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Information on EC 4.2.3.9 - aristolochene synthase and Organism(s) Penicillium roqueforti and UniProt Accession Q03471

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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.3 Acting on phosphates
                4.2.3.9 aristolochene synthase
IUBMB Comments
The initial internal cyclization produces the monocyclic intermediate germacrene A; further cyclization and methyl transfer converts the intermediate into aristolochene. While in some species germacrene A remains as an enzyme-bound intermediate, it has been shown to be a minor product of the reaction in Penicillium roqueforti (see also EC 4.2.3.23, germacrene-A synthase). The enzyme from Penicillium roqueforti requires Mg2+. Mn2+ can partially substitute, at low concentrations. Aristolochene is the likely parent compound for a number of sesquiterpenes produced by filamentous fungi.
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Penicillium roqueforti
UNIPROT: Q03471
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The taxonomic range for the selected organisms is: Penicillium roqueforti
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
sesquiterpene cyclase, aristolochene synthase, 5-epi-aristolochene synthase, farnesylpyrophosphate cyclase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aristolochene synthase
-
aristolochene synthase
-
-
cyclase, farnesyl pyrophosphate
-
-
-
-
farnesylpyrophosphate cyclase
-
-
-
-
FPP-carbocyclase
-
-
-
-
sesquiterpene cyclase
-
-
-
-
synthase, aristolochene
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cyclization
internal cyclization
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
(2E,6E)-farnesyl diphosphate diphosphate-lyase (cyclizing, aristolochene-forming)
The initial internal cyclization produces the monocyclic intermediate germacrene A; further cyclization and methyl transfer converts the intermediate into aristolochene. While in some species germacrene A remains as an enzyme-bound intermediate, it has been shown to be a minor product of the reaction in Penicillium roqueforti [5] (see also EC 4.2.3.23, germacrene-A synthase). The enzyme from Penicillium roqueforti requires Mg2+. Mn2+ can partially substitute, at low concentrations. Aristolochene is the likely parent compound for a number of sesquiterpenes produced by filamentous fungi.
CAS REGISTRY NUMBER
COMMENTARY hide
94185-89-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2E,6E)-farnesyl diphosphate
(+)-5-epi-aristolochene + diphosphate
show the reaction diagram
(2E,6E)-farnesyl diphosphate
aristolochene + diphosphate
show the reaction diagram
-
products are 91.5% aristolochene, 7.5% germacrene A, 1% valencene
-
?
2-trans,6-trans-farnesyl diphosphate
aristolochene + diphosphate
show the reaction diagram
trans,trans-farnesyl diphosphate
(+)-aristolochene + diphosphate
show the reaction diagram
-
(+)-aristolochene + minor amounts of (S)-(-)-germacrene A and (-)-valencene in a 94:4:2 ratio
-
?
(2E,6E)-farnesyl diphosphate
(+)-aristolochene + diphosphate
show the reaction diagram
(2E,6E)-farnesyl diphosphate
aristolochene + diphosphate
show the reaction diagram
-
reaction proceeds via germacrene A and eudesmane cation. The amount of germacrene A generated by mutant enzymes serves as a measure of the stabilization of eudesmane cation
wild-type, about 8% of germacrene A as by-product. His-tagged wild-type, about 4% of germacrene A
-
?
14-fluoro (2E,6Z)-farnesyl diphosphate
14-fluorogermacrene A + diphosphate
show the reaction diagram
-
-
-
-
?
2-fluorofarnesyl-diphosphate
2-fluorogermacrene A
show the reaction diagram
-
-
-
-
?
2-trans,6-trans-farnesyl diphosphate
aristolochene + diphosphate
show the reaction diagram
-
-
-
-
?
6-fluoro-(2E,6Z)-farnesyl diphosphate
6-fluorogermacrene A + diphosphate
show the reaction diagram
-
-
one of 3 major products
-
?
7-methylene farnesyl diphosphate
(+)-aristolochene + diphosphate
show the reaction diagram
-
-
-
-
?
farnesyl diphosphate
(+)-aristolochene + diphosphate
show the reaction diagram
trans,trans-farnesyl diphosphate
aristolochene + diphosphate
show the reaction diagram
trans,trans-farnesyl diphosphate
aristolochene + diphosphate + germacrene
show the reaction diagram
-
-
wild-type enzyme produces 92% aristolochene, 8% germacrene and a small amount of valencene
-
?
additional information
?
-
-
reaction is a a cyclisation cascade that leads to the generation of two 6-membered rings, three chiral centres, and two double bonds with high regio- and stereospecificity. Concurrent to diphosphate expulsion enzyme facilitates attack of C1 in farnesyl diphosphate by the C10, C11-double bond to produce germacryl cation. Proton loss from C12 leads to the production of (S)-germacrene A which is then postulated to undergo reprotonation of the C6, C7-double bond and a further cyclisation to form the bicyclic eudesmane cation. Successive 1,2-hydride shift and methyl migration followed by loss of H on C8 completes the generation of (+)-aristolochene
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2-trans,6-trans-farnesyl diphosphate
aristolochene + diphosphate
show the reaction diagram
2-trans,6-trans-farnesyl diphosphate
aristolochene + diphosphate
show the reaction diagram
-
-
-
-
?
farnesyl diphosphate
(+)-aristolochene + diphosphate
show the reaction diagram
-
biogenetic precursor of more than 300 different sesquiterpene hydrocarbon scaffolds in plants, bacteria and fungi
-
-
?
trans,trans-farnesyl diphosphate
aristolochene + diphosphate
show the reaction diagram
-
the enzyme appeears to be transcriptionally regulated
-
-
?
additional information
?
-
-
reaction is a a cyclisation cascade that leads to the generation of two 6-membered rings, three chiral centres, and two double bonds with high regio- and stereospecificity. Concurrent to diphosphate expulsion enzyme facilitates attack of C1 in farnesyl diphosphate by the C10, C11-double bond to produce germacryl cation. Proton loss from C12 leads to the production of (S)-germacrene A which is then postulated to undergo reprotonation of the C6, C7-double bond and a further cyclisation to form the bicyclic eudesmane cation. Successive 1,2-hydride shift and methyl migration followed by loss of H on C8 completes the generation of (+)-aristolochene
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(4aS,7S)-1,4a-dimethyl-7-(prop-1-en-2-yl)-2,3,4,4a,5,6,7,8-octahydroquinolinium iodide
inhibitor mimics transition state associated with the cyclization of (-)-germacrene A to eudesmane cation, competitive
(4aS,7S)-4a-methyl-7-(prop-1-en-2-yl)-2,3,4,4a,5,6,7,8-octahydroquinolinium chloride
inhibitor mimics transition state associated with the cyclization of (-)-germacrene A to eudesmane cation, competitive
3-phenylfarnesyl diphosphate
-
E-11-phenylfarnesyl diphosphate
-
Z-11-phenylfarnesyl diphosphate
-
12,13-difluoro-farnesyl diphosphate
-
-
4-aza-eudesm-11-ene
-
transition state analogue, competitive
additional information
-
no effect: phosphate up to concentrations of 5.0 mM
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00014 - 2.03
(2E,6E)-farnesyl diphosphate
0.000012 - 0.0101
trans,trans-farnesyl diphosphate
0.00013 - 0.001
(2E,6E)-farnesyl diphosphate
0.0008 - 0.0463
farnesyl diphosphate
0.00052 - 0.1887
trans,trans-farnesyl diphosphate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00049 - 0.084
(2E,6E)-farnesyl diphosphate
0.00012 - 0.043
trans,trans-farnesyl diphosphate
0.0003 - 0.084
(2E,6E)-farnesyl diphosphate
0.0014 - 550
farnesyl diphosphate
0.000021 - 0.043
trans,trans-farnesyl diphosphate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0011 - 158.5
(2E,6E)-farnesyl diphosphate
2.56 - 158.5
(2E,6E)-farnesyl diphosphate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.219
(4aS,7S)-1,4a-dimethyl-7-(prop-1-en-2-yl)-2,3,4,4a,5,6,7,8-octahydroquinolinium iodide
pH not specified in the publication, temperature not specified in the publication
0.0284
(4aS,7S)-4a-methyl-7-(prop-1-en-2-yl)-2,3,4,4a,5,6,7,8-octahydroquinolinium chloride
pH not specified in the publication, temperature not specified in the publication
0.0012
3-phenylfarnesyl diphosphate
-
0.0008
E-11-phenylfarnesyl diphosphate
-
0.0012
Z-11-phenylfarnesyl diphosphate
-
0.00024 - 0.00035
4-aza-eudesm-11-ene, ammonium salt
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
activity assay
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
activity assay
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PRX2_PENRO
342
0
39192
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37000
-
1 * 37000, SDS-PAGE
39000
-
39000, calculated
39200
-
x * 39200, calculation from nucleotide sequence
48000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
2.5-A resolution crystal structure of recombinant enzyme, hanging drop method
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D115E
kcat/KM is 12fold lower than wild-type value. Wild-type enzyme produces (+)-aristolochene, (-)-valencene and (S)-(-)-germacrene A in the ratio 93:2:4, the ratio of the mutant enzyme is 75:6:119
D115N
inactive mutant enzyme
D116E
kcat/KM is 60fold lower than wild-type value. Wild-type enzyme produces (+)-aristolochene, (-)-valencene and (S)-(-)-germacrene A in the ratio 93:2:4, the ratio of the mutant enzyme is 62:3:35
D116N
kcat/KM is 48fold lower than wild-type value. Wild-type enzyme produces (+)-aristolochene, (-)-valencene and (S)-(-)-germacrene A in the ratio 93:2:4, the ratio of the mutant enzyme is 63:2:35
D203L
approximately 150fold decrease in kcat/KM
E119D
kcat/KM is 2.4fold lower than wild-type value. Wild-type enzyme produces (+)-aristolochene, (-)-valencene and (S)-(-)-germacrene A in the ratio 93:2:4, the ratio of the mutant enzyme is 94:2:4
E119Q
kcat/KM is 2.3fold lower than wild-type value. Wild-type enzyme produces (+)-aristolochene, (-)-valencene and (S)-(-)-germacrene A in the ratio 93:2:4, the ratio of the mutant enzyme is 84:2:14
E252D
kcat/KM is 111fold lower than wild-type value. Wild-type enzyme produces (+)-aristolochene, (-)-valencene and (S)-(-)-germacrene A in the ratio 93:2:4, the ratio of the mutant enzyme is 19:0:81
E252Q
mutant enzyme produces only (-)-germacrene A
K251Q
20fold reduction in catalytic efficiency
K251R
6fold reduction in catalytic efficiency
L108A
products are 6.8% aristolochene, 13.9% germacrene A, 26.9% (E)-beta-farnesene, 48.2%(E,E)-alpha-farnesene and 4.1% (E,Z)-alpha-farnesene
L108F
products are 74.1% aristolochene, 13.8% germacrene A, 12% valencene
L108S
products are 9.4% aristolochene, 14.6% germacrene A, 21.5% (E)-beta-farnesene, 49.1% (E,E)-alpha-farnesene and 5.3% (E,Z)-alpha-farnesene
L108V
products are 88.3% aristolochene, 8% germacrene A, 1% valencene, and 2.3% (E,Z)-alpha-farnesene
N244D
kcat/KM is 1978fold lower than wild-type value. Wild-type enzyme produces (+)-aristolochene, (-)-valencene and (S)-(-)-germacrene A in the ratio 93:2:4, the ratio of the mutant enzyme is 19:0:81
N244L
inactive mutant enzyme
R200K
approximately 300fold decrease in kcat/KM, mutant produces significantly increased amounts of germacrene A
R340K
approximately 300fold decrease in kcat/KM, mutant produces significantly increased amounts of germacrene A
S248A
kcat/KM is 300fold lower than wild-type value. Wild-type enzyme produces (+)-aristolochene, (-)-valencene and (S)-(-)-germacrene A in the ratio 93:2:4, the ratio of the mutant enzyme is 21:0:79
S248A/E252D
inactive mutant enzyme
T89A
products are 93.4% aristolochene, 4.4% germacrene A, 2.2% valencene
T89F
products are 67.6% aristolochene, 27.2% germacrene A, 5.2% valencene
V88A
products are 86.2% aristolochene, 11.6% germacrene A, 2.2% valencene
V88F
products are 18.4% aristolochene, 57.8% germacrene A, 23.8% valencene
Y341F
10fold reduction in catalytic efficiency
Y92A
reduction of the size of the side chain of residue 92 leads to the production of the alicyclic sesquiterpenes (E)-beta- and (E,E)-alpha-farnesene. The relative amounts of linear products formed depend linearly on the size of the residues at position 92. ASY92A produces almost 80% of alicyclic sesquiterpenes and no aristolochene
Y92C
reduction of the size of the side chain of residue 92 leads to the production of the alicyclic sesquiterpenes (E)-beta- and (E,E)-alpha-farnesene. Mutant ASY92C still produces about 6.8% of aristolochene
Y92V
reduction of the size of the side chain of residue 92 leads to the production of the alicyclic sesquiterpenes (E)-beta- and (E,E)-alpha-farnesene
F112A
F112A/F178A
-
mutant is constructed to confirm the proposed roles of both F178 and F112
F178C
-
mutant is constructed to distinguish between the importance of size and aromaticity residue 178
F178I
-
mutant is constructed to distinguish between the importance of size and aromaticity residue 178
F178V
F178W
-
mutant is constructed to distinguish between the importance of size and aromaticity residue 178
F178Y
W334F
-
ratio of products: 82% aristolochene, 18% germacrene A
W334H
-
ratio of products: 10% aristolochene, 90% germacrene A
W334L
-
ratio of products: 2% aristolochene, 98% germacrene A
W334Y
-
ratio of products: 62% aristolochene, 38% germacrene A
Y92A
turnover number is approximately 2 orders of magnitude lower than the value observed for the wild-type enzyme,the mutant enzyme produces almost 80% of the alicyclic sesquiterpenes (E)-beta-farnesene and (E,E)-alpha-farnesene. The mutant also produces small amounts of additional hydrocarbons with a molecular weight of 204: alpha-selinene, beta-selinene, selina-4,11-diene, (E,Z)-alpha-farnesene, and beta-bisabolene. Km-value for trans, trans-farnesyl diphosphate is 0.0834 mM compared to 0.0023 mM for the wild-type enzyme
Y92C
turnover number is approximately 2 orders of magnitude lower than the value observed for the wild-type enzyme. Km-value for trans, trans-farnesyl diphosphate is 0.05027 mM compared to 0.0023 mM for the wild-type enzyme
Y92F
-
the mutant enzyme is approximately 0.1% as active as the nonmutated recombinant enzyme, the mutant releases significant amounts of germacrene A and also produces various amounts of a further five hydrocarbons of molecular weight 204, valencene, beta-(E)-farnesene, alpha-selinene, beta-selinene and selina-4,11-diene. The CD spectrum of the mutant enzyme is very similar to that of the wild-type enzyme
Y92V
-
the mutant produces the alicyclic beta-(E)-farnesene as the major product
additional information
-
the replacement of Trp 334 with para-substituted phenylalanines of increasing electron-withdrawing properties leads to a progressive accumulation of germacrene A that shows a good correlation with the interaction energies of simple cations such as Na+ with substituted benzenes. Evidence for the stabilizing role played by Trp334 in aristolochene synthase catalysis for the energetically demanding transformation of germacrene A to eudesmane cation. Replacement of tryptophan by para-substituted phenylalanines with strong electron-withdrawing substituents has only minor effects on the KM values of the reaction but leads to approximately 30fold decreases of kcat relative to mutant W334F. Noncanonical substitutions lead to the following ratios of products: W334naphthyl 78% aristolochene, 22% germacrene A, W334-p-chlorophenylalanine or W334-p-fluorophenylalanine 57% aristolochene, 43% germacrene A, W334-p-trifluoromethylphenylalanine 31% aristolochene, 69% germacrene A, W334-p-nitrophenylalanine 23% aristolochene, 77% germacrene A
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
mutant enzyme Y92C and Y92A
Proteins are extracted from the inclusion bodies and purified following established protocols, each enzyme is pure as judged by SDS-gel electrophoresis
-
recombinant enzyme
-
wild-type and mutant enzymes
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3)
-
expression of AS and AS-F112A in Escherichia coli
-
expression of the fusion protein proteinA/aristolochene synthase in Escherichia coli
-
for expression in Escherichia coli BL21DE3 cells
-
mutant enzymes Y92C and Y92A
wild-type and mutant enzyme Y92F, expression in Escherichia coli
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
extracted from inclusion bodies
-
protein is extracted from inclusion bodies
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hohn, T.M.; Plattner, R.D.
Purification and characterization of the sesquiterpene cyclase aristolochene synthase from Penicillium roqueforti
Arch. Biochem. Biophys.
272
137-143
1989
Penicillium roqueforti
Manually annotated by BRENDA team
Proctor, R.H.; Hohn, T.M.
Aristolochene synthase. Isolation, characterization, and bacterial expression of a sesquiterpenoid biosynthetic gene (Ari1) from Penicillium roqueforti
J. Biol. Chem.
268
4543-4548
1993
Penicillium roqueforti
Manually annotated by BRENDA team
Caruthers, J.M.; Kang, I.; Rynkiewicz, M.J.; Cane, D.E.; Christianson, D.W.
Crystal structure determination of aristolochene synthase from the blue cheese mold, Penicillium roqueforti
J. Biol. Chem.
275
25533-25539
2000
Penicillium roqueforti
Manually annotated by BRENDA team
Calvert, M.J.; Taylor, S.E.; Allemann, R.K.
Tyrosine 92 of aristolochene synthase directs cyclisation of farnesyl pyrophosphate
Chem. Commun. (Camb.)
2002
2384-2385
2002
Penicillium roqueforti
-
Manually annotated by BRENDA team
Calvert, M.J.; Ashton, P.R.; Allemann, R.K.
Germacrene A is a product of the aristolochene synthase-mediated conversion of farnesylpyrophosphate to aristolochene
J. Am. Chem. Soc.
124
11636-11641
2002
Penicillium roqueforti
Manually annotated by BRENDA team
Deligeorgopoulou, A.; Allemann, R.K.
Evidence for differential folding of farnesyl pyrophosphate in the active site of aristolochene synthase: a single-point mutation converts aristolochene synthase into an (E)-b-farnesene synthase
Biochemistry
42
7741-7747
2003
Penicillium roqueforti, Penicillium roqueforti (Q03471)
Manually annotated by BRENDA team
Cane, D.E.; Kang, I.
Aristolochene synthase: purification, molecular cloning, high-level expression in Escherichia coli, and characterization of the Aspergillus terreus cyclase
Arch. Biochem. Biophys.
376
354-364
2000
Aspergillus terreus, Penicillium roqueforti
Manually annotated by BRENDA team
Forcat, S.; Allemann, R.K.
Dual role for phenylalanine 178 during catalysis by aristolochene synthase
Chem. Commun. (Camb.)
2004
2094-2095
2004
Penicillium roqueforti
Manually annotated by BRENDA team
Felicetti, B.; Cane, D.E.
Aristolochene synthase: mechanistic analysis of active site residues by site-directed mutagenesis
J. Am. Chem. Soc.
126
7212-7221
2004
Aspergillus terreus, Penicillium roqueforti (Q03471), Penicillium roqueforti
Manually annotated by BRENDA team
Miller, D.J.; Yu, F.; Allemann, R.K.
Aristolochene synthase-catalyzed cyclization of 2-fluorofarnesyl-diphosphate to 2-fluorogermacrene A
ChemBioChem
8
1819-1825
2007
Penicillium roqueforti
Manually annotated by BRENDA team
Allemann, R.K.; Young, N.J.; Ma, S.; Truhlar, D.G.; Gao, J.
Synthetic efficiency in enzyme mechanisms involving carbocations: aristolochene synthase
J. Am. Chem. Soc.
129
13008-13013
2007
Penicillium roqueforti (Q03471)
Manually annotated by BRENDA team
Forcat, S.; Allemann, R.K.
Stabilisation of transition states prior to and following eudesmane cation in aristolochene synthase
Org. Biomol. Chem.
4
2563-2567
2006
Penicillium roqueforti
Manually annotated by BRENDA team
Miller, D.J.; Yu, F.; Young, N.J.; Allemann, R.K.
Competitive inhibition of aristolochene synthase by phenyl-substituted farnesyl diphosphates: evidence of active site plasticity
Org. Biomol. Chem.
5
3287-3298
2007
Penicillium roqueforti (Q03471), Penicillium roqueforti
Manually annotated by BRENDA team
Miller, D.J.; Gao, J.; Truhlar, D.G.; Young, N.J.; Gonzalez, V.; Allemann, R.K.
Stereochemistry of eudesmane cation formation during catalysis by aristolochene synthase from Penicillium roqueforti
Org. Biomol. Chem.
6
2346-2354
2008
Penicillium roqueforti
Manually annotated by BRENDA team
Faraldos, J.A.; Kariuki, B.; Allemann, R.K.
Intermediacy of eudesmane cation during catalysis by aristolochene synthase
J. Org. Chem.
75
1119-1125
2010
Penicillium roqueforti
Manually annotated by BRENDA team
Miller, D.J.; Yu, F.; Knight, D.W.; Allemann, R.K.
6- and 14-Fluoro farnesyl diphosphate: mechanistic probes for the reaction catalysed by aristolochene synthase
Org. Biomol. Chem.
7
962-975
2009
Penicillium roqueforti
Manually annotated by BRENDA team
Faraldos, J.A.; Antonczak, A.K.; Gonzalez, V.; Fullerton, R.; Tippmann, E.M.; Allemann, R.K.
Probing eudesmane cation-pi interactions in catalysis by aristolochene synthase with non-canonical amino acids
J. Am. Chem. Soc.
133
13906-13909
2011
Penicillium roqueforti
Manually annotated by BRENDA team
Faraldos, J.A.; Gonzalez, V.; Senske, M.; Allemann, R.K.
Templating effects in aristolochene synthase catalysis: elimination versus cyclisation
Org. Biomol. Chem.
9
6920-6923
2011
Penicillium roqueforti (Q03471), Penicillium roqueforti
Manually annotated by BRENDA team
Faraldos, J.A.; Allemann, R.K.
Inhibition of (+)-aristolochene synthase with iminium salts resembling eudesmane cation
Org. Lett.
13
1202-1205
2011
Penicillium roqueforti (Q03471)
Manually annotated by BRENDA team
Faraldos, J.A.; Gonzalez, V.; Allemann, R.K.
The role of aristolochene synthase in diphosphate activation
Chem. Commun. (Camb. )
48
3230-3232
2012
Penicillium roqueforti (Q03471), Penicillium roqueforti
Manually annotated by BRENDA team
Faraldos, J.A.; Grundy, D.J.; Cascon, O.; Leoni, S.; van der Kamp, M.W.; Allemann, R.K.
Enzymatic synthesis of natural (+)-aristolochene from a non-natural substrate
Chem. Commun. (Camb.)
52
14027-14030
2016
Penicillium roqueforti
Manually annotated by BRENDA team