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BRENDA support

Literature summary for 4.2.3.110 extracted from

  • Peters, R.J.; Croteau, R.B.
    Alternative termination chemistries utilized by monoterpene cyclases: chimeric analysis of bornyl diphosphate, 1,8-cineole, and sabinene synthases (2003), Arch. Biochem. Biophys., 417, 203-211.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Salvia officinalis

Protein Variants

Protein Variants Comment Organism
additional information exchange of sequences corresponding by homology to the C-terminal domain including the domain spanning alpha-helix, between sabinene synthase and both bornyl diphosphate synthase and cineole synthase. Exchange of tresidues 304–377 from cineole synthase into sabinene synthase is sufficient to impart the alternative termination chemistry involving water capture to alpha-terpineol and cyclization to 1,8-cineole Salvia officinalis

Organism

Organism UniProt Comment Textmining
Salvia officinalis O81193
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