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Information on EC 4.2.3.38 - alpha-bisabolene synthase
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EC Tree
4.2.3.38 alpha-bisabolene synthaseIUBMB Comments
This cytosolic sesquiterpenoid synthase requires a divalent cation cofactor (Mg2+ or, to a lesser extent, Mn2+) to neutralize the negative charge of the diphosphate leaving group. While unlikely to encounter geranyl diphosphate (GDP) in vivo as it is localized to plastids, the enzyme can use GDP as a substrate in vitro to produce (+)-(4R)-limonene [cf. EC 4.2.3.20, (R)-limonene synthase]. The enzyme is induced as part of a defense mechanism in the grand fir Abies grandis as a response to stem wounding.
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Word Map
- 4.2.3.38
-
sesquiterpene
- synthases
-
terpene
-
biofuels
-
terpenoids
- abies
-
monoterpene
-
feedstock
-
conifer
-
herbivores
-
climate
-
cyanobacterial
- synechocystis
- grandis
The enzyme appears in viruses and cellular organisms
Synonyms
bisabolene synthase, (e)-alpha-bisabolene synthase, e-alpha-bisabolene synthase, gbtps2, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(E)-alpha-bisabolene synthase
bisabolene synthase
-
-
-
-
additional information
additional information
the enzyme belongs to the terpenoid synthases, subgroup sesquiterpene synthases
additional information
the enzyme belongs to the sesquiterpene synthase family of enzymes, TPS-d subfamily
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(2E,6E)-farnesyl diphosphate = (E)-alpha-bisabolene + diphosphate
-
-
-
-
(2E,6E)-farnesyl diphosphate = (E)-alpha-bisabolene + diphosphate
electrophilic reaction mechanism
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
(2E,6E)-farnesyl-diphosphate diphosphate-lyase [(E)-alpha-bisabolene-forming]
This cytosolic sesquiterpenoid synthase requires a divalent cation cofactor (Mg2+ or, to a lesser extent, Mn2+) to neutralize the negative charge of the diphosphate leaving group. While unlikely to encounter geranyl diphosphate (GDP) in vivo as it is localized to plastids, the enzyme can use GDP as a substrate in vitro to produce (+)-(4R)-limonene [cf. EC 4.2.3.20, (R)-limonene synthase]. The enzyme is induced as part of a defense mechanism in the grand fir Abies grandis as a response to stem wounding.
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CAS REGISTRY NUMBER
COMMENTARY
211049-94-4
-
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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
(E)-gamma-bisabolene + diphosphate
-
product identification by GC-MS, overview
-
-
?
(2E,6E)-farnesyl diphosphate
(S)-beta-bisabolene + alpha-bisabolol + diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate
(E)-alpha-bisabolene + diphosphate
-
(E)-alpha-bisabolene is the precursor in Abies species of todomatuic acid, juvabione, and related insect juvenile hormone mimics, overview
-
?
(2E,6E)-farnesyl diphosphate
(E)-alpha-bisabolene + diphosphate
the recombinant enzymes is substrate-specific and produces (E)-alpha-bisabolene as sole product
-
-
?
(2E,6E)-farnesyl diphosphate
(E)-alpha-bisabolene + diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate
(E)-alpha-bisabolene + diphosphate
-
product identification by GC-MS
-
?
(2E,6E)-farnesyl diphosphate
(E)-alpha-bisabolene + diphosphate
a step in the terpene synthesis pathway, overview
-
-
?
additional information
?
-
induced (E)-alpha-bisabolene biosynthesis constitutes part of a defense response targeted to insect herbivores, and possibly fungal pathogens, that is distinct from induced oleoresin monoterpene production
-
-
?
additional information
?
-
-
induced (E)-alpha-bisabolene biosynthesis constitutes part of a defense response targeted to insect herbivores, and possibly fungal pathogens, that is distinct from induced oleoresin monoterpene production
-
-
?
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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
(2E,6E)-farnesyl diphosphate
(S)-beta-bisabolene + alpha-bisabolol + diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate
(E)-alpha-bisabolene + diphosphate
-
(E)-alpha-bisabolene is the precursor in Abies species of todomatuic acid, juvabione, and related insect juvenile hormone mimics, overview
-
?
(2E,6E)-farnesyl diphosphate
(E)-alpha-bisabolene + diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate
(E)-alpha-bisabolene + diphosphate
a step in the terpene synthesis pathway, overview
-
-
?
additional information
?
-
induced (E)-alpha-bisabolene biosynthesis constitutes part of a defense response targeted to insect herbivores, and possibly fungal pathogens, that is distinct from induced oleoresin monoterpene production
-
-
?
additional information
?
-
-
induced (E)-alpha-bisabolene biosynthesis constitutes part of a defense response targeted to insect herbivores, and possibly fungal pathogens, that is distinct from induced oleoresin monoterpene production
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
KCl
only weakly influences GDP conversion with the ag1 enzyme causing a 2fold activation at 100 mM KCl, but the monovalent cation has no effect with FDP as substrate
Mg2+
Mn2+
activates, but Mn2+ at concentrations higher than 1 mM results in a decline of activity with either substrate
additional information
Mg2+
activates, saturation with Mg2+ is reached at 5 mM, and no apparent inhibition of catalysis occurs up to 100 mM
additional information
the activity of recombinant ag1 requires a divalent cation cofactor, Mg2+ or Mn2+, which is employed to neutralize the negative charge of the diphosphate leaving group in the substrate ionization step of the reaction sequence. Mg2+ is more efficient in catalysis than is Mn2+. With GDP as substrate, however, Mn2+ at 0.5 mM yields a 4fold higher rate of monoterpene synthase activity compared to Mg2+ at concentrations up to 50 mM
additional information
-
the activity of recombinant ag1 requires a divalent cation cofactor, Mg2+ or Mn2+, which is employed to neutralize the negative charge of the diphosphate leaving group in the substrate ionization step of the reaction sequence. Mg2+ is more efficient in catalysis than is Mn2+. With GDP as substrate, however, Mn2+ at 0.5 mM yields a 4fold higher rate of monoterpene synthase activity compared to Mg2+ at concentrations up to 50 mM
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Mn2+
activates, but Mn2+ at concentrations higher than 1 mM results in a decline of activity with either substrate
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.01259
(2E,6E)-farnesyl diphosphate
at 30°C, pH not specified in the publication
0.0495
(2E,6E)-farnesyl diphosphate
in 25 mM Tris, 15 mM MgCl2, pH 7.5, at 30°C
0.07742
(2E,6E)-farnesyl diphosphate
pH 7.5, 22°C, recombinant His-tagged enzyme
additional information
additional information
Michaelis-Menten steady-state kinetics, the enzyme exhibits a hyperbolic FPP saturation kinetic plot
-
additional information
additional information
-
Michaelis-Menten steady-state kinetics, the enzyme exhibits a hyperbolic FPP saturation kinetic plot
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.002
(2E,6E)-farnesyl diphosphate
in 25 mM Tris, 15 mM MgCl2, pH 7.5, at 30°C
0.0067
(2E,6E)-farnesyl diphosphate
at 30°C, pH not specified in the publication
0.01
(2E,6E)-farnesyl diphosphate
pH 7.5, 22°C, recombinant His-tagged enzyme
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.038
(2E,6E)-farnesyl diphosphate
in 25 mM Tris, 15 mM MgCl2, pH 7.5, at 30°C
0.129
(2E,6E)-farnesyl diphosphate
pH 7.5, 22°C, recombinant His-tagged enzyme
0.5
(2E,6E)-farnesyl diphosphate
at 30°C, pH not specified in the publication
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
fresh, green, with needles, from 1-year-old rooted saplings
brenda
additional information
additional information
the highest GbTPS2 transcripts levels are observed in seedling root systems, which are approximately twofold higher than the levels observed in mature leaves. GbTPS2 transcript levels are substantially higher in these two tissues than all others analyzed, and the lowest levels are observed in mature seeds and stems
brenda
additional information
-
the highest GbTPS2 transcripts levels are observed in seedling root systems, which are approximately twofold higher than the levels observed in mature leaves. GbTPS2 transcript levels are substantially higher in these two tissues than all others analyzed, and the lowest levels are observed in mature seeds and stems
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
phylogenetic analysis reveals the two terpene synthase genes GbTPS1 and GbTPS2, encoding farnesol and bisabolene synthases, respectively, as primitive genes that might have evolved from an ancestral diterpene synthase. The enzyme belongs to the terpene synthase family, gymnosperm-specific TPSd subfamily, that further segregates into the TPSd1, TPSd2, and TPSd3 clades based on the phylogenetic analysis of 29 and 72 gymnosperm TPSs. The majority of gymnosperm sesquiterpene synthases fall within the TPSd2 clade
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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). TPS5_PSEAD
814
0
93272
Swiss-Prot
Chloroplast (Reliability: 4)
TPS8_HEDCO
591
0
68357
Swiss-Prot
Mitochondrion (Reliability: 5)
TPSD1_ABIGR
817
0
93749
Swiss-Prot
Chloroplast (Reliability: 4)
TPSD1_PSEMZ
66
0
8105
Swiss-Prot
other Location (Reliability: 5)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
apo form and bound to five inhibitors, sitting drop vapor diffusion method, using 100 mM Tris pH 8.5, 100 mM NaCl, and 23% (w/v) PEG 3350
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning from a cDNA library, DNA and amino acid sequence determination and analysis, sequence comparisons, functional expression in Escherichia coli strain BL21
-
expressed in Saccharomyces cerevisiae strain INVSc1 and Escherichia coli BL21 (DE) cells
expression of the enzyme under control of the potato proteinase inhibitor II pinII-promoter in Picea glauca seedlings, as well as in Arabidopsis thaliana and Nicotiana tabacum in a cell-specific manner in trichomes, expression analysis of theGUS-(E)-alpha-bisabolene synthase construct, overview
-
gene ag1, cloning from a wound-induced stem-cDNA library, DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic tree, functional expression in Escherichia coli strain XL1-Blue
gene PaTPS-Bis, DNA and amino acid sequence determination and analysis, expression and phylogenetic analysis, sequence comparison with other enzymes of the terpene synthase family, functional expression in Escherichia coli
gene TPS2, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression of C-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3), functional recombinant expression in Saccharomyces cerevisiae strain INVSc1
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Martin, D.M.; Faeldt, J.; Bohlmann, J.
Functional characterization of nine Norway spruce TPS genes and evolution of gymnosperm terpene synthases of the TPS-d subfamily
Plant Physiol.
135
1908-1927
2004
Picea abies (Q675L6), Picea abies
brenda
Huber, D.P.; Philippe, R.N.; Godard, K.A.; Sturrock, R.N.; Bohlmann, J.
Characterization of four terpene synthase cDNAs from methyl jasmonate-induced Douglas-fir, Pseudotsuga menziesii
Phytochemistry
66
1427-1439
2005
Pseudotsuga menziesii
brenda
Godard, K.A.; Byun-McKay, A.; Levasseur, C.; Plant, A.; Seguin, A.; Bohlmann, J.
Testing of a heterologous, wound- and insect-inducible promoter for functional genomics studies in conifer defense
Plant Cell Rep.
26
2083-2090
2007
Picea glauca
brenda
Bohlmann, J.; Crock, J.; Jetter, R.; Croteau, R.
Terpenoid-based defenses in conifers: cDNA cloning, characterization, and functional expression of wound-inducible (E)-alpha-bisabolene synthase from grand fir (Abies grandis)
Proc. Natl. Acad. Sci. USA
95
6756-6761
1998
Abies grandis (O81086), Abies grandis
brenda
McAndrew, R.P.; Peralta-Yahya, P.P.; DeGiovanni, A.; Pereira, J.H.; Hadi, M.Z.; Keasling, J.D.; Adams, P.D.
Structure of a three-domain sesquiterpene synthase: a prospective target for advanced biofuels production
Structure
19
1876-1884
2011
Abies grandis (O81086)
brenda
Parveen, I.; Wang, M.; Zhao, J.; Chittiboyina, A.G.; Tabanca, N.; Ali, A.; Baerson, S.R.; Techen, N.; Chappell, J.; Khan, I.A.; Pan, Z.
Investigating sesquiterpene biosynthesis in Ginkgo biloba molecular cloning and functional characterization of (E,E)-farnesol and alpha-bisabolene synthases
Plant Mol. Biol.
89
451-462
2015
Ginkgo biloba (A0A097SRT3), Ginkgo biloba
brenda
Srivastava, P.L.; Daramwar, P.P.; Krithika, R.; Pandreka, A.; Shankar, S.S.; Thulasiram, H.V.
Functional characterization of novel sesquiterpene synthases from indian sandalwood, Santalum album
Sci. Rep.
5
10095
2015
Santalum album (A0A0A0RDZ8), Santalum album
brenda
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