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Literature summary for 2.5.1.69 extracted from

  • Thulasiram, H.V.; Erickson, H.K.; Poulter, C.D.
    A common mechanism for branching, cyclopropanation, and cyclobutanation reactions in the isoprenoid biosynthetic pathway (2008), J. Am. Chem. Soc., 130, 1966-1971.
    View publication on PubMed
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Protein Variants

Protein Variants Comment Organism
additional information chimera c98f, constructed by replacing the first 98 residues in Artemisia tridentata ssp. spiciformis farnesyl diphosphate synthase with the corresponding sequence from Artemisia tridentata chrysanthemyl diphosphate synthase is able to produce a 6:5 mixture of (R)-lavandulol and (R)-maconelliol and a small amount of planococcyl alcohol in presence of alkaline phosphatase. Chimeric proteins constructed from farnesyl diphosphate synthase, which catalyzes chain elongation, and chrysanthemyl diphosphate synthase, which catalyzes cyclopropanation, catalyze all four of the known isoprenoid coupling reactions to give a mixture of geranyl diphosphate by chain elongation, chrysanthemyl diphosphate by cyclopropanation, lavandulyl diphosphate by branching, and maconelliyl and planococcyl diphosphate by cyclobutanation Artemisia tridentata

Organism

Organism UniProt Comment Textmining
Artemisia tridentata
-
 ssp. spiciformis
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 dimethylallyl diphosphate
-
 Artemisia tridentata (R)-lavandulol + (R)-maconelliol + diphosphate in presence of alkaline phosphatase, chimera c98f produces a 6:5 mixture of (R)-lavandulol and (R)-maconelliol and a small amount of planococcyl alcohol ?