(+)-δ-Cadinene is a product of sesquiterpene cyclase activity in cotton

Davis, Garrett J.; Essenberg, Margaret

doi:10.1016/0031-9422(95)00067-h

Cited by 66 publications

(42 citation statements)

References 62 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…LL-B7 (Cane and Tandon, 1995). Since CDN has been shown to be the precursor of dHG and HG in cotton (Davis and Essenberg, 1995), the proposed mechanism for the cyclization of E,E-FDP to CDN by CDN1-C1 accounts for the formation of the carbon structure of these defense sesquiterpenes.…”

Section: Discussionmentioning

confidence: 99%

“…In cotton, ␦-cadinene (CDN) synthase catalyzes the first step in the synthesis of dHG and HG from farnesyl diphosphate (FDP; Benedict et al, 1995;Chen et al, 1995;Davis and Essenberg, 1995;Davis et al, 1996). This reaction is induced by the infection of cotton with V. dahliae (Benedict et al, 1995;Bianchini et al, 1999).…”

mentioning

confidence: 99%

“…This reaction is induced by the infection of cotton with V. dahliae (Benedict et al, 1995;Bianchini et al, 1999). The infusion of cotton cotyledons with 3 H-CDN labels dHG and HG (Davis and Essenberg, 1995). Four cDNAs of CDN synthase (cdn1-C1, cdn1-C14, cdn1-A, and cdn1-C2) from Gossypium arboreum have been isolated and the molecular weight and kinetic properties of the expressed recombinant CDN synthase (CDN1-C1) for FDP have been reported (Chen et al, 1995(Chen et al, , 1996Meng et al, 1999).…”

mentioning

confidence: 99%

See 2 more Smart Citations

The Cyclization of Farnesyl Diphosphate and Nerolidyl Diphosphate by a Purified Recombinant δ-Cadinene Synthase

Benedict

Pettigrew

et al. 2001

Plant Physiology

View full text Add to dashboard Cite

The first step in the conversion of the isoprenoid intermediate, farnesyl diphosphate (FDP), to sesquiterpene phytoalexins in cotton (Gossypium barbadense) plants is catalyzed by ␦-cadinene (CDN) synthase. CDN is the precursor of desoxyhemigossypol and hemigossypol defense sesquiterpenes. In this paper we have studied the mechanism for the cyclization of FDP and the putative intermediate, nerolidyl diphosphate, to CDN. A purified recombinant CDN synthase (CDN1-C1) expressed in Escherichia coli from CDN1-C1 cDNA isolated from Gossypium arboreum cyclizes (1RS) uses (E,E)-FDP as effectively as (3R)-nerolidyl diphosphate in the formation of CDN. Cyclization studies with (3R)-nerolidyl diphosphate show that the formation of CDN, (E)-␤-farnesene, and ␤-bisabolene are enzyme dependent, but the formation of ␣-bisabolol in the reaction mixtures was a Mg 2ϩ -dependent solvolysis of nerolidyl diphosphate. Enzyme mechanisms are proposed for the formation of CDN from (E,E)-FDP and for the formation of CDN, (E)-␤-farnesene, and ␤-bisabolene from (3RS)-nerolidyl diphosphate. The primary structures of cotton CDN synthase and tobacco epi-aristolochene synthase show 48% identity, suggesting similar three-dimensional structures. We used the SWISS-MODEL to test this. The two enzymes have the same overall structure consisting of two ␣-helical domains and epi-aristolochene synthase is a good model for the structure of CDN synthase. Several amino acids in the primary structures of both synthases superimpose. The amino acids having catalytic roles in epi-aristochene synthase are substituted in the CDN synthase and may be related to differences in catalytic properties.

show abstract

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

See 1 more Smart Citation

The Cyclization of Farnesyl Diphosphate and Nerolidyl Diphosphate by a Purified Recombinant δ-Cadinene Synthase

Benedict

Pettigrew

et al. 2001

Plant Physiology

View full text Add to dashboard Cite

show abstract

“…In the case of Dilleniidae, biological responses to uronides have been characterized in cucumber (Robertsen and Svalheim, 1990) and cotton (Davis and Essenberg, 1995). Currently, we are unaware of any published data concerning the biological effects of OGAs on Arabidopsis.…”

Section: Discussionmentioning

confidence: 99%

Cloning of a cDNA encoding a plasma membrane-associated, uronide binding phosphoprotein with physical properties similar to viral movement proteins.

et al. 1996

View full text Add to dashboard Cite

Oligogalacturonides are structural and regulatory homopolymers from the extracellular pectic matrix of plants. In vitro micromolar concentrations of oligogalacturonates and polygalacturonates were shown previously to stimulate the phosphorylation of a small plasma membrane-associated protein in potato. lmmunologically cross-reactive proteins were detected in plasma membrane-enriched fractions from all angiosperm subclasses in the Cronquist system. Polygalacturonate-enhanced phosphorylation of the protein was observed in four of the six dicotyledon subclasses but not in any of the five monocotyledon subclasses. A cDNA for the protein was cloned from potato. The deduced protein is extremely hydrophilic and has a proline-rich N terminus. The C-terminal half of the protein was predicted to be a coiled coil, suggesting that the protein interacts with other macromolecules. The recombinant protein was found to bind both simple and complex galacturonides. The behavior of the protein suggests severa1 parallels with vira1 proteins involved in intercellular communication.

show abstract

“…Moreover, the total proteins isolated from cotton cotyledons treated with pathogen elicitors was able to catalyze the conversion of FPP into (+)--cadinene at a high rate, indicating that (+)--cadinene is a critical precursor or intermediate for phytoalexin biosynthesis Davila-Huerta et al, 1995;Davis and Essenberg, 1995). Later characterization of multiple (+)--cadinene synthase (CDN) proteins with different sequences revealed that it is encoded by a family includes at least CDN-A, CDN-B, CDN-C and CDN-D subfamilies Benedict et al, 2001;Chen et al, 1995;Davis et al, 1996;Davis and Essenberg, 1995;Meng et al, 1999), and each has variable expression pattern in different tissues (Benedict et al, 2004;Meng et al, 1999;Tan et al, 2000) and can be induced by pathogens (Davila-Huerta et al, 1995;Davis et al, 1996;Liu et al, 1999a) (Figure 1B).…”

Section: (+)--Cadinene Synthase (Cdn)mentioning

confidence: 99%

Gossypol: phytoalexin of cotton

Tian

Ruan

Huang

et al. 2016

Sci. China Life Sci.

View full text Add to dashboard Cite

Sesquiterpenoids are a class of 15-carbon secondary metabolites that play diverse roles in plant adaptation to environment. Cotton plants accumulate a large amount of sesquiterpene aldehydes (including gossypol) as phytoalexins against pathogens and herbivores. They are stored in pigment glands of aerial organs and in epidermal layers of roots. Several enzymes of gossypol biosynthesis pathway have been characterized, including 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMGR) and farnesyl diphosphate synthase (FPS) that catalyze the formation of the precursor farnesyl diphosphate (FPP), (+)--cadinene synthase (CDN) which is the first enzyme committed to gossypol biosynthesis, and the downstream enzymes of CYP706B1 and methyltransferase. Expressions of these genes are tightly regulated during cotton plants development and induced by jasmonate and fungi elicitors. The transcription factor GaWRKY1 has been shown to be involved in gossypol pathway regulation. Recent development of new genomic platforms and methods and releases of diploid and tetraploid cotton genome sequences will greatly facilitate the elucidation of gossypol biosynthetic pathway and its regulation.cotton, secondary metabolism, gossypol, sesquiterpenoid Citation:

show abstract

(+)-δ-Cadinene is a product of sesquiterpene cyclase activity in cotton

Cited by 66 publications

References 62 publications

The Cyclization of Farnesyl Diphosphate and Nerolidyl Diphosphate by a Purified Recombinant δ-Cadinene Synthase

The Cyclization of Farnesyl Diphosphate and Nerolidyl Diphosphate by a Purified Recombinant δ-Cadinene Synthase

Cloning of a cDNA encoding a plasma membrane-associated, uronide binding phosphoprotein with physical properties similar to viral movement proteins.

Gossypol: phytoalexin of cotton

Contact Info

Product

Resources

About