethylallyl Diphosphate ◽  
And Function

Isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP) serve as the universal precursors for the biosynthesis of terpenes. Besides the well-known mevalonate pathway, a second biosynthetic pathway conducive to IPP and DMAPP via 1-deoxy-d-xylulose-5-phosphate and 2C-methyl-d-erythritol-4-phosphate has been discovered recently in plants and certain eubacteria. 2C-Methyl-d-erythritol-4-phosphate, the first committed intermediate of the deoxyxylulose phosphate pathway, is converted into 2C-methyl-d-erythritol 2,4-cyclodiphosphate by the catalytic action of three enzymes specified by the ispDEF genes. The cyclic diphosphate is reductively opened by the IspG protein affording 1-hydroxy-2-methyl-2-(E)-butenyl-4-diphosphate. This compound can be converted into IPP as well as DMAPP by the catalytic action of IspH protein. The enzymes of this pathway are potential targets for novel antibacterial, antimalarial, and herbicide agents.

scholarly journals Cloning and Characterization of 1-Deoxy-d-Xylulose 5-Phosphate Synthase fromStreptomyces sp. Strain CL190, Which Uses both the Mevalonate and Nonmevalonate Pathways for Isopentenyl Diphosphate Biosynthesis

2000 ◽  
Vol 182 (4) ◽  
pp. 891-897 ◽  
Author(s):  
Tomohisa Kuzuyama ◽  
Motoki Takagi ◽  
Shunji Takahashi ◽  
Haruo Seto
Keyword(s):  
Molecular Mass ◽  
Mevalonate Pathway ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Initial Step ◽  
Enzymatic Properties ◽  
Isopentenyl Diphosphate ◽  
Ph Optimum ◽  
Nonmevalonate Pathway

ABSTRACT In addition to the ubiquitous mevalonate pathway,Streptomyces sp. strain CL190 utilizes the nonmevalonate pathway for isopentenyl diphosphate biosynthesis. The initial step of this nonmevalonate pathway is the formation of 1-deoxy-d-xylulose 5-phosphate (DXP) by condensation of pyruvate and glyceraldehyde 3-phosphate catalyzed by DXP synthase. The corresponding gene, dxs, was cloned from CL190 by using PCR with two oligonucleotide primers synthesized on the basis of two highly conserved regions among dxs homologs from six genera. Thedxs gene of CL190 encodes 631 amino acid residues with a predicted molecular mass of 68 kDa. The recombinant enzyme overexpressed in Escherichia coli was purified as a soluble protein and characterized. The molecular mass of the enzyme was estimated to be 70 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and 130 kDa by gel filtration chromatography, suggesting that the enzyme is most likely to be a dimer. The enzyme showed a pH optimum of 9.0, with a V max of 370 U per mg of protein and Km s of 65 μM for pyruvate and 120 μM for d-glyceraldehyde 3-phosphate. The purified enzyme catalyzed the formation of 1-deoxyxylulose by condensation of pyruvate and glyceraldehyde as well, with aKm value of 35 mM ford-glyceraldehyde. To compare the enzymatic properties of CL190 and E. coli DXP synthases, the latter enzyme was also overexpressed and purified. Although these two enzymes had different origins, they showed the same enzymatic properties.

scholarly journals Escherichia coli Open Reading Frame 696 Is idi, a Nonessential Gene Encoding Isopentenyl Diphosphate Isomerase

1999 ◽  
Vol 181 (15) ◽  
pp. 4499-4504 ◽  
Author(s):  
Frederick M. Hahn ◽  
Anthony P. Hurlburt ◽  
C. Dale Poulter
Keyword(s):  
Escherichia Coli ◽  
Mevalonate Pathway ◽  
Open Reading Frame ◽  
Restrictive Temperature ◽  
Isopentenyl Diphosphate ◽  
Isopentenyl Diphosphate Isomerase ◽  
Reading Frame ◽  
E Coli ◽  
Isoprene Unit ◽  
Nonessential Gene

ABSTRACT Isopentenyl diphosphate isomerase catalyzes the interconversion of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). In eukaryotes, archaebacteria, and some bacteria, IPP is synthesized from acetyl coenzyme A by the mevalonate pathway. The subsequent isomerization of IPP to DMAPP activates the five-carbon isoprene unit for subsequent prenyl transfer reactions. In Escherichia coli, the isoprene unit is synthesized from pyruvate and glyceraldehyde-3-phosphate by the recently discovered nonmevalonate pathway. An open reading frame (ORF696) encoding a putative IPP isomerase was identified in the E. coli chromosome at 65.3 min. ORF696 was cloned into an expression vector; the 20.5 kDa recombinant protein was purified in three steps, and its identity as an IPP isomerase was established biochemically. The gene for IPP isomerase, idi, is not clustered with other known genes for enzymes in the isoprenoid pathway. E. coli FH12 was constructed by disruption of the chromosomal idi gene with the aminoglycoside 3′-phosphotransferase gene and complemented by the wild-type idi gene on plasmid pFMH33 with a temperature-sensitive origin of replication. FH12/pFMH33 was able to grow at the restrictive temperature of 44°C and FH12 lacking the plasmid grew on minimal medium, thereby establishing thatidi is a nonessential gene. Although theV max of the bacterial protein was 20-fold lower than that of its yeast counterpart, the catalytic efficiencies of the two enzymes were similar through a counterbalance inKm s. The E. coli protein requires Mg2+ or Mn2+ for activity. The enzyme contains conserved cysteine and glutamate active-site residues found in other IPP isomerases.

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