Literature summary for 4.2.3.108 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.

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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 residues 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	O81191	-	-

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Release 2023.1 (January 2023)