Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

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

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.2.3.9 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

EC Number Inhibitors Comment Organism Structure
4.2.3.9 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

EC Number Metals/Ions Comment Organism Structure
4.2.3.9 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)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.3.9 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

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

Purification (Commentary)

EC Number Purification (Comment) Organism
4.2.3.9
-
 Aspergillus terreus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.3.9 2-fluorofarnesyl diphosphate two products are identified in a 95/5 ratio by GS-MS Aspergillus terreus 2-fluorogermacrene A + diphosphate
-
 ?
4.2.3.9 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

EC Number Subunits Comment Organism
4.2.3.9 dimer in solution Aspergillus terreus
4.2.3.9 tetramer crystal structure Aspergillus terreus

Synonyms

EC Number Synonyms Comment Organism
4.2.3.9 aristolochene synthase sesquiterpene cyclase Aspergillus terreus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.2.3.9 30
-
 assay at Aspergillus terreus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.2.3.9 7.6
-
 assay at Aspergillus terreus