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EC Tree
IUBMB Comments Requires Mg2+, Mn2+, Ni2+ or Co2+. The formation of (+)-germacrene D involves a 1,2-hydride shift whereas for (-)-germacrene D there is a 1,3-hydride shift (see EC 4.2.3.75).
The enzyme appears in viruses and cellular organisms
Synonyms
GDS, GDS1,
Sc11 , TPS2,
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(2E,6E)-farnesyl diphosphate = (+)-germacrene D + diphosphate
(2E,6E)-farnesyl diphosphate = (+)-germacrene D + diphosphate
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(2E,6E)-farnesyl diphosphate = (+)-germacrene D + diphosphate
the initial step is abstraction of the diphosphate moiety under ring closure to yield germacrenyl cation. The next step is a 1,2-hydride shift of H-7 into the isopropyl group, generating a germacrenyl cation with the positive charge at position 7. The cation undergoes a 1,2-hydride shift of H-6 yielding a cation with positive charge at position 6. During this step the configuration at C-7 is fixed. Finally, the cation is deprotonated at C-15 and the positive charge is quenched by two electron pair shifts to generate (+)-germacrene D
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2E,6E)-farnesyl-diphosphate diphosphate-lyase [(+)-germacrene-D-forming]
Requires Mg2+, Mn2+, Ni2+ or Co2+. The formation of (+)-germacrene D involves a 1,2-hydride shift whereas for (-)-germacrene D there is a 1,3-hydride shift (see EC 4.2.3.75).
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(2E,6E)-farnesyl diphosphate
(+)-germacrene D + diphosphate
additional information
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(2E,6E)-farnesyl diphosphate
(+)-germacrene D + diphosphate
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single product, exclusively synthesizes the (+)-configuration of germacrene D
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(2E,6E)-farnesyl diphosphate
(+)-germacrene D + diphosphate
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(2E,6E)-farnesyl diphosphate
(+)-germacrene D + diphosphate
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(2E,6E)-farnesyl diphosphate
(+)-germacrene D + diphosphate
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(2E,6E)-farnesyl diphosphate
(+)-germacrene D + diphosphate
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(2E,6E)-farnesyl diphosphate
(+)-germacrene D + diphosphate
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products are 50.2% (+)-germacrene D, 17.1% germacrene B, plus a number of minor products
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additional information
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no substrate: geranyl diphosphate
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additional information
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no substrate: geranyl diphosphate
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(2E,6E)-farnesyl diphosphate
(+)-germacrene D + diphosphate
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Co2+
1 mM, 33% of the activity with Mg2+
Ni2+
0.5 mM, 6% of the activity with Mg2+
Mg2+
preferred over Mn2+
Mg2+
required. Bi-dentate Mg2+-binding by residue 303 is not obligatory
Mg2+
maximum activity at 0.1 mM
Mn2+
43% of the maximal velocity in presence of Mg2+
Mn2+
0.1 mM, 24% of the activity with Mg2+
additional information
divalent cation required
additional information
divalent cation absolutely required, inactive with Cu2+ or Zn2+
additional information
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divalent cation absolutely required, inactive with Cu2+ or Zn2+
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0.0025 - 0.379
(2E,6E)-farnesyl diphosphate
0.0025
(2E,6E)-farnesyl diphosphate
pH 7.5, 30°C, presence of Mg2+
0.003
(2E,6E)-farnesyl diphosphate
25°C, pH not specified in the publication
0.379
(2E,6E)-farnesyl diphosphate
pH 7.8, 12°C
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0.017 - 0.04
(2E,6E)-farnesyl diphosphate
0.017
(2E,6E)-farnesyl diphosphate
pH 7.5, 30°C, presence of Mg2+
0.02
(2E,6E)-farnesyl diphosphate
25°C, pH not specified in the publication
0.04
(2E,6E)-farnesyl diphosphate
pH 7.8, 12°C
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6.7
(2E,6E)-farnesyl diphosphate
6.7
(2E,6E)-farnesyl diphosphate
25°C, pH not specified in the publication
6.7
(2E,6E)-farnesyl diphosphate
pH 7.5, 30°C, presence of Mg2+
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6.5 - 9
almost completely inactive below and above
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UniProt
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UniProt
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SwissProt
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SwissProt
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expression is significantly higher in flowers than in leaf tissue. Expression increases at 08.00 h and then drops to about a half by 20.00 h
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expression is significantly higher in flowers than in leaf tissue
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TSGD1_ZINOF
550
0
63755
Swiss-Prot
other Location (Reliability: 2 )
MTS17_SELML
348
0
38990
Swiss-Prot
Secretory Pathway (Reliability: 4 )
TPS8_MAIZE
539
0
62026
Swiss-Prot
other Location (Reliability: 3 )
FARS_MAIZE
533
0
61534
Swiss-Prot
other Location (Reliability: 3 )
A0A6B8N2N0_TAICR
576
0
66872
TrEMBL
other Location (Reliability: 2 )
A0A2P6PRW9_ROSCH
131
0
14947
TrEMBL
other Location (Reliability: 3 )
Q32W37_ACTDE
565
0
65180
TrEMBL
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Q70EZ6_9ASTR
551
0
65164
TrEMBL
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Q70EZ7_9ASTR
551
0
64803
TrEMBL
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60000
x * 63800, calculated, x * 60000, SDS-PAGE
63800
x * 63800, calculated, x * 60000, SDS-PAGE
64802
x * 64802, calculated
65200
x * 65200, calculated
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x * 65200, calculated
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x * 63800, calculated, x * 60000, SDS-PAGE
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N303D
mimicking of corresponding amino acid in (-)-germacrene D synthase Sc19. Kinetic data similar to wild-type
N303E
less than 0.25% of wild-type activity
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Agrobacterium tumefaciens-mediated expression in Nicotiana benthamiana
expressed in Escherichia coli
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expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
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analysis
use of NMR spectroscopy as a tool to analyze the kinetics of enzyme reactions using progress curves. The protocol presented is also a simple and direct approach for the measurement of enzyme kinetics in the presence of synthetic inhibitors. The conversion of farnesyl diphosphate into (+)-germacrene D by the enzyme germacrene D synthase involves an amphiphilic substrate forming micelles and a water insoluble product. Using proper controls, the conversion can well be analyzed by the progress curve approach using the Lambert W function
synthesis
improved conditions for expression of Zingiber officinale (+)-germacrene synthase in Escherichia coli. Comparison of bacterial strains; BL21 (DE3), BL21 (DE3) Tuner BL21(DE3) pLysS and BL21 (DE3) pLysS Tuner using different inducing agents. The change between BL21 (DE3) cells and BL21 (DE3) Tuner, induced with IPTG, leads to a twofold increase in enzyme activity in the soluble fraction while a reduction in activity is observed when using the pLysS strains. The same doubling of activity is observed for germacrene synthase when the commonly used BL.21 (DE3) is induced with The Inducer. Addition of 2.5 mM glycine betaine and 660 mM sorbitol to the bacterial growth media results in reduction of growth rate and biomass yield but under these conditions the best overall protein production is obtained
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Prosser, I.; Altug, I.G.; Phillips, A.L.; Koenig, W.A.; Bouwmeester, H.J.; Beale, M.H.
Enantiospecific (+)- and (-)-germacrene D synthases, cloned from goldenrod, reveal a functionally active variant of the universal isoprenoid-biosynthesis aspartate-rich motif
Arch. Biochem. Biophys.
432
136-144
2004
Solidago canadensis (Q70EZ7), Solidago canadensis
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Schmidt, C.O.; Bouwmeester, H.J.; Franke, S.; Konig, W.A.
Mechanisms of the biosynthesis of sesquiterpene enantiomers (+)- and (-)-germacrene D in Solidago canadensis
Chirality
11
353-362
1999
Solidago canadensis
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Picaud, S.; Olsson, M.E.; Brodelius, M.; Brodelius, P.E.
Cloning, expression, purification and characterization of recombinant (+)-germacrene D synthase from Zingiber officinale
Arch. Biochem. Biophys.
452
17-28
2006
Zingiber officinale (Q0VHD6), Zingiber officinale
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Picaud, S.; Olsson, M.E.; Brodelius, P.E.
Improved conditions for production of recombinant plant sesquiterpene synthases in Escherichia coli
Protein Expr. Purif.
51
71-79
2007
Zingiber officinale (Q0VHD6)
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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 (Q32W37)
brenda
Exnowitz, F.; Meyer, B.; Hackl, T.
NMR for direct determination of K(m) and V(max) of enzyme reactions based on the Lambert W function-analysis of progress curves
Biochim. Biophys. Acta
1824
443-449
2012
Solidago canadensis (Q70EZ6)
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Hattan, J.I.; Shindo, K.; Sasaki, T.; Misawa, N.
Isolation and functional characterization of new terpene synthase genes from traditional edible plants
J. Oleo Sci.
67
1235-1246
2018
Chengiopanax sciadophylloides
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History
Enzyme Nomenclature
4.2.3.77 (+)-germacrene D synthase
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