4.2.3.47: beta-farnesene synthase
This is an abbreviated version!
For detailed information about beta-farnesene synthase, go to the full flat file.
Word Map on EC 4.2.3.47
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4.2.3.47
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synthases
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terpenoids
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monoterpene
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diterpene
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geranyl
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linalool
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gpp
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herbivory
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scent
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fragrance
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limonene
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sesquiterpenoids
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germacrene
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carbocation
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sesterterpene
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myrcene
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herbivore-induced
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e-nerolidol
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e-beta-farnesene
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dimethylallyl
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1,8-cineole
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enemy
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sabinene
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5-epi-aristolochene
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bouquet
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ddxxd
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e,e-farnesyl
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pinene
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terpinolene
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agriculture
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multiproduct
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oleoresin
- 4.2.3.47
- synthases
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terpenoids
-
monoterpene
-
diterpene
-
geranyl
- linalool
- gpp
- herbivory
-
scent
-
fragrance
- limonene
- sesquiterpenoids
- germacrene
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carbocation
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sesterterpene
- myrcene
-
herbivore-induced
-
e-nerolidol
-
e-beta-farnesene
-
dimethylallyl
- 1,8-cineole
-
enemy
- sabinene
- 5-epi-aristolochene
-
bouquet
-
ddxxd
-
e,e-farnesyl
- pinene
- terpinolene
- agriculture
-
multiproduct
-
oleoresin
Reaction
Synonyms
(E)-alpha-farnesene synthase, (E)-beta-farnesene synthase, acyclic sesquiterpene synthase, betaFS, betaFS1, betaFS2, CJFS, EbetaF, EbetaF synthase, farnesene synthase, Os08g07100, sesquiterpene synthase, terpene synthase, terpene synthase 10, terpene synthase 10-B73, terpene synthase 10-per, terpene synthase T0, terpene synthase TPS10, TPS10, TPS10-dip, TPS5
ECTree
4.2.3.47 beta-farnesene synthaseAdvanced search results
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results (Engineering
Engineering on EC 4.2.3.47 - beta-farnesene synthase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
L405V
products are 1.9% 7-epi-sesquithujene, 8.1% (E)-alpha-bergamotene, 8.9% sesquiabinene A, 23.9% (E)-beta-farnesene, 0% gamma-curcumene, 9.7% zingiberene, 12.0% beta-bisabolene, 26.6% beta-sesquiphellandrene, 8.9% (E)-gamma-bisabolene
L405V/Y373S
products are 1.2% 7-epi-sesquithujene, 23.6% (E)-alpha-bergamotene, 17.7% sesquiabinene A, 53.0% (E)-beta-farnesene, 0% gamma-curcumene, 0.6% zingiberene, 1.3% beta-bisabolene, 2.6% beta-sesquiphellandrene, 0% (E)-gamma-bisabolene
Y373S
products are 7.6% 7-epi-sesquithujene, 24.8% (E)-alpha-bergamotene, 18.2% sesquiabinene A, 38.5% (E)-beta-farnesene, 0% gamma-curcumene, 4.7% zingiberene, 2.5% beta-bisabolene, 3.7% beta-sesquiphellandrene, 0% (E)-gamma-bisabolene
additional information
additional information
generation the two cross-convergent mutants, TPS10-B73 L356F and TPS10-dip F356L, by site-directed mutagenesis. The mutated enzymes are heterologously expressed, purified and assayed with the substrate (E,E)-farnesyl diphosphate. The mutant enzyme TPS10-B73 L356F produces less cyclic compounds than the wild type TPS10-B73 and has a product spectrum nearly identical to that of the wild type allele TPS10-dip which contains a phenylalanine at position 356. Conversely, the mutation of phenylalanine 356 to leucine in TPS10-dip results in a product profile dominated by (E)-alpha-bergamotene that is very similar to that of TPS10-B73. These results demonstrate that phenylalanine at position 356 is responsible for the decreased production of cyclic compounds in TPS10-dip and TPS10-per
additional information
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generation the two cross-convergent mutants, TPS10-B73 L356F and TPS10-dip F356L, by site-directed mutagenesis. The mutated enzymes are heterologously expressed, purified and assayed with the substrate (E,E)-farnesyl diphosphate. The mutant enzyme TPS10-B73 L356F produces less cyclic compounds than the wild type TPS10-B73 and has a product spectrum nearly identical to that of the wild type allele TPS10-dip which contains a phenylalanine at position 356. Conversely, the mutation of phenylalanine 356 to leucine in TPS10-dip results in a product profile dominated by (E)-alpha-bergamotene that is very similar to that of TPS10-B73. These results demonstrate that phenylalanine at position 356 is responsible for the decreased production of cyclic compounds in TPS10-dip and TPS10-per
additional information
generation the two cross-convergent mutants, TPS10-B73 L356F and TPS10-dip F356L, by site-directed mutagenesis. The mutated enzymes are heterologously expressed, purified and assayed with the substrate (E,E)-farnesyl diphosphate. The mutant enzyme TPS10-B73 L356F produces less cyclic compounds than the wild type TPS10-B73 and has a product spectrum nearly identical to that of the wild type allele TPS10-dip which contains a phenylalanine at position 356. Conversely, the mutation of phenylalanine 356 to leucine in TPS10-dip results in a product profile dominated by (E)-alpha-bergamotene that is very similar to that of TPS10-B73. These results demonstrate that phenylalanine at position 356 is responsible for the decreased production of cyclic compounds in TPS10-dip and TPS10-per
additional information
generation the two cross-convergent mutants, TPS10-B73 L356F and TPS10-dip F356L, by site-directed mutagenesis. The mutated enzymes are heterologously expressed, purified and assayed with the substrate (E,E)-farnesyl diphosphate. The mutant enzyme TPS10-B73 L356F produces less cyclic compounds than the wild type TPS10-B73 and has a product spectrum nearly identical to that of the wild type allele TPS10-dip which contains a phenylalanine at position 356. Conversely, the mutation of phenylalanine 356 to leucine in TPS10-dip results in a product profile dominated by (E)-alpha-bergamotene that is very similar to that of TPS10-B73. These results demonstrate that phenylalanine at position 356 is responsible for the decreased production of cyclic compounds in TPS10-dip and TPS10-per
additional information
generation the two cross-convergent mutants, TPS10-B73 L356F and TPS10-dip F356L, by site-directed mutagenesis. The mutated enzymes are heterologously expressed, purified and assayed with the substrate (E,E)-farnesyl diphosphate. The mutant enzyme TPS10-B73 L356F produces less cyclic compounds than the wild type TPS10-B73 and has a product spectrum nearly identical to that of the wild type allele TPS10-dip which contains a phenylalanine at position 356. Conversely, the mutation of phenylalanine 356 to leucine in TPS10-dip results in a product profile dominated by (E)-alpha-bergamotene that is very similar to that of TPS10-B73. These results demonstrate that phenylalanine at position 356 is responsible for the decreased production of cyclic compounds in TPS10-dip and TPS10-per
additional information
-
generation the two cross-convergent mutants, TPS10-B73 L356F and TPS10-dip F356L, by site-directed mutagenesis. The mutated enzymes are heterologously expressed, purified and assayed with the substrate (E,E)-farnesyl diphosphate. The mutant enzyme TPS10-B73 L356F produces less cyclic compounds than the wild type TPS10-B73 and has a product spectrum nearly identical to that of the wild type allele TPS10-dip which contains a phenylalanine at position 356. Conversely, the mutation of phenylalanine 356 to leucine in TPS10-dip results in a product profile dominated by (E)-alpha-bergamotene that is very similar to that of TPS10-B73. These results demonstrate that phenylalanine at position 356 is responsible for the decreased production of cyclic compounds in TPS10-dip and TPS10-per
additional information
generation the two cross-convergent mutants, TPS10-B73 L356F and TPS10-dip F356L, by site-directed mutagenesis. The mutated enzymes are heterologously expressed, purified and assayed with the substrate (E,E)-farnesyl diphosphate. The mutant enzyme TPS10-B73 L356F produces less cyclic compounds than the wild type TPS10-B73 and has a product spectrum nearly identical to that of the wild type allele TPS10-dip which contains a phenylalanine at position 356. Conversely, the mutation of phenylalanine 356 to leucine in TPS10-dip results in a product profile dominated by (E)-alpha-bergamotene that is very similar to that of TPS10-B73. These results demonstrate that phenylalanine at position 356 is responsible for the decreased production of cyclic compounds in TPS10-dip and TPS10-per
