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Literature summary for 4.2.1.137 extracted from

  • Sato, T.; Hoshino, H.; Yoshida, S.; Nakajima, M.; Hoshino, T.
    Bifunctional triterpene/sesquarterpene cyclase: Tetraprenyl-beta-curcumene cyclase is also squalene cyclase in bacillus megaterium (2011), J. Am. Chem. Soc., 133, 17540-17543.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Priestia megaterium

Organism

Organism UniProt Comment Textmining
Priestia megaterium
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information it is demonstrated that a tetraprenyl-beta-curcumene cyclase also cyclizes a tail-to-tail type of linear squalene into a bicyclic triterpenol, 8alpha-hydroxypolypoda-13,17,21-triene Priestia megaterium ?
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Synonyms

Synonyms Comment Organism
tetraprenyl-beta-curcumene cyclase bifunctional enzyme, cyclizing both tetraprenyl-beta-curcumene and squalene in vivo Priestia megaterium

General Information

General Information Comment Organism
metabolism tetraprenyl-beta-curcumene cyclase is bifunctional, cyclizing both tetraprenyl-beta-curcumene and squalene in vivo Priestia megaterium