Studies on isoprenoid biosynthesis with bacterial intact cells

Takatsuji, Hiroshi; Nishino, Tokuzo; Miki, Ichiro; Katsuki, Hirohiko

doi:10.1016/0006-291x(83)91278-0

Cited by 15 publications

(14 citation statements)

References 14 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Although isoprenic alcohol esters have been repeatedly described in eukaryotes and prokaryotes [17 - [21]. This esterification performed in high yield (70%) consumed most of the starting material and no pentaprenol cyclization was observed.…”

Section: Resultsmentioning

confidence: 94%

Enzymatic cyclization of all‐trans pentaprenyl and hexaprenyl methyl ethers by a cell‐free system from the protozoon Tetrahymena pyriformis

Renoux¹,

Rohmer²

1986

European Journal of Biochemistry

View full text Add to dashboard Cite

A cell-free system from the protozoon Tetrahymenapyriforrnis capable of cyclizing squalene into tetrahymanol cyclizes all-trans pentaprenyl methyl ether to a scalarane-type sesterterpene and all-trans hexaprenyl methyl ether to bicyclo-, tricyclo-, tetracyclo-and pentacyclohexaprenyl methyl ethers, each corresponding to a possible cationic intermediate. The structures of the cyclization products have been determined by spectroscopic methods and are compatible with a biogenetic scheme involving polyprenyl ether cyclization. This is the first direct proof of an enzymatic cyclization of higher isoprenic alcohol derivatives, and we assume it was performed by the squalene-to-hopane cyclase of the protozoon. The formation of a scalarane-type sesterterpene from CZ5 polyprenyl methyl ether suggests that these terpenoids, whose presence is restricted to a few sponges, might be in fact microbial metabolites. Tricyclopolyprenyl derivatives have been identified in the organic matter from numerous sediments and they were interpreted as being chemical fossils of still unidentified microorganisms. The cyclization of hexaprenyl methyl ether is the first attempt of identification of these tricyclopolyprenol derivatives in living organisms.Some of the numerous microbial lipids have been discovered after the identification of their chemical fossils dispersed in the organic matter of sediments [l]. The ubiquitous geohopanoids are the most striking example: they have been found to be present, varied and abundant, in all sediments analyzed up to now, and they were found to be the molecular fossils of a new class of widespread and varied prokaryotic lipids, the microbial hopanoids [2, 31. The existence of other new classes of microbial lipids has been postulated by us from the wide distribution of still 'orphan' chemical fossils, plausible precursors of which were unknown in extant microorganisms [l]. These included, for instance, aliphathic glycerol ethers similar to the archaebacterial lipid ethers, the pentacyclic triterpene isoarborinol and the tricyclopolyprenols. The existence of the latter compounds in microorganisms was suggested by the identification of tricyclic sedimentary hydrocarbons in the CI9 to C45 range' [4-71. Biogenetically, these isoprenoids can be deduced from a proton-catalyzed cyclization of suitable regular polyprenol derivatives giving tricyclic compounds, the structures of which resemble those of some natural sesterterpenes isolated from a fern or a nudibranch [8,9]. Such cyclizations have already been studied in the biosynthesis of lower homologues from the mono-, sesqui-and diterpene series.Correspondence to M. Rohmer, Ecole Nationale Superieure de Chimie de Mulhouse, 3 rue Alfred Werner, F-68093 Mulhouse Cedex, France A bbreviutions. TLC, thin-layer chromatography; GLC, gas-liquid chromatography; MS, mass spectrometry; NMR, nuclear magnetic resonance.In an attempt to detect these isoprenoids in living organisms, we tried to cyclize tritium-labelled all-trans pentaprenol and hexaprenol derivatives with cell...

show abstract

Section: Resultsmentioning

confidence: 94%

Enzymatic cyclization of all‐trans pentaprenyl and hexaprenyl methyl ethers by a cell‐free system from the protozoon Tetrahymena pyriformis

Renoux¹,

Rohmer²

1986

European Journal of Biochemistry

View full text Add to dashboard Cite

show abstract

“…(Raman et al, 1965) and by permeabilized E. coli (Fujisaki et al, 1986a). Mevalonate also failed to be incorporated into isoprenoid compounds by a series of bacteria isolated from soil which could use mevalonate as their sole carbon source (Takatsuji et al, 1983). Other observations include the inability of cell extracts of Rhodospirillum rubrum to incorporate mevalonate into polyprenylphenol precursors of ubiquinones (Raman et al, 1969), and the lack of incorporation of mevalonate into the modified bases of tRNA by E. coli (Peterkofsky, 1968).…”

Section: Introductionmentioning

confidence: 95%

Early steps of isoprenoid biosynthesis in Escherichia coli

Zhou

White

1991

Biochemical Journal

View full text Add to dashboard Cite

The incorporation of 2H- and 13C-labelled precursors into ubiquinone-8 (Uq-8) by strains of Escherichia coli was measured in order to define the pathway for the early steps in the biosynthesis of isoprenoids in these eubacteria. Cells grown with DL-[methyl-2H6]valine were found to label both the alpha-oxoisovaleric (‘alpha-ketoisovaleric’) acid alpha-oxoisohexanoic (‘alpha-ketoisocaproic’) acid, but not the Uq-8. Since these acids are required for the biosynthesis of isoprenoids by the acetolactate pathway, the operation of this pathway in the biosynthesis of Uq-8 is excluded. Cells grown with [1,2-13C2]acetate and non-labelled glucose readily incorporated 13C2 units into fatty acids, but failed to incorporate any label into the Uq-8. Cells grown with [U-13C6]glucose and non-labelled acetate, however, were found to label both the fatty acids and the Uq-8. Oxidative cleavage with periodate/permanganate of the Uq-8 isolated from cells grown with U-13C6-labelled glucose produced laevulinic acid, which was shown to be derived from two C2 units and one C1 unit of the labelled glucose by mass-spectral analysis of the 4,5-dihydro-6-methyl-2-phenylpyridazin-3(2H)-one derivative. The results of this work indicate that the C-2 and C-3 carbon unit of pyruvate, not acetyl-CoA, is the precursor to isopentenyl pyrophosphate (IPP) in these cells; however, the labelling pattern observed is consistent with the established acetoacetate pathway of isoprenoid biosynthesis. These data, coupled with the observed lack of inhibition of the growth of E. coli by mevinolin, a specific inhibitor of 3-hydroxy-3-methylglutaryl-CoA, can be best rationalized by the biosynthesis of IPP occurring in E. coli through a series of bound intermediates.

show abstract

“…While the biosynthetic role of mevalonate in mammalian cells has been well established, little is known about mevalonate utilization in bacteria. Several procaryotes capable of growth on mevalonate as their sole carbon source have, however, been isolated (3,8,9,23,24,27).…”

mentioning

confidence: 99%

Nucleotide sequence and expression in Escherichia coli of the 3-hydroxy-3-methylglutaryl coenzyme A lyase gene of Pseudomonas mevalonii

Anderson

Rodwell

1989

J Bacteriol

View full text Add to dashboard Cite

The mva operon of Pseudomonas mevalonii encodes two enzymes that can convert internalized mevalonate into acetoacetate and acetyl-coenzyme A (CoA). The promoter-proximal gene of this operon is mvaA, the structural gene for 3-hydroxy-3-methylglutaryl (HMG)-CoA reductase (EC 1.1.1.88). The cloning, characterization, and expression of mvaA has been reported (M. J. Beach and V. W. Rodwell, J. Bacteriol. 171:2994-3001, 1989). We report here the nucleotide sequence of another gene of this operon, mvaB, its expression in Escherichia coli, and its identification as the structural gene for HMG-CoA lyase (EC 4.1.3.4). P. mevalonii HMG-CoA lyase is a cytosolic protein with 301 amino acid residues and a molecular weight of 31,600. This represents the first reported sequence of an HMG-CoA lyase from any source.

show abstract

Studies on isoprenoid biosynthesis with bacterial intact cells

Cited by 15 publications

References 14 publications

Enzymatic cyclization of all‐trans pentaprenyl and hexaprenyl methyl ethers by a cell‐free system from the protozoon Tetrahymena pyriformis

Enzymatic cyclization of all‐trans pentaprenyl and hexaprenyl methyl ethers by a cell‐free system from the protozoon Tetrahymena pyriformis

Early steps of isoprenoid biosynthesis in Escherichia coli

Nucleotide sequence and expression in Escherichia coli of the 3-hydroxy-3-methylglutaryl coenzyme A lyase gene of Pseudomonas mevalonii

Contact Info

Product

Resources

About