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Information on EC 4.2.3.46 - alpha-farnesene synthase
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4.2.3.46 alpha-farnesene synthaseSpecify your search results
Word Map
The enzyme appears in viruses and cellular organisms
Synonyms
(E,E)-alpha-farnesene synthase, AdAFS1, AFS, AFS-1, AFS1, alpha farnesene synthase 1, alpha-farnesene synthase, alpha-farnesene synthase-1, E,E-alpha-farnesene synthase, MdAFS1, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(E,E)-alpha-farnesene synthase
MdAFS1
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(2E,6E)-farnesyl diphosphate = (3E,6E)-alpha-farnesene + diphosphate
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
(2E,6E)-farnesyl-diphosphate lyase [(3E,6E)-alpha-farnesene-forming]
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(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 + 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
(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
-
-
?
(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
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
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
?
-
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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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
?
(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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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K+
Mg2+
Mn2+
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+
Mn2+
KM: about 0.02 mM, divalent cation required, preference for Mg2+. Maximal velocities with Mn2+ is about 50% of that with Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-methylcyclopropene
after treatment of fruits at harvest with a blocker of ethylene action, AFS1 mRNA declines sharply over the initial 4 weeks of cold storage, and falls to nearly undetectable levels by 8 weeks
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0026
(2E,6E)-farnesyl diphosphate
accession Columbia, 30°C, pH not specified in the publication
0.004
(2E,6E)-farnesyl diphosphate
accession Wassilewskija, 30°C, pH not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.0026
farnesyl diphosphate
mutant S487A, 50 mM KCl, 10 mM MgCl2
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
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.12
(2E,6E)-farnesyl diphosphate
accession Wassilewskija, 30°C, pH not specified in the publication
1.82
(2E,6E)-farnesyl diphosphate
accession Columbia, 30°C, pH not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
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 (wild-type and S487K respective kcat/Km values of 17.5 and 13.3 mM/s)
additional information
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 (wild-type and S487K respective kcat/Km values of 17.5 and 13.3 mM/s)
additional information
-
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 (wild-type and S487K respective kcat/Km values of 17.5 and 13.3 mM/s)
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
genomic structure and sequence polymorphism of E,E-alpha farnesene synthase gene in Malus domestica; Borkh.
UniProt
brenda
genomic structure and sequence polymorphism of E,E-alpha-farnesene synthase gene in Malus domestica; Borkh.
UniProt
brenda
The deduced amino acid sequence of this enzyme shares the greatest degree of homology with a variety of monoterpene synthases, including alpha-(-)beta-pinene synthase, a gamma-terpinene synthase, and a (+)-limonene synthase from Citrus limon, which have 41-42% amino acid identity. A geraniol synthase from Cinnamomum tenuipilum and an isoprene synthase from Populus tremuloides have 42% identity to AFS1. The closest homology is with a linalool/nerolidol synthase from Fragaria ananassa (35% identity) and a (+)-delta-cadinene synthase from Gossypium hirsutum (33% identity).; Malus domestica Borkh., cultivar Law Rome
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
production of (E,E)-alpha-farnesene occurs in the epidermal (peel tissue) or adjacent hypodermal cell layers and the sesquiterpene can accumulate to high levels in the natural epicuticular coating of scald-susceptible apples during the first weeks of storage
brenda
within floral tissues, expression is highest in petals and stamens
brenda
within floral tissues, expression is highest in petals and stamens
brenda
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
brenda
expression occurs constitutively in floral tissues
brenda
CmTpsDul expression is specific to ’Dulce’ rind. CmTpsDul is not expressed in either the rind or flesh of ‘Noy Yizre’el’ melons at any developmental stage
brenda
Cucumis melo variety Noy Yizre'el
-
CmTpsDul expression is specific to ’Dulce’ rind. CmTpsDul is not expressed in either the rind or flesh of ‘Noy Yizre’el’ melons at any developmental stage
brenda
expression of AdAFS1 is significantly higher in flowers than in leaf tissue. AdAFS1 expression is similar in leaves of both cultivars ‘Chieftain’ and ‘Hayward’
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
plastidial transit peptide of 25 amino acids, and fluoresence studies using GPF-fusion protein, accession Wassilewskija
brenda
additional information
AdAFS1 protein sequences lacks predicted N-terminal transit peptide-like sequences for chloroplast targeting
-
brenda
The encoded protein appears to lack approximately 20 amino acids that are present in the N-terminal chloroplast-targeting region of monoterpene synthases. Thus, the product of this TS gene is most likely localized in the cytosol.
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
differences in the relative emissions of (E)-beta-ocimene and (E,E)-alpha-farnesene from accession Wassilewskija, a high-(E)-beta-ocimene emitter, and accession Columbia, a trace-(E)-beta-ocimene emitter, are attributed to allelic variation of closely related, tandem-duplicated terpene synthase genes, TPS02 and TPS03. The Wassilewskija genome contains a functional allele of TPS02 but not of TPS03, while the opposite is the case for Columbia. Recombinant proteins of the functional Wassilewskija TPS02 and Columbia TPS03 genes both show (E)-beta-ocimene and (E,E)-alpha-farnesene synthase activities. Differential subcellular compartmentalization of the two enzymes in plastids and the cytosol is responsible for the ecotype-specific differences in (E)-beta-ocimene/(E,E)-alpha-farnesene emission
physiological function
-
the enzyme contributes to the resistance of soybean to Soybean cyst nematodes and is involved in synthesizing insect-induced volatiles
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PT5_PINTA
574
0
65941
Swiss-Prot
other Location (Reliability: 2)
TPS7_RICCO
564
0
65793
Swiss-Prot
other Location (Reliability: 5)
TPS03_ARATH
565
0
65753
Swiss-Prot
Mitochondrion (Reliability: 3)
AFSY1_CUCME
560
0
65190
Swiss-Prot
other Location (Reliability: 5)
OCISB_ARATH
589
0
69047
Swiss-Prot
Chloroplast (Reliability: 2)
AFS1_MALDO
576
0
66183
Swiss-Prot
other Location (Reliability: 3)
A0A2P6Q9K5_ROSCH
171
0
19906
TrEMBL
Mitochondrion (Reliability: 3)
A0A2P6S2Z2_ROSCH
852
0
96913
TrEMBL
other Location (Reliability: 2)
A0A396J1K1_MEDTR
398
0
45843
TrEMBL
other Location (Reliability: 4)
A0A5B7BFK3_DAVIN
578
0
67053
TrEMBL
other Location (Reliability: 4)
A0A068B2J7_9ROSA
573
0
65693
TrEMBL
other Location (Reliability: 2)
A0A2G9H9P8_9LAMI
540
0
62104
TrEMBL
Mitochondrion (Reliability: 5)
A0A396J534_MEDTR
106
0
12565
TrEMBL
Secretory Pathway (Reliability: 5)
A0A396GVL8_MEDTR
308
0
35671
TrEMBL
other Location (Reliability: 4)
A0A1S2XAE3_CUCME
560
0
65190
TrEMBL
other Location (Reliability: 5)
A0A2P6Q9L9_ROSCH
199
0
23572
TrEMBL
other Location (Reliability: 4)
A0A1U9M7X9_MURKO
560
0
64644
TrEMBL
other Location (Reliability: 3)
A0A2P6SBG1_ROSCH
288
0
33799
TrEMBL
Mitochondrion (Reliability: 4)
A0A396J5B0_MEDTR
136
0
15921
TrEMBL
other Location (Reliability: 4)
A0A2P6Q9J5_ROSCH
221
0
26020
TrEMBL
Mitochondrion (Reliability: 3)
I6XZ73_9CARY
562
0
65104
TrEMBL
other Location (Reliability: 4)
A0A2G9HXD9_9LAMI
515
0
59734
TrEMBL
other Location (Reliability: 4)
A0A396J5S7_MEDTR
283
0
32427
TrEMBL
other Location (Reliability: 5)
A0A2P6Q325_ROSCH
580
0
66741
TrEMBL
other Location (Reliability: 2)
A0A2P6Q9N2_ROSCH
179
0
20289
TrEMBL
other Location (Reliability: 3)
A0A396GT68_MEDTR
299
0
35642
TrEMBL
Secretory Pathway (Reliability: 5)
A0A2P6Q9K0_ROSCH
337
0
38557
TrEMBL
other Location (Reliability: 3)
A0A2G9HXI0_9LAMI
559
0
65184
TrEMBL
Chloroplast (Reliability: 5)
A0A2G9HQD4_9LAMI
846
0
97658
TrEMBL
other Location (Reliability: 3)
GCSY1_CUCME
571
0
66633
Swiss-Prot
other Location (Reliability: 4)
C7SHN9_ACTDE
768
0
88181
TrEMBL
other Location (Reliability: 4)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
S485A
S487A
S487K
S488A
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 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
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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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
sesquiterpene synthase activity declined below pH 7.0 and at pH 5.0-5.5, it is reduced more than 50%
694765
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
AFS1 transcript increases about 4fold in peel tissue of apple fruit during the first 4 weeks of storage at 0.5°C
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
After screening a cDNA library generated from the peel tissue mRNA, a full-length terpene synthase cDNA 1931 nucleotides long is isolated (hot phenol RNA extraction protocol is used). The 1728-bp open reading frame encodes the 576 amino acid protein. Expression of the apple gene in Escherichia coli.
expressed in Escherichia coli BL21 (DE3) CodonPlus cells and transgenic hairy roots of Glycine max
-
expression in Escherichia coli
mutated enzymes are generated using the QuickChange II site-directed mutagenesis kit. The PCR-based mutagenesis protocol is performed using pET-30a harbouring the MdAFS1 cDNAs as template. The single-site mutant enzymes overexpressed in Escherichia coli.
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
myc-tagged and untagged AFS1 expressed protein in bacterial inclusion-body fractions is urea-denatured, purified and renatured prior to assay of enzymatic activity.
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
Because diphenylamine treatment leaves unwanted chemical residues on the fruit, restricts export markets, and creates environmental concerns, a long-range molecular genetic strategy for control of scald by reduction of (E,E)-alpha-farnesene synthesis in scald-susceptible apples is searched. The success of this strategy will rely on our ability to identify, clone, and characterize key genes involved in alpha-farnesene biosynthesis and its regulation by ethylene.
synthesis
expression in Sacchaomyces cerevisiae leads to a titer of (-)-alpha-copaene of 9 mg/l at 48 h and around 7 mg/l in Eschrichia coli, and the titer of (+)-delta-cadinene is 6 mg/l in Saccharomyces cerevisiae and 3.5 mg/l in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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.; Köllner, 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
brenda
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)
brenda
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)
brenda
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
brenda
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