Molecular and structural basis of metabolic diversity mediated by prenyldiphosphate converting enzymes

Brandt, Wolfgang; Bräuer, Lars; Günnewich, Nils; Kufka, Julia; Rausch, Felix; Schulze, Diana; Schulze, Eva; Weber, Roman; Zakharova, S. V.; Wessjohann, Ludger A.

doi:10.1016/j.phytochem.2009.09.001

Cited by 52 publications

(51 citation statements)

References 115 publications

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“…The side chains of F734, F737, and F738 seem to be sterically not accessible for cation stabilization. This again shows the importance of aromatic side chains for the cation-p stabilization of cyclic terpene cations (Petersen et al, 2005;Dougherty, 2007;Brandt et al, 2009). …”

Section: Nobilis a Dioecious Arboraceous Basal Dicotyledonous Spmentioning

confidence: 73%

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Identification, Functional Characterization, and Evolution of Terpene Synthases from a Basal Dicot

Yahyaa¹,

Matsuba²,

Brandt³

et al. 2015

Plant Physiol.

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Section: Nobilis a Dioecious Arboraceous Basal Dicotyledonous Spmentioning

confidence: 73%

“…Furthermore, an Arg (R296) may serve as a proton donor to thermodynamically support the cleavage of the diphosphate by protonation after the first step of the reaction (Brandt et al, 2009). In agreement (e.g.…”

Section: Nobilis a Dioecious Arboraceous Basal Dicotyledonous Spmentioning

confidence: 99%

Identification, Functional Characterization, and Evolution of Terpene Synthases from a Basal Dicot

Yahyaa¹,

Matsuba²,

Brandt³

et al. 2015

Plant Physiol.

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“…S2 in the supplemental material). The lye gene product is a member of the ubiA protein superfamily, which includes enzymes that transfer 5-carbon prenyl groups to various substrates (8). A membrane topology analysis by the TMHMM tool (18) predicted that lye encodes an integral membrane protein with 7 transmembrane domains (see Fig.…”

Section: Deletion Of Bop Results In Accumulation Of Bacterioruberinsmentioning

confidence: 99%

Bacterioopsin-Mediated Regulation of Bacterioruberin Biosynthesis in Halobacterium salinarum

et al. 2011

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Integral membrane protein complexes consisting of proteins and small molecules that act as cofactors have important functions in all organisms. To form functional complexes, cofactor biosynthesis must be coordinated with the production of corresponding apoproteins. To examine this coordination, we study bacteriorhodopsin (BR), a light-induced proton pump in the halophilic archaeon Halobacterium salinarum. This complex consists of a retinal cofactor and bacterioopsin (BO), the BR apoprotein. To examine possible novel regulatory mechanisms linking BO and retinal biosynthesis, we deleted bop, the gene that encodes BO. bop deletion resulted in a dramatic increase of bacterioruberins, carotenoid molecules that share biosynthetic precursors with retinal. Additional studies revealed that bacterioruberins accumulate in the absence of BO regardless of the presence of retinal or BR, suggesting that BO inhibits bacterioruberin biosynthesis to increase the availability of carotenoid precursors for retinal biosynthesis. To further examine this potential regulatory mechanism, we characterized an enzyme, encoded by the lye gene, that catalyzes bacterioruberin biosynthesis. BO-mediated inhibition of bacterioruberin synthesis appears to be specific to the H. salinarum lye-encoded enzyme, as expression of a lye homolog from Haloferax volcanii, a related archaeon that synthesizes bacterioruberins but lacks opsins, resulted in bacterioruberin synthesis that was not reduced in the presence of BO. Our results provide evidence for a novel regulatory mechanism in which biosynthesis of a cofactor is promoted by apoprotein-mediated inhibition of an alternate biochemical pathway. Specifically, BO accumulation promotes retinal production by inhibiting bacterioruberin biosynthesis.

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“…During chain elongation, the allylic cosubstrate (DMADP or GDP) undergoes coupling with IDP through electrophilic alkylation at its carbon-carbon double bond (18,19). The reaction depends for activation on a trinuclear metal cluster, usually containing Mg 2+ or Mn 2+ (20).…”

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confidence: 99%

Metal ions control product specificity of isoprenyl diphosphate synthases in the insect terpenoid pathway

Frick¹,

Nagel

Schmidt

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

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Isoprenyl diphosphate synthases (IDSs) produce the ubiquitous branched-chain diphosphates of different lengths that are precursors of all major classes of terpenes. Typically, individual shortchain IDSs (scIDSs) make the C 10 , C 15 , and C 20 isoprenyl diphosphates separately. Here, we report that the product length synthesized by a single scIDS shifts depending on the divalent metal cofactor present. This previously undescribed mechanism of carbon chainlength determination was discovered for a scIDS from juvenile horseradish leaf beetles, Phaedon cochleariae. The recombinant enzyme P. cochleariae isoprenyl diphosphate synthase 1 (PcIDS1) yields 96% C 10 -geranyl diphosphate (GDP) and only 4% C 15 -farnesyl diphosphate (FDP) in the presence of Co 2+ or Mn 2+ as a cofactor, whereas it yields only 18% C 10 GDP but 82% C 15 FDP in the presence of Mg 2+. In reaction with Co 2+ , PcIDS1 has a K m of 11.6 μM for dimethylallyl diphosphate as a cosubstrate and 24.3 μM for GDP. However, with Mg 2+ , PcIDS1 has a K m of 1.18 μM for GDP, suggesting that this substrate is favored by the enzyme under such conditions. RNAi targeting PcIDS1 revealed the participation of this enzyme in the de novo synthesis of defensive monoterpenoids in the beetle larvae. As an FDP synthase, PcIDS1 could be associated with the formation of sesquiterpenes, such as juvenile hormones. Detection of Co , or Mg 2+ in the beetle larvae suggests flux control into C 10 vs. C 15 isoprenoids could be accomplished by these ions in vivo. The dependence of product chain length of scIDSs on metal cofactor identity introduces an additional regulation for these branch point enzymes of terpene metabolism.cobalt | kinetic | prenyltransferase | secretions | silencing

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Molecular and structural basis of metabolic diversity mediated by prenyldiphosphate converting enzymes

Cited by 52 publications

References 115 publications

Identification, Functional Characterization, and Evolution of Terpene Synthases from a Basal Dicot

Identification, Functional Characterization, and Evolution of Terpene Synthases from a Basal Dicot

Bacterioopsin-Mediated Regulation of Bacterioruberin Biosynthesis in Halobacterium salinarum

Metal ions control product specificity of isoprenyl diphosphate synthases in the insect terpenoid pathway

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