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Literature summary for 5.5.1.8 extracted from

  • Whittington, D.A.; Wise, M.L.; Urbansky, M.; Coates, R.M.; Croteau, R.B.; Christianson, D.W.
    Bornyl diphosphate synthase: structure and strategy for carbocation manipulation by a terpenoid cyclase (2002), Proc. Natl. Acad. Sci. USA, 99, 15375-15380.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging-drop vapor-diffusion method, structure of complexes with aza analogues of substrate and carbocation intermediates, as well as complexes with diphosphate and bornyl diphosphate, determined at 2.0 A resolution Salvia officinalis

Organism

Organism UniProt Comment Textmining
Salvia officinalis O81192
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the C-terminal domain catalyzes the cyclization of geranyl diphosphate, orienting and stabilizing multiple reactive carbocation intermediates. The N-terminal domain has no clearly defined function, although its N-terminus caps the active site in the C-terminal domain during catalysis Salvia officinalis ?
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Subunits

Subunits Comment Organism
dimer each monomer contains two alpha-helical domains Salvia officinalis