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(2E,6E)-farnesyl diphosphate
(3E,6E)-alpha-farnesene + beta-farnesene + diphosphate
when farnesyl diphosphate, synthesised from 96% (E,E)-farnesol, is incubated with recombinant protein, (E,E)- and (Z,E)-alpha-farnesene are produced in a ratio of 96:4, respectively
-
-
?
(2E,6E)-farnesyl diphosphate
(3E,6E)-alpha-farnesene + diphosphate
(2E,6E)-farnesyl diphosphate
alpha-farnesene + diphosphate
(2E,6E)-farnesyl diphosphate + H2O
(3E,6E)-alpha-farnesene + diphosphate
-
-
about 95% of total product, plus trace amounts of beta-farnesene
-
?
farnesyl diphosphate
(E,E)-alpha-farnesene + diphosphate
sesquiterpene synthase activity
-
-
?
farnesyl diphosphate
(Z,E)-alpha-farnesene + diphosphate
isomers of farnesene produced in apple fruit are (E,E)-alpha and (Z,E)-alpha are in a ratio of 300:1
trace amounts
-
?
geranyl diphosphate
(E)-beta-ocimene + beta-myrcene
poor substrate
-
-
?
geranyl diphosphate
(E)-beta-ocimene + diphosphate
geranyl diphosphate
(Z)-beta-ocimene + diphosphate
monoterpene synthase activity
-
-
?
geranyl diphosphate
linalool + (Z)-beta-ocimene + (E)-beta-ocimene + beta-myrcene
at 18% of the optimised rate for alpha-farnesene synthesis from farnesyl diphosphate
-
-
?
additional information
?
-
(2E,6E)-farnesyl diphosphate
(3E,6E)-alpha-farnesene + diphosphate
the product consists primarily of (E,E)-alpha-farnesene (more than 95%) with trace amounts of (Z,E)-alpha-farnesene
-
-
?
(2E,6E)-farnesyl diphosphate
(3E,6E)-alpha-farnesene + diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate
(3E,6E)-alpha-farnesene + diphosphate
-
-
-
-
?
(2E,6E)-farnesyl diphosphate
(3E,6E)-alpha-farnesene + diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate
(3E,6E)-alpha-farnesene + diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate
(3E,6E)-alpha-farnesene + diphosphate
commentary
-
-
?
(2E,6E)-farnesyl diphosphate
(3E,6E)-alpha-farnesene + diphosphate
alpha-farnesene synthase is a key enzyme in the pathway of alpha-farnesene synthesis
-
-
?
(2E,6E)-farnesyl diphosphate
(3E,6E)-alpha-farnesene + diphosphate
apha-farnesene synthase is a key enzyme in the pathway of alpha-farnesene synthesis
-
-
?
(2E,6E)-farnesyl diphosphate
(3E,6E)-alpha-farnesene + diphosphate
-
sole product
-
?
(2E,6E)-farnesyl diphosphate
alpha-farnesene + diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate
alpha-farnesene + diphosphate
Cucumis melo variety Noy Yizre'el
-
-
-
-
?
geranyl diphosphate
(E)-beta-ocimene + diphosphate
AdAFS1 can function as a bifunctional enzyme possessing both sesquiterpene and monoterpene synthase activities. Exhibits significant monoterpene synthase activity, producing exclusively (E)-beta-ocimene. kcat/Km is about 5fold lower than kcat/Km for farnesyl diphosphate
-
-
?
geranyl diphosphate
(E)-beta-ocimene + diphosphate
in monoterpene synthase assays, only (E)-beta-ocimene is produced at much reduced levels
-
-
?
additional information
?
-
enzyme shows both (E)-beta-ocimene and (E,E)-alpha-farnesene synthase activities
-
-
?
additional information
?
-
enzyme shows both (E)-beta-ocimene and (E,E)-alpha-farnesene synthase activities
-
-
?
additional information
?
-
-
no activity with geranyl diphosphate
-
-
?
additional information
?
-
other sesquiterpenes identified in trace amounts are (E)-nerolidol and beta-farnesene
-
-
?
additional information
?
-
the monoterpene synthase ((E)-beta-ocimene and beta-myrcene) and sesquiterpene synthase (alpha-farnesene) products produced by the mutated and wild-type enzymes are identical, there are no significant alterations in the ratios of the alpha-farnesene isomers produced
-
-
?
additional information
?
-
the monoterpene synthase ((E)-beta-ocimene and beta-myrcene) and sesquiterpene synthase (alpha-farnesene) products produced by the mutated and wild-type enzymes are identical, there are no significant alterations in the ratios of the alpha-farnesene isomers produced
-
-
?
additional information
?
-
-
the monoterpene synthase ((E)-beta-ocimene and beta-myrcene) and sesquiterpene synthase (alpha-farnesene) products produced by the mutated and wild-type enzymes are identical, there are no significant alterations in the ratios of the alpha-farnesene isomers produced
-
-
?
additional information
?
-
although (E,E)-farnesyl diphosphate is the preferred substrate, the enzyme accepts all four isomeric forms of the farnesyl diphosphate precursor. Both isomers of beta-farnesene are also synthesised by the enzyme presumably from a specific farnesene isomer. The enzyme also produces alpha-farnesene by a reaction involving coupling of geranyl diphosphate and isoprenyl diphosphate but at less than 1% of the rate with farnesyl diphosphate
-
-
?
additional information
?
-
-
although (E,E)-farnesyl diphosphate is the preferred substrate, the enzyme accepts all four isomeric forms of the farnesyl diphosphate precursor. Both isomers of beta-farnesene are also synthesised by the enzyme presumably from a specific farnesene isomer. The enzyme also produces alpha-farnesene by a reaction involving coupling of geranyl diphosphate and isoprenyl diphosphate but at less than 1% of the rate with farnesyl diphosphate
-
-
?
additional information
?
-
-
Populus trichocarpa Pts2 also acceepts geranyl diphosphate to produce small amounts of (E)-beta-ocimene
-
-
?
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(2E,6E)-farnesyl diphosphate
(3E,6E)-alpha-farnesene + diphosphate
farnesyl diphosphate
(E,E)-alpha-farnesene + diphosphate
sesquiterpene synthase activity
-
-
?
farnesyl diphosphate
(Z,E)-alpha-farnesene + diphosphate
isomers of farnesene produced in apple fruit are (E,E)-alpha and (Z,E)-alpha are in a ratio of 300:1
trace amounts
-
?
geranyl diphosphate
(E)-beta-ocimene + diphosphate
in monoterpene synthase assays, only (E)-beta-ocimene is produced at much reduced levels
-
-
?
geranyl diphosphate
(Z)-beta-ocimene + diphosphate
monoterpene synthase activity
-
-
?
additional information
?
-
(2E,6E)-farnesyl diphosphate
(3E,6E)-alpha-farnesene + diphosphate
-
-
-
-
?
(2E,6E)-farnesyl diphosphate
(3E,6E)-alpha-farnesene + diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate
(3E,6E)-alpha-farnesene + diphosphate
commentary
-
-
?
(2E,6E)-farnesyl diphosphate
(3E,6E)-alpha-farnesene + diphosphate
alpha-farnesene synthase is a key enzyme in the pathway of alpha-farnesene synthesis
-
-
?
(2E,6E)-farnesyl diphosphate
(3E,6E)-alpha-farnesene + diphosphate
apha-farnesene synthase is a key enzyme in the pathway of alpha-farnesene synthesis
-
-
?
additional information
?
-
other sesquiterpenes identified in trace amounts are (E)-nerolidol and beta-farnesene
-
-
?
additional information
?
-
the monoterpene synthase ((E)-beta-ocimene and beta-myrcene) and sesquiterpene synthase (alpha-farnesene) products produced by the mutated and wild-type enzymes are identical, there are no significant alterations in the ratios of the alpha-farnesene isomers produced
-
-
?
additional information
?
-
the monoterpene synthase ((E)-beta-ocimene and beta-myrcene) and sesquiterpene synthase (alpha-farnesene) products produced by the mutated and wild-type enzymes are identical, there are no significant alterations in the ratios of the alpha-farnesene isomers produced
-
-
?
additional information
?
-
-
the monoterpene synthase ((E)-beta-ocimene and beta-myrcene) and sesquiterpene synthase (alpha-farnesene) products produced by the mutated and wild-type enzymes are identical, there are no significant alterations in the ratios of the alpha-farnesene isomers produced
-
-
?
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K+
-
required
K+
500 mM are included in monoterpene synthase assay
K+
MdAFS1 retains up to 12% of its activity in the absence of K+, enzyme contains K+ binding region, MdAFS1 exhibits a type II K+ response, MdAFS1 is not absolutely dependent upon M+ its unequivocal classification as type I or type II K+ activated, or that of any other terpene synthases, will not be possibl, then type I enzymes can exhibit type II kinetics and vice versa.
K+
30-50 mM, enhances activity 5fold. Km: 3 mM. Addition of K+ reduces monoterpene synthase activity
K+
activity is dependent on K+, the potassium binding region is defined
K+
-
in presence of 50 mM potassium, the enzyme activity increases 15fold as compared to the activity in an assay devoid of potassium
Mg2+
Km: 0.248 mM, divalent cation required, preference for Mg2+. Maximal velocities with Mn2+ is about 50% of that with Mg2+
Mg2+
10 mM are included in farnesyl diphosphate activity assay
Mg2+
10 mM are included in sesquiterpene synthase assay
Mn2+
KM: about 0.02 mM, divalent cation required, preference for Mg2+. Maximal velocities with Mn2+ is about 50% of that with Mg2+
Mn2+
1 mM is included in monoterpene synthase assay
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0.0026 - 0.44
(2E,6E)-farnesyl diphosphate
0.0026 - 0.0613
farnesyl diphosphate
0.000005 - 0.03
geranyl diphosphate
0.0026
(2E,6E)-farnesyl diphosphate
pH 7.5, 30°C, mutant enzyme S487A
0.0045
(2E,6E)-farnesyl diphosphate
accession Wassilewskija, 30°C, pH not specified in the publication
0.0048
(2E,6E)-farnesyl diphosphate
accession Columbia, 30°C, pH not specified in the publication
0.0086
(2E,6E)-farnesyl diphosphate
pH 7.5, 30°C, mutant enzyme D484A
0.039
(2E,6E)-farnesyl diphosphate
pH 7.5, 30°C, mutant enzyme S488A
0.0553
(2E,6E)-farnesyl diphosphate
pH 7.5, 30°C, wild-type enzyme
0.0613
(2E,6E)-farnesyl diphosphate
pH 7.5, 30°C, mutant enzyme S485A
0.44
(2E,6E)-farnesyl diphosphate
pH 7.5
0.0026
farnesyl diphosphate
mutant S487A, 50 mM KCl, 10 mM MgCl2
0.0062
farnesyl diphosphate
without K+
0.0086
farnesyl diphosphate
mutant D484A, 50 mM KCl, 10 mM MgCl2
0.022
farnesyl diphosphate
without K+, sesquiterpene synthase activity in mutant S487K is independent of K+
0.039
farnesyl diphosphate
mutant S488A, 50 mM KCl, 10 mM MgCl2
0.0533
farnesyl diphosphate
wild-type MdAFS, 50 mM KCl, 10 mM MgCl2
0.0613
farnesyl diphosphate
mutant S485A, 50 mM KCl, 10 mM MgCl2
0.000005
geranyl diphosphate
mutant S487A
0.000005
geranyl diphosphate
pH 7.5, 30°C, mutant enzyme S487A
0.000034
geranyl diphosphate
mutant D484A
0.000034
geranyl diphosphate
pH 7.5, 30°C, mutant enzyme D484A
0.000052
geranyl diphosphate
mutant S488A
0.000052
geranyl diphosphate
pH 7.5, 30°C, mutant enzyme S488A
0.000281
geranyl diphosphate
wild-type
0.000281
geranyl diphosphate
pH 7.5, 30°C, wild-type enzyme
0.000588
geranyl diphosphate
mutant S485A
0.000588
geranyl diphosphate
pH 7.5, 30°C, mutant enzyme S485A
0.03
geranyl diphosphate
pH 7.5
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AFSY1_CUCME
560
0
65190
Swiss-Prot
other Location (Reliability: 5)
OCISB_ARATH
589
0
69047
Swiss-Prot
Chloroplast (Reliability: 2)
TPS7_RICCO
564
0
65793
Swiss-Prot
other Location (Reliability: 5)
FARNS_PICXS
580
0
66198
Swiss-Prot
other Location (Reliability: 3)
AFS1_MALDO
576
0
66183
Swiss-Prot
other Location (Reliability: 3)
PT5_PINTA
574
0
65941
Swiss-Prot
other Location (Reliability: 2)
TPS03_ARATH
565
0
65753
Swiss-Prot
Mitochondrion (Reliability: 3)
A0A8F8AI47_9LAMI
525
0
61065
TrEMBL
other Location (Reliability: 4)
A0A2G9HXD9_9LAMI
515
0
59734
TrEMBL
other Location (Reliability: 4)
A0A2P6Q9N2_ROSCH
179
0
20289
TrEMBL
other Location (Reliability: 3)
A0A5B7BFK3_DAVIN
578
0
67053
TrEMBL
other Location (Reliability: 4)
A0A2P6Q9K5_ROSCH
171
0
19906
TrEMBL
Mitochondrion (Reliability: 3)
A0A2P6S2Z2_ROSCH
852
0
96913
TrEMBL
other Location (Reliability: 2)
A0A2G9HXI0_9LAMI
559
0
65184
TrEMBL
Chloroplast (Reliability: 5)
A0A1U9M7X9_MURKO
560
0
64644
TrEMBL
other Location (Reliability: 3)
A0A396J1K1_MEDTR
398
0
45843
TrEMBL
other Location (Reliability: 4)
A0A396J5B0_MEDTR
136
0
15921
TrEMBL
other Location (Reliability: 4)
A0A2G9HQD4_9LAMI
846
0
97658
TrEMBL
other Location (Reliability: 3)
A0A396J534_MEDTR
106
0
12565
TrEMBL
Secretory Pathway (Reliability: 5)
A0A2P6Q9L9_ROSCH
199
0
23572
TrEMBL
other Location (Reliability: 4)
A0A068B2J7_9ROSA
573
0
65693
TrEMBL
other Location (Reliability: 2)
A0A2P6Q9J5_ROSCH
221
0
26020
TrEMBL
Mitochondrion (Reliability: 3)
A0A2G9H9P8_9LAMI
540
0
62104
TrEMBL
Mitochondrion (Reliability: 5)
A0A513Q7C2_CAMSI
530
0
61403
TrEMBL
other Location (Reliability: 1)
A0A2P6Q325_ROSCH
580
0
66741
TrEMBL
other Location (Reliability: 2)
A0A2P6Q9K0_ROSCH
337
0
38557
TrEMBL
other Location (Reliability: 3)
I6XZ73_9CARY
562
0
65104
TrEMBL
other Location (Reliability: 4)
A0A396GVL8_MEDTR
308
0
35671
TrEMBL
other Location (Reliability: 4)
A0A2P6SBG1_ROSCH
288
0
33799
TrEMBL
Mitochondrion (Reliability: 4)
A0A1S2XAE3_CUCME
560
0
65190
TrEMBL
other Location (Reliability: 5)
A0A396GT68_MEDTR
299
0
35642
TrEMBL
Secretory Pathway (Reliability: 5)
A0A396J5S7_MEDTR
283
0
32427
TrEMBL
other Location (Reliability: 5)
GCSY1_CUCME
571
0
66633
Swiss-Prot
-
B2ZZ11_MALDO
162
0
18042
TrEMBL
-
C7SHN9_ACTDE
768
0
88181
TrEMBL
-
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D326A
alpha-farnesene synthase, monoterpene synthase and prenyltransferase activities are lost in the mutant
D326A/D330A
alpha-farnesene synthase, monoterpene synthase and prenyltransferase activities are lost in the mutant
D484A
85% loss of sesquiterpene synthase activity compared with wild-type enzyme when K+ is present
D484A
85% loss of sesquiterpene synthase activity compared with wild-type enzyme. Little change in K+-independent activity
S485A
exhibits marginally increased sesquiterpene synthase activities, and an approximate 2fold increase in monoterpene synthase activity compared with the wild-type enzyme
S485A
mutant exhibits marginally increased sesquiterpene synthase activities, and an approximate 2fold increase in monoterpene synthase activity compared with the wild-type enzyme
S487A
95% decrease in sesquiterpene synthase activity compared with wild-type enzyme when K+ is present
S487A
95% decrease in sesquiterpene synthase activity compared with wild-type enzyme. Little change in K+-independent activity
S487K
The S487K mutant has 35-45% of the wild-type activity with farnesyl diphosphate, with no significant alterations in the alpha-farnesene isomer ratios produced and a small decrease in catalytic efficiency
S487K
mutant has 3545% of the wild-type activity with farnesyl diphosphate, with no significant alterations in the alpha-farnesene isomer ratios produced and a small decrease in catalytic efficiency
S488A
mutant shows decreases in both sesqui- and monoterpene synthase activities compared with the WT enzyme, with mono-TPS activity being reduced more than sesquiterpene synthase activity. Sesquiterpene synthase (alpha-farnesene) products produced by the mutated and wild-type enzymes are identical, there are no significant alterations in the ratios of the alpha-farnesene isomers produced.
S488A
mutant shows decreases in both sesqui- and mono-terpene synthases activities, compared with the wild-type enzyme, with mono-terpene synthases activity being reduced more than sesqui-terpene synthases activity
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enzyme expression is induced by Tetranychus urticae (two-spotted spider mites) and exogenous application of methyl jasmonate
-
expression is induced in leaves by elicitor and insect treatment
expression of AdAFS1 is significantly higher in flowers than in leaf tissue. Within floral tissues, expression is highest in petals and stamens. AdAFS1 expression is low in sepals in both sexes and also in Hayward pistils. AdAFS1 expression in Hayward is co-ordinated with anthesis, with low levels of expression in unopened flower buds and high levels detected in open flowers. The temporal accumulation patterns of AdAFS1 mRNA is constitutive. No difference in expression between male and female flowers. AdAFS1 expression is similar in leaves of both cultivars Chieftain and Hayward
expression of pMdAFS1 is repressed by 1-methylcyclopropene treatment, pMdAFS1 expression is controlled by ethylene
induced by Lymantria dispar feeding, up to 136fold increase in transcript abundance
-
MdAFS1 transcript abundance increases rapidly in untreated Cortland and Law Rome fruit, reaching close to maximal values after 2 weeks of storage, whereas in Idared controls it increases through 4 weeks, declines slightly, and then increases to a maximum by 10 weeks. 1-Methylcyclopropene treatment initially suppresses MdAFS1 expression in all three cultivars. However, Cortland and Law Rome escape from this suppression after 10-15 weeks, with MdAFS1 transcript abundance increasing to maximal control levels by 15-20 weeks. In Cortland, but not in Law Rome, this delayed increase in expression occurrs sooner in green than in red tissue. MdAFS1 transcript levels increase gradually in 1-methylcyclopropene-treated Idared fruit, but throughout storage remains much lower than the maximum levels in untreated fruit
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Green, S.; Squire, C.J.; Nieuwenhuizen, N.J.; Baker, E.N.; Laing, W.
Defining the potassium binding region in an apple terpene synthase
J. Biol. Chem.
284
8661-8669
2009
Malus domestica (B2ZZ11), Malus domestica (Q84LB2), Malus domestica
brenda
Pechous S.W.; Whitaker, B.D.
Cloning and functional expression of an (E,E)-alpha-farnesene synthase cDNA from peel tissue of apple fruit
Planta
219
84-94
2004
Malus domestica (Q84LB2)
brenda
Ban, Y.; Oyama-Okubo, N.; Honda, C.; Nakayama, M.; Moriguchi, T.
Emitted and endogenous volatiles in 'Tsugaru' apple: The mechanism of ester and (E,E)-?-farnesene accumulation
Food Chem.
118
272-277
2010
Malus domestica (B2ZZ11)
brenda
Yuan, K.; Liu, Q.; Li, B.; Zhang, L.
Genomic structure and sequence polymorphism of E,E-alpha-farnesene synthase gene in apples (Malus domestica Borkh.)
Front. Agric. China
2
190-193
2008
Malus domestica (Q84LB2)
-
brenda
Beuning, L.; Green, S.; Yauk, Y.-K.
The genomic sequence of AFS-1 - an alpha-farnesene synthase from the apple cultivar Royal Gala
Front. Agric. China
4
74-78
2010
Malus domestica (Q84LB2)
-
brenda
Tsantili, E.; Gapper, N.E.; Arquiza, J.M.; Whitaker, B.D.; Watkins, C.B.
Ethylene and alpha-farnesene metabolism in green and red skin of three apple cultivars in response to 1-methylcyclopropene (1-MCP) treatment
J. Agric. Food Chem.
55
5267-5276
2007
Malus domestica (B2ZZ11), Malus domestica
brenda
Nieuwenhuizen, N.J.; Wang, M.Y.; Matich, A.J.; Green, S.A.; Chen, X.; Yauk, Y.-K.; Beuning, L.L.; Atkinson, R.G.
Two terpene synthases are responsible for the major sesquiterpenes emitted from the flowers of kiwifruit (Actinidia deliciosa)
J. Exp. Bot.
60
3203-3219
2009
Actinidia deliciosa (C7SHN9)
brenda
Green, S.; Friel, E.N.; Matich, A.; Beuning, L.L.; Cooney, J.M.; Rowan, D.D.; MacRae, E.
Unusual features of a recombinant apple alpha-farnesene synthase
Phytochemistry
68
176-188
2006
Malus domestica (Q84LB2), Malus domestica
brenda
Portnoy, V.; Benyamini, Y.; Bar, E.; Harel-Beja, R.; Gepstein, S.; Giovannoni, J.J.; Schaffer, A.A.; Burger, J.; Tadmor, Y.; Lewinsohn, E.; Katzir, N.
The molecular and biochemical basis for varietal variation in sesquiterpene content in melon (Cucumis melo L.) rinds
Plant Mol. Biol.
66
647-661
2008
Cucumis melo (B2KSJ5)
brenda
Danner, H.; Boeckler, G.; Irmisch, S.; Yuan, J.; Chen, F.; Gershenzon, J.; Unsicker, S.; Kllner, T.
Four terpene synthases produce major compounds of the gypsy moth feeding-induced volatile blend of Populus trichocarpa
Phytochemistry
72
897-908
2011
Populus trichocarpa
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Huang, M.; Abel, C.; Sohrabi, R.; Petri, J.; Haupt, I.; Cosimano, J.; Gershenzon, J.; Tholl, D.
Variation of herbivore-induced volatile terpenes among Arabidopsis ecotypes depends on allelic differences and subcellular targeting of two terpene synthases, TPS02 and TPS03
Plant Physiol.
153
1293-1310
2010
Arabidopsis thaliana (A4FVP2), Arabidopsis thaliana (P0CJ43)
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Xie, X.; Kirby, J.; Keasling, J.D.
Functional characterization of four sesquiterpene synthases from Ricinus communis (castor bean)
Phytochemistry
78
20-28
2012
Ricinus communis (B9RXW0)
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Lin, J.; Wang, D.; Chen, X.; Koellner, T.G.; Mazarei, M.; Guo, H.; Pantalone, V.R.; Arelli, P.; Stewart, C.N.; Wang, N.; Chen, F.
An (E,E)-alpha-farnesene synthase gene of soybean has a role in defence against nematodes and is involved in synthesizing insect-induced volatiles
Plant Biotechnol. J.
15
510-519
2017
Glycine max
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