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(2E,6E)-farnesyl diphosphate
(+)-5-epi-aristolochene + diphosphate
(2E,6E)-farnesyl diphosphate
(+)-5-epiaristolochene + diphosphate
-
-
in addition to the major products (+)-5-epiaristolochene (78.9%), its DELTA1(10) isomer (-)-4-epieremophilene (6.2%), and (R)-germacrene A (3.7%), incubations of (2Z,6E)-farnesyl diphosphate with the enzyme lead to 22 additional sesquiterpenes (11% of total products), among the identified minor products are (-)-R-cedrene, an isomer of (-)-prezizaene and an acoradiene (together accounting for 2.5% of the total hydrocarbon fraction)
-
?
(2E,6E)-farnesyl diphosphate
(+)-aristolochene + diphosphate
(2E,6E)-farnesyl diphosphate
aristolochene + diphosphate
(2Z,6E)-farnesyl diphosphate
(+)-2-epiprezizaene + (-)-alpha-cedrene + (-)-beta-curcumene + alpha-acoradiene + 4-epi-alpha-acoradiene + alpha-bisabolol + epi-alpha-bisabolol + nerolidol + (2Z,6E)-farnesol + diphosphate
-
-
(+)-2-epiprezizaene (44% yield), (-)-alpha-cedrene (21.5% yield), (-)-beta-curcumene (15.5% yield), alpha-acoradiene (3.9% yield), 4-epi-alpha-acoradiene (1.3% yield), alpha-bisabolol (1.8% yield), epi-alpha-bisabolol (1.8% yield), nerolidol (3.6% yield), (2Z,6E)-farnesol (6.7% yield)
-
?
14-fluoro (2E,6Z)-farnesyl diphosphate
14-fluorogermacrene A + diphosphate
-
-
-
-
?
2-fluorofarnesyl diphosphate
2-fluorogermacrene A + diphosphate
2-fluorofarnesyl-diphosphate
2-fluorogermacrene A
-
-
-
-
?
2-trans,6-trans-farnesyl diphosphate
aristolochene + diphosphate
6-fluoro-(2E,6Z)-farnesyl diphosphate
6-fluorogermacrene A + diphosphate
-
-
one of 3 major products
-
?
7-methylene farnesyl diphosphate
(+)-aristolochene + diphosphate
-
-
-
-
?
anilinogeranyl diphosphate
(4E,8E)-4,8-dimethyl-2-azabicyclo[9.2.2]pentadeca-1(13),4,8,11,14-pentaene + diphosphate
-
-
-
?
farnesyl diphosphate
(+)-aristolochene + diphosphate
trans,trans-farnesyl diphosphate
(+)-aristolochene + diphosphate
trans,trans-farnesyl diphosphate
aristolochene + diphosphate
trans,trans-farnesyl diphosphate
aristolochene + diphosphate + germacrene
-
-
wild-type enzyme produces 92% aristolochene, 8% germacrene and a small amount of valencene
-
?
additional information
?
-
(2E,6E)-farnesyl diphosphate
(+)-5-epi-aristolochene + diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate
(+)-5-epi-aristolochene + diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate
(+)-5-epi-aristolochene + diphosphate
-
the steric bulk of residue 92 is central in binding of farnesyl diphosphate to the active site of aristolochene synthase in a quasi-cyclic conformation, thereby facilitating attack of C1 by the C10-C11 double bond to produce the cis-fused decalin S-germacrene A. 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
-
?
(2E,6E)-farnesyl diphosphate
(+)-aristolochene + diphosphate
-
-
-
-
?
(2E,6E)-farnesyl diphosphate
(+)-aristolochene + diphosphate
-
-
major product (92%)
-
?
(2E,6E)-farnesyl diphosphate
aristolochene + diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate
aristolochene + diphosphate
-
products are 91.5% aristolochene, 7.5% germacrene A, 1% valencene
-
?
(2E,6E)-farnesyl diphosphate
aristolochene + diphosphate
-
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
-
?
2-fluorofarnesyl diphosphate
2-fluorogermacrene A + diphosphate
-
-
-
-
?
2-fluorofarnesyl diphosphate
2-fluorogermacrene A + diphosphate
two products are identified in a 95/5 ratio by GS-MS
-
-
?
2-trans,6-trans-farnesyl diphosphate
aristolochene + diphosphate
-
-
-
?
2-trans,6-trans-farnesyl diphosphate
aristolochene + diphosphate
-
terpenoid biosynthesis
-
-
r
2-trans,6-trans-farnesyl diphosphate
aristolochene + diphosphate
-
-
-
-
?
2-trans,6-trans-farnesyl diphosphate
aristolochene + diphosphate
-
-
-
-
?
2-trans,6-trans-farnesyl diphosphate
aristolochene + diphosphate
-
-
-
?
2-trans,6-trans-farnesyl diphosphate
aristolochene + diphosphate
-
-
-
-
?
farnesyl diphosphate
(+)-aristolochene + 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
-
-
?
farnesyl diphosphate
(+)-aristolochene + diphosphate
-
-
-
-
?
farnesyl diphosphate
(+)-aristolochene + diphosphate
-
-
-
-
?
farnesyl diphosphate
(+)-aristolochene + diphosphate
-
biogenetic precursor of more than 300 different sesquiterpene hydrocarbon scaffolds in plants, bacteria and fungi
-
-
?
trans,trans-farnesyl diphosphate
(+)-aristolochene + diphosphate
-
-
(+)-aristolochene is the only product
-
?
trans,trans-farnesyl diphosphate
(+)-aristolochene + diphosphate
-
(+)-aristolochene + minor amounts of (S)-(-)-germacrene A and (-)-valencene in a 94:4:2 ratio
-
?
trans,trans-farnesyl diphosphate
aristolochene + diphosphate
-
-
-
?
trans,trans-farnesyl diphosphate
aristolochene + diphosphate
-
cyclization of trans,trans-farnesyl diphosphate is proceeding with inversion of configuration at C-1 of farnesyl diphosphate
-
?
trans,trans-farnesyl diphosphate
aristolochene + diphosphate
-
H8si is lost in the formation of the 9,10-double bond of aristolochene
-
?
trans,trans-farnesyl diphosphate
aristolochene + diphosphate
-
-
-
?
trans,trans-farnesyl diphosphate
aristolochene + diphosphate
-
-
-
?
trans,trans-farnesyl diphosphate
aristolochene + diphosphate
-
-
-
?
trans,trans-farnesyl diphosphate
aristolochene + diphosphate
-
-
-
?
trans,trans-farnesyl diphosphate
aristolochene + diphosphate
-
-
7.5% of the total amount of products are released from wild-type aristolochene synthase. The mutant enzyme Y92F 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
?
trans,trans-farnesyl diphosphate
aristolochene + diphosphate
-
metal-triggered carbocation formation initiates the cyclization cascade, which procedes through multiple complex intermediates to yield one exclusive structural stereochemical isomer of aristolochene
-
?
trans,trans-farnesyl diphosphate
aristolochene + diphosphate
the steric bulk of residue 92 is central in binding of farnesyl diphosphate to the active site of the enzyme in a quasi-cyclic conformation, thereby facilitating attack of C1 by the C10-C11 double bond to produce the cis-fused decalin S-germacrene A. The cyclization of farnesyl diphosphate to germacrene A in aristolochene synthase proceeds in a stepwise fashion through farnesyl cation
the mutant Y92A 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
?
trans,trans-farnesyl diphosphate
aristolochene + diphosphate
-
the enzyme appeears to be transcriptionally regulated
-
-
?
additional information
?
-
no activity with farnesyl S-thiolodiphosphate
-
-
?
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
-
-
?
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(2E,6E)-farnesyl diphosphate
(+)-5-epi-aristolochene + diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate
aristolochene + diphosphate
-
-
-
?
2-trans,6-trans-farnesyl diphosphate
aristolochene + diphosphate
farnesyl diphosphate
(+)-aristolochene + diphosphate
trans,trans-farnesyl diphosphate
aristolochene + diphosphate
-
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
-
-
?
2-trans,6-trans-farnesyl diphosphate
aristolochene + diphosphate
-
-
-
?
2-trans,6-trans-farnesyl diphosphate
aristolochene + diphosphate
-
terpenoid biosynthesis
-
-
r
2-trans,6-trans-farnesyl diphosphate
aristolochene + diphosphate
-
-
-
-
?
2-trans,6-trans-farnesyl diphosphate
aristolochene + diphosphate
-
-
-
-
?
2-trans,6-trans-farnesyl diphosphate
aristolochene + diphosphate
-
-
-
?
2-trans,6-trans-farnesyl diphosphate
aristolochene + diphosphate
-
-
-
-
?
farnesyl diphosphate
(+)-aristolochene + 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
-
-
?
farnesyl diphosphate
(+)-aristolochene + diphosphate
-
biogenetic precursor of more than 300 different sesquiterpene hydrocarbon scaffolds in plants, bacteria and fungi
-
-
?
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0.000042 - 2.03
(2E,6E)-farnesyl diphosphate
0.0143
(2Z,6E)-farnesyl diphosphate
-
in 200 mM Tris-HCl (pH 7.5), 40 mM MgCl2, at 22°C
0.0082
anilinogeranyl diphosphate
at pH 7.5 and 37°C
0.0008 - 0.0463
farnesyl diphosphate
0.000012 - 0.1887
trans,trans-farnesyl diphosphate
0.000042
(2E,6E)-farnesyl diphosphate
mutant enzyme Q151H, at pH 8.0 and 30°C
0.000061
(2E,6E)-farnesyl diphosphate
mutant enzyme S303H, at pH 8.0 and 30°C
0.000099
(2E,6E)-farnesyl diphosphate
wild type enzyme, at pH 8.0 and 30°C
0.0001
(2E,6E)-farnesyl diphosphate
mutant enzyme Q151E, at pH 8.0 and 30°C
0.00012
(2E,6E)-farnesyl diphosphate
mutant enzyme S303A, at pH 8.0 and 30°C
0.00013
(2E,6E)-farnesyl diphosphate
-
mutant W334H, pH not specified in the publication, temperature not specified in the publication
0.00014
(2E,6E)-farnesyl diphosphate
mutant K251R, pH not specified in the publication, temperature not specified in the publication
0.00018
(2E,6E)-farnesyl diphosphate
mutant Y341F, pH not specified in the publication, temperature not specified in the publication
0.00024
(2E,6E)-farnesyl diphosphate
mutant K251Q, pH not specified in the publication, temperature not specified in the publication
0.00028
(2E,6E)-farnesyl diphosphate
-
mutant W334F, pH not specified in the publication, temperature not specified in the publication
0.00036
(2E,6E)-farnesyl diphosphate
mutant enzyme S303D, at pH 8.0 and 30°C
0.00041
(2E,6E)-farnesyl diphosphate
mutant enzyme N299A, at pH 8.0 and 30°C
0.00041
(2E,6E)-farnesyl diphosphate
mutant enzyme N299A/S303A, at pH 8.0 and 30°C
0.00053
(2E,6E)-farnesyl diphosphate
-
-
0.00053
(2E,6E)-farnesyl diphosphate
-
wild-type, pH not specified in the publication, temperature not specified in the publication
0.00053
(2E,6E)-farnesyl diphosphate
wild-type, pH not specified in the publication, temperature not specified in the publication
0.00053
(2E,6E)-farnesyl diphosphate
-
wild-type, pH not specified in the publication, temperature not specified in the publication
0.00064
(2E,6E)-farnesyl diphosphate
mutant V88A, pH not specified in the publication, temperature not specified in the publication
0.0007
(2E,6E)-farnesyl diphosphate
mutant V88F, pH not specified in the publication, temperature not specified in the publication
0.00074
(2E,6E)-farnesyl diphosphate
mutant D203L, pH not specified in the publication, temperature not specified in the publication
0.00075
(2E,6E)-farnesyl diphosphate
-
mutant W334L, pH not specified in the publication, temperature not specified in the publication
0.001
(2E,6E)-farnesyl diphosphate
-
mutant W334Y, pH not specified in the publication, temperature not specified in the publication
0.00104
(2E,6E)-farnesyl diphosphate
mutant R200K, pH not specified in the publication, temperature not specified in the publication
0.00159
(2E,6E)-farnesyl diphosphate
mutant R340K, pH not specified in the publication, temperature not specified in the publication
0.00175
(2E,6E)-farnesyl diphosphate
mutant T89A, pH not specified in the publication, temperature not specified in the publication
0.0023
(2E,6E)-farnesyl diphosphate
wild-type, pH 7.5, temperature not specified in the publication
0.00447
(2E,6E)-farnesyl diphosphate
at pH 7.5 and 37°C
0.005
(2E,6E)-farnesyl diphosphate
mutant T89F, pH not specified in the publication, temperature not specified in the publication
0.0502
(2E,6E)-farnesyl diphosphate
mutant Y92C, pH 7.5, temperature not specified in the publication
0.0834
(2E,6E)-farnesyl diphosphate
mutant Y92A, pH 7.5, temperature not specified in the publication
0.7
(2E,6E)-farnesyl diphosphate
mutant L108A, pH not specified in the publication, temperature not specified in the publication
0.99
(2E,6E)-farnesyl diphosphate
mutant L108S, pH not specified in the publication, temperature not specified in the publication
1.76
(2E,6E)-farnesyl diphosphate
mutant L108F, pH not specified in the publication, temperature not specified in the publication
2.03
(2E,6E)-farnesyl diphosphate
mutant L108V, pH not specified in the publication, temperature not specified in the publication
0.0008
farnesyl diphosphate
-
assay under normal conditions and in D2O, 20 mM Tris, 5 mM MgCl2, 5 mM 2-mercaptoethanol and 15% glycerol
0.0009
farnesyl diphosphate
-
mutant F178I
0.002
farnesyl diphosphate
-
mutant F178V
0.0023
farnesyl diphosphate
-
-
0.0047
farnesyl diphosphate
-
mutant F178W
0.0059
farnesyl diphosphate
-
mutant F178C
0.0087
farnesyl diphosphate
-
wild-type
0.0099
farnesyl diphosphate
-
mutant F178Y
0.0197
farnesyl diphosphate
-
mutant F112A
0.0463
farnesyl diphosphate
-
mutant F112A-178A
0.000012
trans,trans-farnesyl diphosphate
pH 8.0, 30°C, mutant enzyme Y92F
0.0000135
trans,trans-farnesyl diphosphate
-
pH 8.0, 30°C, native enzyme
0.0000148
trans,trans-farnesyl diphosphate
-
pH 8.0, 30°C, recombinant enzyme
0.00015
trans,trans-farnesyl diphosphate
pH 8.0, 30°C, mutant enzyme E119Q
0.00032
trans,trans-farnesyl diphosphate
pH 8.0, 30°C, mutant enzyme E119D
0.00052
trans,trans-farnesyl diphosphate
-
pH 8.0, 30°C, recombinant enzyme
0.00055
trans,trans-farnesyl diphosphate
-
pH 7.5
0.0006
trans,trans-farnesyl diphosphate
pH 8.0, 30°C, wild-type enzyme
0.0011
trans,trans-farnesyl diphosphate
pH 8.0, 30°C, mutant enzyme D116E
0.0013
trans,trans-farnesyl diphosphate
-
pH 8.0, 30°C, wild-type enzyme
0.0014
trans,trans-farnesyl diphosphate
-
pH 8.0, 30°C, mutant enzyme E227D
0.0015
trans,trans-farnesyl diphosphate
pH 8.0, 30°C, mutant enzyme D116N
0.0023
trans,trans-farnesyl diphosphate
-
pH 7.5, 30°C, recombinant wild-type enzyme
0.0027
trans,trans-farnesyl diphosphate
pH 8.0, 30°C, mutant enzyme D115E
0.0033
trans,trans-farnesyl diphosphate
pH 8.0, 30°C, mutant enzyme N244D
0.0034
trans,trans-farnesyl diphosphate
pH 8.0, 30°C, mutant enzyme E252D
0.0039
trans,trans-farnesyl diphosphate
-
pH 8.0, 30°C, mutant enzyme N219D
0.0051
trans,trans-farnesyl diphosphate
-
wild-type enzyme, mutant enzyme F178Y
0.0055
trans,trans-farnesyl diphosphate
pH 8.0, 30°C, mutant enzyme S248A
0.0101
trans,trans-farnesyl diphosphate
pH 8.0, 30°C, mutant enzyme E252Q
0.0112
trans,trans-farnesyl diphosphate
-
wild-type enzyme, mutant enzyme F178V
0.05027
trans,trans-farnesyl diphosphate
pH 7.5, mutant enzyme Y92C
0.0834
trans,trans-farnesyl diphosphate
pH 7.5, mutant enzyme Y92A
0.1887
trans,trans-farnesyl diphosphate
-
pH 7.5, 30°C, mutant enzyme Y92F
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0003 - 0.084
(2E,6E)-farnesyl diphosphate
0.095
(2Z,6E)-farnesyl diphosphate
-
in 200 mM Tris-HCl (pH 7.5), 40 mM MgCl2, at 22°C
0.00012
anilinogeranyl diphosphate
at pH 7.5 and 37°C
0.0014 - 550
farnesyl diphosphate
0.000021 - 0.043
trans,trans-farnesyl diphosphate
0.0003
(2E,6E)-farnesyl diphosphate
-
mutant W334H, pH not specified in the publication, temperature not specified in the publication
0.00041
(2E,6E)-farnesyl diphosphate
mutant enzyme S303D, at pH 8.0 and 30°C
0.00049
(2E,6E)-farnesyl diphosphate
mutant Y92C, pH 7.5, temperature not specified in the publication
0.0006
(2E,6E)-farnesyl diphosphate
mutant R200K, pH not specified in the publication, temperature not specified in the publication
0.00063
(2E,6E)-farnesyl diphosphate
mutant enzyme Q151H, at pH 8.0 and 30°C
0.00075
(2E,6E)-farnesyl diphosphate
mutant D203L, pH not specified in the publication, temperature not specified in the publication
0.0008
(2E,6E)-farnesyl diphosphate
mutant V88F, pH not specified in the publication, temperature not specified in the publication
0.0008
(2E,6E)-farnesyl diphosphate
mutant R340K, pH not specified in the publication, temperature not specified in the publication
0.0009
(2E,6E)-farnesyl diphosphate
mutant L108A, pH not specified in the publication, temperature not specified in the publication
0.0011
(2E,6E)-farnesyl diphosphate
mutant T89F, pH not specified in the publication, temperature not specified in the publication
0.0013
(2E,6E)-farnesyl diphosphate
mutant enzyme S303H, at pH 8.0 and 30°C
0.0014
(2E,6E)-farnesyl diphosphate
mutant Y92A, pH 7.5, temperature not specified in the publication
0.0015
(2E,6E)-farnesyl diphosphate
mutant enzyme Q151E, at pH 8.0 and 30°C
0.002
(2E,6E)-farnesyl diphosphate
mutant K251Q, pH not specified in the publication, temperature not specified in the publication
0.0025
(2E,6E)-farnesyl diphosphate
mutant V88A, pH not specified in the publication, temperature not specified in the publication
0.0025
(2E,6E)-farnesyl diphosphate
mutant Y341F, pH not specified in the publication, temperature not specified in the publication
0.0027
(2E,6E)-farnesyl diphosphate
-
mutant W334L, pH not specified in the publication, temperature not specified in the publication
0.0036
(2E,6E)-farnesyl diphosphate
mutant L108F, pH not specified in the publication, temperature not specified in the publication
0.0037
(2E,6E)-farnesyl diphosphate
mutant K251R, pH not specified in the publication, temperature not specified in the publication
0.0057
(2E,6E)-farnesyl diphosphate
mutant L108V, pH not specified in the publication, temperature not specified in the publication
0.0058
(2E,6E)-farnesyl diphosphate
mutant enzyme N299A/S303A, at pH 8.0 and 30°C
0.006
(2E,6E)-farnesyl diphosphate
-
mutant W334F, pH not specified in the publication, temperature not specified in the publication
0.0066
(2E,6E)-farnesyl diphosphate
mutant T89A, pH not specified in the publication, temperature not specified in the publication
0.007
(2E,6E)-farnesyl diphosphate
-
mutant W334Y, pH not specified in the publication, temperature not specified in the publication
0.0095
(2E,6E)-farnesyl diphosphate
mutant L108S, pH not specified in the publication, temperature not specified in the publication
0.012
(2E,6E)-farnesyl diphosphate
mutant enzyme N299A, at pH 8.0 and 30°C
0.027
(2E,6E)-farnesyl diphosphate
wild type enzyme, at pH 8.0 and 30°C
0.03
(2E,6E)-farnesyl diphosphate
wild-type, pH 7.5, temperature not specified in the publication
0.032
(2E,6E)-farnesyl diphosphate
at pH 7.5 and 37°C
0.045
(2E,6E)-farnesyl diphosphate
mutant enzyme S303A, at pH 8.0 and 30°C
0.084
(2E,6E)-farnesyl diphosphate
-
-
0.084
(2E,6E)-farnesyl diphosphate
-
wild-type, pH not specified in the publication, temperature not specified in the publication
0.084
(2E,6E)-farnesyl diphosphate
wild-type, pH not specified in the publication, temperature not specified in the publication
0.084
(2E,6E)-farnesyl diphosphate
-
wild-type, pH not specified in the publication, temperature not specified in the publication
0.0014
farnesyl diphosphate
-
mutant F112A-178A
0.0023
farnesyl diphosphate
-
mutant F112A
0.0041
farnesyl diphosphate
-
mutant F178I
0.0063
farnesyl diphosphate
-
mutant F178V
0.0099
farnesyl diphosphate
-
mutant F178C
0.02
farnesyl diphosphate
-
assay under normal conditions and in D2O, 20 mM Tris, 5 mM MgCl2, 5 mM 2-mercaptoethanol and 15% glycerol
0.052
farnesyl diphosphate
-
mutant F178Y
0.079
farnesyl diphosphate
-
mutant F178W
0.55
farnesyl diphosphate
-
wild-type
1.4
farnesyl diphosphate
-
mutant F112A-178A
2.3
farnesyl diphosphate
-
mutant F112A
4.1
farnesyl diphosphate
-
mutant F178I
6.3
farnesyl diphosphate
-
mutant F178V
9.9
farnesyl diphosphate
-
mutant F178C
52
farnesyl diphosphate
-
mutant F178Y
79
farnesyl diphosphate
-
mutant F178W
550
farnesyl diphosphate
-
wild-type
0.000021
trans,trans-farnesyl diphosphate
-
wild-type enzyme, mutant enzyme F178V
0.000076
trans,trans-farnesyl diphosphate
-
pH 8.0, 30°C, mutant enzyme N219D
0.00012
trans,trans-farnesyl diphosphate
pH 8.0, 30°C, mutant enzyme N244D
0.00022
trans,trans-farnesyl diphosphate
pH 8.0, 30°C, mutant enzyme E252Q
0.0004
trans,trans-farnesyl diphosphate
pH 8.0, 30°C, mutant enzyme Y92F
0.000491
trans,trans-farnesyl diphosphate
pH 7.5, mutant enzyme Y92C
0.001
trans,trans-farnesyl diphosphate
-
wild-type enzyme, mutant enzyme F178Y
0.0013
trans,trans-farnesyl diphosphate
pH 8.0, 30°C, mutant enzyme D116E
0.0013
trans,trans-farnesyl diphosphate
pH 8.0, 30°C, mutant enzyme S248A
0.00137
trans,trans-farnesyl diphosphate
pH 7.5, mutant enzyme Y92A
0.0016
trans,trans-farnesyl diphosphate
-
pH 8.0, 30°C, mutant enzyme E227D
0.0022
trans,trans-farnesyl diphosphate
pH 8.0, 30°C, mutant enzyme D116N
0.0022
trans,trans-farnesyl diphosphate
pH 8.0, 30°C, mutant enzyme E252D
0.0023
trans,trans-farnesyl diphosphate
-
pH 7.5, 30°C, mutant enzyme Y92F
0.0048
trans,trans-farnesyl diphosphate
pH 8.0, 30°C, mutant enzyme E119Q
0.0097
trans,trans-farnesyl diphosphate
pH 8.0, 30°C, mutant enzyme E119D
0.014
trans,trans-farnesyl diphosphate
-
pH 8.0, 30°C, native enzyme
0.015
trans,trans-farnesyl diphosphate
-
pH 8.0, 30°C, recombinant enzyme
0.0162
trans,trans-farnesyl diphosphate
pH 8.0, 30°C, mutant enzyme D115E
0.0173
trans,trans-farnesyl diphosphate
-
pH 8.0, 30°C, wild-type enzyme
0.03
trans,trans-farnesyl diphosphate
-
pH 7.5, 30°C, recombinant wild-type enzyme
0.043
trans,trans-farnesyl diphosphate
-
pH 8.0, 30°C, recombinant enzyme
0.043
trans,trans-farnesyl diphosphate
pH 8.0, 30°C, wild-type enzyme
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0.0011 - 370
(2E,6E)-farnesyl diphosphate
0.0068
(2Z,6E)-farnesyl diphosphate
-
in 200 mM Tris-HCl (pH 7.5), 40 mM MgCl2, at 22°C
0.0011
(2E,6E)-farnesyl diphosphate
mutant V88F, pH not specified in the publication, temperature not specified in the publication
0.0013
(2E,6E)-farnesyl diphosphate
mutant L108A, pH not specified in the publication, temperature not specified in the publication
0.0021
(2E,6E)-farnesyl diphosphate
mutant L108F, pH not specified in the publication, temperature not specified in the publication
0.0022
(2E,6E)-farnesyl diphosphate
mutant T89F, pH not specified in the publication, temperature not specified in the publication
0.0028
(2E,6E)-farnesyl diphosphate
mutant L108V, pH not specified in the publication, temperature not specified in the publication
0.0038
(2E,6E)-farnesyl diphosphate
mutant T89A, pH not specified in the publication, temperature not specified in the publication
0.0039
(2E,6E)-farnesyl diphosphate
mutant V88A, pH not specified in the publication, temperature not specified in the publication
0.0096
(2E,6E)-farnesyl diphosphate
mutant L108S, pH not specified in the publication, temperature not specified in the publication
0.01
(2E,6E)-farnesyl diphosphate
mutant Y92C, pH 7.5, temperature not specified in the publication
0.016
(2E,6E)-farnesyl diphosphate
mutant Y92A, pH 7.5, temperature not specified in the publication
0.158
(2E,6E)-farnesyl diphosphate
wild-type, pH not specified in the publication, temperature not specified in the publication
0.51
(2E,6E)-farnesyl diphosphate
mutant R340K, pH not specified in the publication, temperature not specified in the publication
0.62
(2E,6E)-farnesyl diphosphate
mutant R200K, pH not specified in the publication, temperature not specified in the publication
1.01
(2E,6E)-farnesyl diphosphate
mutant D203L, pH not specified in the publication, temperature not specified in the publication
1.1
(2E,6E)-farnesyl diphosphate
mutant enzyme S303D, at pH 8.0 and 30°C
2.56
(2E,6E)-farnesyl diphosphate
-
mutant W334H, pH not specified in the publication, temperature not specified in the publication
3.56
(2E,6E)-farnesyl diphosphate
-
mutant W334L, pH not specified in the publication, temperature not specified in the publication
5
(2E,6E)-farnesyl diphosphate
-
-
5
(2E,6E)-farnesyl diphosphate
-
wild-type protein
6.95
(2E,6E)-farnesyl diphosphate
-
mutant W334Y, pH not specified in the publication, temperature not specified in the publication
8.5
(2E,6E)-farnesyl diphosphate
mutant K251Q, pH not specified in the publication, temperature not specified in the publication
11.8
(2E,6E)-farnesyl diphosphate
-
A274T/V372I/Y406L/V516I mutant protein
13.04
(2E,6E)-farnesyl diphosphate
wild-type, pH 7.5, temperature not specified in the publication
14
(2E,6E)-farnesyl diphosphate
mutant Y341F, pH not specified in the publication, temperature not specified in the publication
14
(2E,6E)-farnesyl diphosphate
mutant enzyme N299A/S303A, at pH 8.0 and 30°C
15
(2E,6E)-farnesyl diphosphate
mutant enzyme Q151E, at pH 8.0 and 30°C
15
(2E,6E)-farnesyl diphosphate
mutant enzyme Q151H, at pH 8.0 and 30°C
21
(2E,6E)-farnesyl diphosphate
mutant enzyme S303H, at pH 8.0 and 30°C
22.6
(2E,6E)-farnesyl diphosphate
-
mutant W334F, pH not specified in the publication, temperature not specified in the publication
26.4
(2E,6E)-farnesyl diphosphate
mutant K251R, pH not specified in the publication, temperature not specified in the publication
29
(2E,6E)-farnesyl diphosphate
mutant enzyme N299A, at pH 8.0 and 30°C
118
(2E,6E)-farnesyl diphosphate
-
-
158.5
(2E,6E)-farnesyl diphosphate
-
wild-type, pH not specified in the publication, temperature not specified in the publication
158.5
(2E,6E)-farnesyl diphosphate
wild-type, pH not specified in the publication, temperature not specified in the publication
270
(2E,6E)-farnesyl diphosphate
wild type enzyme, at pH 8.0 and 30°C
370
(2E,6E)-farnesyl diphosphate
mutant enzyme S303A, at pH 8.0 and 30°C
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E227D
-
kcat/KM is 1182fold higher than wild-type value, in contrast to wild-type enzyme that exclusively produces aristolochene from trans,trans-farnesyl diphosphate, the mutant enzyme produces 26% aristolochene and 74% germacrene A
E227Q
-
inactive mutant enzyme
N219D
-
kcat/KM is 6667fold higher than wild-type value, in contrast to wild-type enzyme that exclusively produces aristolochene from trans,trans-farnesyl diphosphate, the mutant enzyme produces 44% aristolochene and 56% germacrene A
N299A
the mutation has decreasing effects on catalysis but significant effects on sesquiterpene product distributions of 50% germacrene A and 50% aristolochene
N299A/S303A
the decreasing have modest effects on catalysis but significant effects on sesquiterpene product distributions with germacrene A as main product and (E)-nerolidol and aristolochene as by-products
N299L
the mutation has decreasing effects on sesquiterpene product distributions with germacrene A and aristolochene as main product and (E)-nerolidol as by-product
Q151E
the mutation has decreasing effects on catalysis but significant effects on sesquiterpene product distributions with aristolochene and germacrene A as main products, and (E)-nerolidol and (E,E)-farnesol as by-products
Q151H
the mutation has decreasing effects on catalysis but significant effects on sesquiterpene product distributions with germacrene A and (E,E)-farnesol as main products and (E)-nerolidol and aristolochene as by-products
S303A
the mutation has increasing effects on catalysis and significant effects on sesquiterpene product distributions with germacrene A and (E)-nerolidol as by-products
S303D
the mutation has decreasing effects on catalysis but significant effects on sesquiterpene product distributions with germacrene A and (E,E)-farnesol as main products and (E)-nerolidol and aristolochene as by-products
S303H
the mutation has decreasing effects on catalysis but significant effects on sesquiterpene product distributions with germacrene A as main product and (E,E)-farnesol, (E)-nerolidol and aristolochene as by-products
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
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
F178W
-
mutant is constructed to distinguish between the importance of size and aromaticity residue 178
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
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
Y341F
10fold reduction in catalytic efficiency
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
F112A
-
residue 112 contributes to the stabilisation of the transition state following farnesyl cation
F112A
-
expression of AS-F112A in Escherichia coli
F178V
-
wild-type enzyme produces 92% aristolochene, 8% germacrene and a small amount of valencene. Mutant enzyme produces 10.8% aristolochene, 54.1% germacrene, 5.2% valencene, 5.7% alpha-selinene, 9.1% beta-selinine, 9.2% (E)-beta-farnesene and 2.7% (E,E)-alpha-farnesene. kcat is 1429fold lower than wild-type value, Km-value is 4.9fold higher than wild-type value
F178V
-
mutation leads to the accumulation of the intermediate germacrene A, the production of selinenes and the linear alpha- and beta-farnesene
F178Y
-
wild-type enzyme produces 92% aristolochene, 8% germacrene and a small amount of valencene. Mutant enzyme produces 86.4% aristolochene, 10.7% germacrene, and 2.7% valencene. kcat is 30fold lower than wild-type value, Km-value is 2.2fold higher than wild-type value
F178Y
-
mutant is constructed to distinguish between the importance of size and aromaticity residue 178
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
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
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
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
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
Y92F
100fold reduction in kcat, 50fold decrease in KM, resulting in 2fold decrease in kcat/Km. The mutant enzyme produces (+)-aristolochene as 81% of the product, 7% (-)-valencene and 12% (S)-(-)-germacrene A
Y92F
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
Y92V
-
the mutant produces the alicyclic beta-(E)-farnesene as the major product
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
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Cane, D.E.; Prabhakaran, P.C.; Oliver, J.S.; McIlwaine, D.B.
Aristolochene biosynthesis. Stereochemistry of the deprotonation steps in the enzymatic cyclization of farnesyl pyrophosphate
J. Am. Chem. Soc.
112
3209-3210
1990
Aspergillus terreus
-
brenda
Cane, D.E.; Prabhakaran, P.C.; Salaski, E.J.; Harrison, P.M.H.; Noguchi, H.; Rawlings, B.J.
Aristolochene biosynthesis and enzymatic cyclization of farnesyl pyrophosphate
J. Am. Chem. Soc.
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8914-8916
1989
Aspergillus terreus
-
brenda
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
brenda
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
brenda
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
brenda
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
-
brenda
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
brenda
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)
brenda
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
brenda
Forcat, S.; Allemann, R.K.
Dual role for phenylalanine 178 during catalysis by aristolochene synthase
Chem. Commun. (Camb.)
2004
2094-2095
2004
Penicillium roqueforti
brenda
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
brenda
Shishova, E.Y.; Di Costanzo, L.; Cane, D.E.; Christianson, D.W.
X-ray crystal structure of aristolochene synthase from Aspergillus terreus and evolution of templates for the cyclization of farnesyl diphosphate
Biochemistry
46
1941-1951
2007
Aspergillus terreus (Q9UR08), Aspergillus terreus
brenda
Yu, F.; Miller, D.J.; Allemann, R.K.
Probing the reaction mechanism of aristolochene synthase with 12,13-difluorofarnesyl diphosphate
Chem. Commun. (Camb. )
2007
4155-4157
2007
Escherichia coli
brenda
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
brenda
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)
brenda
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
brenda
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
brenda
Christianson, D.W.
Unearthing the roots of the terpenome
Curr. Opin. Chem. Biol.
12
141-150
2008
Aspergillus terreus
brenda
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
J. Biol. Chem.
283
15431-15439
2008
Aspergillus terreus (Q9UR08), Aspergillus terreus
brenda
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
brenda
Faraldos, J.A.; OMaille, P.E.; Dellas, N.; Noel, J.P.; Coates, R.M.
Bisabolyl-derived sesquiterpenes from tobacco 5-epi-aristolochene synthase-catalyzed cyclization of (2Z,6E)-farnesyl diphosphate
J. Am. Chem. Soc.
132
4281-4289
2010
Nicotiana tabacum
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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)
brenda
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
Biochemistry
52
5441-5453
2013
Aspergillus terreus (Q9UR08), Aspergillus terreus
brenda
van der Kamp, M.W.; Sirirak, J.; ?urek, J.; Allemann, R.K.; Mulholland, A.J.
Conformational change and ligand binding in the aristolochene synthase catalytic cycle
Biochemistry
52
8094-8105
2013
Aspergillus terreus (Q9UR08)
brenda
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
brenda
Rising, K.A.; Crenshaw, C.M.; Koo, H.J.; Subramanian, T.; Chehade, K.A.; Starks, C.; Allen, K.D.; Andres, D.A.; Spielmann, H.P.; Noel, J.P.; Chappell, J.
Formation of a novel macrocyclic alkaloid from the unnatural farnesyl diphosphate analogue anilinogeranyl diphosphate by 5-epi-aristolochene synthase
ACS Chem. Biol.
10
1729-1736
2015
Nicotiana tabacum (Q40577), Nicotiana tabacum
brenda
Chen, M.; Chou, W.K.; Al-Lami, N.; Faraldos, J.A.; Allemann, R.K.; Cane, D.E.; Christianson, D.W.
Probing the role of active site water in the sesquiterpene cyclization reaction catalyzed by aristolochene synthase
Biochemistry
55
2864-2874
2016
Aspergillus terreus (Q9UR08)
brenda
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
brenda