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Literature summary for 4.2.3.86 extracted from

  • Drew, D.P.; Andersen, T.B.; Sweetman, C.; M?ller, B.L.; Ford, C.; Simonsen, H.T.
    Two key polymorphisms in a newly discovered allele of the Vitis vinifera TPS24 gene are responsible for the production of the rotundone precursor ?-guaiene (2016), J. Exp. Bot., 67, 799-808 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.2.3.86

Cloned(Commentary)

Cloned (Comment) Organism
construction of the synthetic terpene synthase construct from the sequence of alpga-guaiene synthase (EC 4.2.3.87), sequence comparisons and phylogenetic analysis, the recombinant enzyme is transiently expressed in Nicotiana benthamiana leaves and produces mainly alpha-guaiene and alpha-bulnesene, and also lower amounts of alpha-copaene, alpha-gurjunene, gamm-gurlunene, epiglobulol, epi-?alpha-selinene, and pogostol. Selina-4(14),11-diene, alpha-selinene, delta-cadinene, and intermedeol are not found Vitis vinifera

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(2E,6E)-farnesyl diphosphate Vitis vinifera
-
 alpha-guaiene + diphosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Vitis vinifera AM459143 cv. Shiraz, grown in the Nuriootpa Research vineyard, Barossa Valley, South Australia, and harvested at various times of the 2013 season
-

Source Tissue

Source Tissue Comment Organism Textmining
fruit
-
 Vitis vinifera
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(2E,6E)-farnesyl diphosphate
-
 Vitis vinifera alpha-guaiene + diphosphate
-
 ?
additional information substrate analysis of wild-type and mutant enzymes compared to alpha-guaiene synthase, EC 4.2.3.87 Vitis vinifera ?
-
 ?

Synonyms

Synonyms Comment Organism
selinene synthase
-
 Vitis vinifera
VvPNSeInt
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 Vitis vinifera

General Information

General Information Comment Organism
additional information molecular modelling of the two enzymes, selinene synthase (EC 4.2.3.86) and alpha-guayene synthase (EC 4.2.3.87) based on the TEAS template structure reveals that two of the varying amino acid positions are directly located in the active site, proximal to the location of FPP binding and subsequent catalysis, while the other four amino acid differences are located more peripherally, structure-function analysis. The S414 and M530 residues both contribute to the internal binding site of farnesyl diphosphate and are located on separate alpha-helices that contribute to the formation of the internal cavity comprising the FPP substrate-binding site Vitis vinifera
physiological function the enzyme produces alpha-guaiene, a precursor of rotundone Vitis vinifera