The enzymatic cyclization of nerolidyl diphosphate by δ-cadinene synthase from cotton stele tissue infected with verticillium dahliae

Alchanati, Iris; Patel, Jo Ann Acreman; Liu, Jinggao; Benedict, C. R.; Stipanovic, Robert D.; Bell, Alois A.; Cui, Yunxing; Magill, Clint

doi:10.1016/s0031-9422(98)80054-x

Cited by 33 publications

(7 citation statements)

References 22 publications

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“…The formation of an early intermediate (ϩ)-δ-cadinene 174 in enzyme preparations from G. barbadense has been investigated by feeding 2 H-labelled FPP and nerolidyl PP precursors. 170 Labelling patterns generated were consistent with the sequence shown in Scheme 36, in which the nerolidyl cation cyclizes to a germacradienyl cation 173 followed by a 1,3-hydride shift, a second cyclization, then proton loss. Thus, (1-RS)-[1-2 H]-FPP was converted into [5-2 H]-and [11-2 H]-δ-cadinene, demonstrating the 1,3-hydride shift, and a 2 H 5 -labelled sample of nerolidyl PP was converted with retention of all labels.…”

Section: Soluble Enzyme Preparations From Leaves Catalysed Divalentsupporting

confidence: 74%

The biosynthesis of C5–C25 terpenoid compounds

2002

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This review covers recently-published experimental information on the biosynthesis of terpenoids in the range C5-C25. In addition to sections on the mevalonate and mevalonate-independent (deoxyxylulose phosphate) pathways, the review considers in turn hemiterpenoids, polyprenyl diphosphate synthases, monoterpenoids, sesquiterpenoids, diterpenoids, and sesterterpenoids. The literature from January 1998 to December 2000 is reviewed, with 248 references cited.

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Section: Soluble Enzyme Preparations From Leaves Catalysed Divalentsupporting

confidence: 74%

The biosynthesis of C5–C25 terpenoid compounds

2002

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“…Deprotonation of this cation would produce δ-cadinene ( 9s ), while 1,2-hydride shift followed by 2,6-ring closure and quenching of the ensuing carbocation with H 2 O yields the tricyclic cubebol ( 8s ) as the second major product of Cop4. Labeling studies with deuterated (E,E) -FPP and reactions with ( 3R )-NPP using a recombinant sesquiterpene synthase from cotton have confirmed that δ-cadinene biosynthesis requires the isomerization (E,E) -FPP [28, 32]. A similar mechanism via ( 3R )-NPP has also been described for the synthesis of (−)–germacrene D by germacradienol/germacrene D synthase from Streptomyces coelicolor [54].…”

Section: Discussionmentioning

confidence: 82%

“…FPP isomers and analogs have been used in studies with several sesquiterpene synthases to determine the mechanism of carbocation quenching [28–31] and the initial ionization and isomerization of all-trans- FPP for cis-trans-pathway specific enzymes [32–35]. However, most studies compared the kinetic properties of different FPP substrate geometrical isomers.…”

Section: Introductionmentioning

confidence: 99%

Sesquiterpene Synthases Cop4 and Cop6 from Coprinus cinereus: Catalytic Promiscuity and Cyclization of Farnesyl Pyrophosphate Geometric Isomers

et al. 2010

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Sesquiterpene synthases catalyze with different catalytic fidelity the cyclization of farnesyl pyrophosphate (FPP) into hundreds of known compounds with diverse structures and stereochemistries. Two sesquiterpene synthases, Cop4 and Cop6, were previously isolated from Coprinus cinereus as part of a fungal genome survey. This study investigates the reaction mechanism and catalytic fidelity of the two enzymes. Cyclization of all-trans-FPP ((E,E)-FPP) was compared to the cyclization of the cis-trans isomer of FPP ((Z,E)-FPP) as a surrogate for the secondary cisoid neryl cation intermediate generated by sesquiterpene synthases capable of isomerizing the C2-C3 π bond of all-trans-FPP. Cop6 is a “high-fidelity” α-cuprenene synthase that retains its fidelity under various conditions tested. Cop4 is a catalytically promiscuous enzyme that cyclizes (E,E)-FPP into multiple products, including (−)-germacrene D and cubebol. Changing the pH of the reaction drastically alters the fidelity of Cop4 and makes it a highly selective enzyme. Cyclization of (Z,E)-FPP by Cop4 and Cop6 yields products that are very different from those obtained with (E,E)-FPP. Conversion of (E,E)-FPP proceeds via a (6R)-β-bisabolyl carbocation in the case of Cop6 and an (E,E)-germacradienyl carbocation in the case of Cop4. However, (Z,E)-FPP is cyclized via a (6S)-β-bisabolene carbocation by both enzymes. Structural modeling suggests that differences in the active site and the loop that covers the active site of the two enzymes may explain their different catalytic fidelities.

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“…Many of the finer points in the mechanism of formation of inter alia (+)-aristolochene (11), 30,57 trichodiene (20), 32,58 d-cadinene (22), 59,60 epi-cubenol (24), 61-64 pentalenene (16), [65][66][67] and (À) and (+)-germacrene D (25 and 26) 68 were uncovered using deuterated, tritiated and carbon-14 labelled analogues of FDP and NDP. Much of this work has been reviewed previously.…”

Section: Substrate Analoguesmentioning

confidence: 99%

Sesquiterpene synthases: Passive catalysts or active players?

2012

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Sesquiterpene synthases catalyse the metal dependent turnover of farnesyl diphosphate to generate a class of natural products characterised by an enormous diversity in structure, stereochemistry, biological function and application. It has been proposed that these enzymes take a passive role in the reactions they catalyse and that they serve mostly as stereochemical templates, within which the reactions take place. Here, recent research into the structure and function of sesquiterpene synthases and the mechanisms of the reactions that they catalyse will be reviewed to suggest that these fascinating enzymes play multifaceted active roles in what are arguably the most complex biosynthetic reactions.

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The enzymatic cyclization of nerolidyl diphosphate by δ-cadinene synthase from cotton stele tissue infected with verticillium dahliae

Cited by 33 publications

References 22 publications

The biosynthesis of C5–C25 terpenoid compounds

The biosynthesis of C5–C25 terpenoid compounds

Sesquiterpene Synthases Cop4 and Cop6 from Coprinus cinereus: Catalytic Promiscuity and Cyclization of Farnesyl Pyrophosphate Geometric Isomers

Sesquiterpene synthases: Passive catalysts or active players?

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