Literature summary extracted from

Chen, M.; Al-lami, N.; Janvier, M.; DAntonio, E.L.; Faraldos, J.A.; Cane, D.E.; Allemann, R.K.; Christianson, D.W.
Mechanistic insights from the binding of substrate and carbocation intermediate analogues to aristolochene synthase (2013), Biochemistry, 52, 5441-5453.

Cloned(Commentary)

EC Number	Cloned (Comment)	Organism
4.2.3.9	-	Aspergillus terreus

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
4.2.3.9	X-ray crystal structure of aristolochene synthase complexed with three Mg2+ ions and the unreactive substrate analogue farnesyl-S-thiolodiphosphate, showing that the substrate diphosphate group is anchored by metal coordination and hydrogen bond interactions. The binding conformation of farnesyl-S-thiolodiphosphate directly mimics that expected for productively bound farnesyl diphosphate, with the exception of the precise alignment of the C-S bond with regard to the C10-C11 pi system that would be required for C1-C10 bond formation in the first step of catalysis. Crystal structures of aristolochene synthase complexed with Mg2+3-diphosphate and ammonium or iminium analogues of bicyclic carbocation intermediates proposed for the natural cyclization cascade show various binding orientations for these bicyclic analogues, which appear to be driven by favorable electrostatic interactions between the positively charged ammonium group of the analogue and the negatively charged diphosphate anion. The active site is sufficiently flexible to accommodate analogues with partially or completely incorrect stereochemistry	Aspergillus terreus

Organism

EC Number	Organism	UniProt	Comment	Textmining
4.2.3.9	Aspergillus terreus	Q9UR08	-	-

Synonyms

EC Number	Synonyms	Comment	Organism
4.2.3.9	Ari1	-	Aspergillus terreus

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Release 2023.1 (January 2023)