Literature summary for 4.2.3.9 extracted from

Shishova, E.Y.; Yu, F.; Miller, D.J.; Faraldos, J.A.; Zhao, Y.; Coates, R.M.; Allemann, R.K.; Cane, D.E.; Christianson, D.W.
X-ray crystallographic studies of substrate binding to aristolochene synthase suggest a metal ion binding sequence for catalysis (2008), J. Biol. Chem., 283, 15431-15439.

Cloned(Commentary)

Cloned (Comment)	Organism
recombinant aristolochene synthase is expressed in Escherichia coli BL21(DE3)pLysS	Aspergillus terreus

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystallization by the hanging drop, vapor diffusion method at 4°C, the crystal structure determined from crystals soaked with farnesyl diphosphate reveals the binding of intact farnesyl diphosphate to monomers A-C, and the binding of diphosphate anion and Mg2+ to monomer D. The structure of the complex with 2-fluorofarnesyl diphosphate reveals 2-fluorofarnesyl diphosphate binding to all subunits of the tetramer, with Mg2+B accompanying the binding of this analogue only in monomer D. The structure of the complex with 12,13-difluorofarnesyl diphosphate reveals the binding of intact 12,13-difluorofarnesyl diphosphate to monomers A-C in the open conformation and the binding of diphosphate anion, Mg2+B, and Mg2+C to monomer D in a predominantly closed conformation	Aspergillus terreus

Crystallization (Comment)

Organism

crystallization by the hanging drop, vapor diffusion method at 4°C, the crystal structure determined from crystals soaked with farnesyl diphosphate reveals the binding of intact farnesyl diphosphate to monomers A-C, and the binding of diphosphate anion and Mg2+ to monomer D. The structure of the complex with 2-fluorofarnesyl diphosphate reveals 2-fluorofarnesyl diphosphate binding to all subunits of the tetramer, with Mg2+B accompanying the binding of this analogue only in monomer D. The structure of the complex with 12,13-difluorofarnesyl diphosphate reveals the binding of intact 12,13-difluorofarnesyl diphosphate to monomers A-C in the open conformation and the binding of diphosphate anion, Mg2+B, and Mg2+C to monomer D in a predominantly closed conformation

Aspergillus terreus

Inhibitors

Inhibitors	Comment	Organism	Structure
12,13-difluorofarnesyl diphosphate	incubation of 12,13-difluorofarnesyl diphosphate with for 30 h does not generate any pentane-extractable products based on GC-MS analysis	Aspergillus terreus

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	enzyme utilizes a trinuclear magnesium cluster to trigger the departure of the diphosphate leaving group, thereby forming an allylic carbocation that typically reacts with one of the remaining sigma-bonds of the substrate	Aspergillus terreus

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
farnesyl diphosphate	Aspergillus terreus	The universal sesquiterpene precursor farnesyl diphosphate (15-carbon isoprenoid) is cyclized in an Mg2-dependent reaction to form the bicyclic hydrocarbon aristolochene and a diphosphate anion coproduct	(+)-aristolochene + diphosphate	-	?

Organism

Organism	UniProt	Comment	Textmining
Aspergillus terreus	Q9UR08	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Aspergillus terreus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2-fluorofarnesyl diphosphate	two products are identified in a 95/5 ratio by GS-MS	Aspergillus terreus	2-fluorogermacrene A + diphosphate	-	?
farnesyl diphosphate	The universal sesquiterpene precursor farnesyl diphosphate (15-carbon isoprenoid) is cyclized in an Mg2-dependent reaction to form the bicyclic hydrocarbon aristolochene and a diphosphate anion coproduct	Aspergillus terreus	(+)-aristolochene + diphosphate	-	?

Subunits

Subunits	Comment	Organism
dimer	in solution	Aspergillus terreus
tetramer	crystal structure	Aspergillus terreus

Synonyms

Synonyms	Comment	Organism
aristolochene synthase	sesquiterpene cyclase	Aspergillus terreus

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
30	-	assay at	Aspergillus terreus

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.6	-	assay at	Aspergillus terreus