4.2.3.87: alpha-guaiene synthase
This is an abbreviated version!
For detailed information about alpha-guaiene synthase, go to the full flat file.
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Synonyms
Pat177, patchoulol synthase, PTS, TPS, TPS24, VIT_19s0014g02590, VvGuaS, VvTPS24
ECTree
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General Information on EC 4.2.3.87 - alpha-guaiene synthase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
metabolism
enzyme produces alpha-guaiene, a precursor of rotundone, proposed pathway for (-)-rotundone biosynthesis overview. Analysis of the cultivars Syrah, grown in the Iwaimura and Johnohira vineyards in Japan, reveals that the expression levels of the mevalonate pathway genes, Vixadtis vinifera terpene synthase gene (VvTPS24) and cyxadtochrome P450 gene (CYP71BE5) in the final step of (-)-rotundone biosynthesis are not significantly difxadferent between samples from the two vineyards during grape maturation. In contrast, the farnesyl diphosxadphate synthase gene (FPPS) expression level is conxadsiderably higher in the grape exocarp from the Johnoxadhira vineyard than in that from the Iwaimura vineyard. Relationship between alpha-guaiene and (-)-rotundone accumulation during grape maturation in the grape exocarp, overview
physiological function
the enzyme produces alpha-guaiene, a precursor of rotundone
additional information
additional information
the T414 and V530 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. 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
additional information
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the T414 and V530 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. 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
