Literature summary extracted from

  • Lopez-Gallego, F.; Wawrzyn, G.; Schmidt-Dannert, C.
    Selectivity of fungal sesquiterpene synthases: Role of the active sites H-1alpha loop in catalysis (2010), Appl. Environ. Microbiol., 76, 7723-7733.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.3.91 expressed in Escherichia coli strain JM109 or BL21 Coprinopsis cinerea
4.2.3.125 expression of wild-type and mutant Cop3 in Escherichia coli strain JM109 Coprinopsis cinerea
4.2.3.126 expression of wild-type and mutant Cop3s in Escherichia coli strain JM109 Coprinopsis cinerea
4.2.3.127 expression of wild-type and mutant Cop4 in Escherichia coli strain JM109 Coprinopsis cinerea
4.2.3.128 expression of wild-type and mutant enzymes in Escherichia coli strain JM109 Coprinopsis cinerea
4.2.3.129 expression of wild-type and mutant enzymes in Escherichia coli strain JM109 Coprinopsis cinerea

Engineering

EC Number Protein Variants Comment Organism
4.2.3.95 additional information in the Cop6 loop graft mutant Cop6L4, loop replacement has no influence on the selectivity of the enzyme for alpha-cuprenene, the mutation reduces the catalytic efficiency 3-17fold Coprinopsis cinerea
4.2.3.128 additional information directed mutations of the H-alpha1 loop have a marked effect on the product profile Cop4, loop mutations in Cop4 also implicate specific residues responsible for the pH sensitivity of the enzyme. H-alpha1 loop swap between Cop4 and Cop6 shifts Cop4 to a germacrene D synthase Coprinopsis cinerea
4.2.3.129 additional information directed mutations of the H-alpha1 loop have a marked effect on the product profile Cop4, loop mutations in Cop4 also implicate specific residues responsible for the pH sensitivity of the enzyme. H-alpha1 loop swap between Cop4 and Cop6 shifts Cop4 to a germacrene D synthase Coprinopsis cinerea
4.2.3.95 C236A the mutant produces 96% (-)-alpha-cuprenene, 3% gamma-cuprenene and 1% sesquiterpene products from (2E,6E)-farnesyl diphosphate (41.2% of wild type activity) Coprinopsis cinerea
4.2.3.91 H235P the mutant makes (-)-germacrene D as the major cyclization product and also synthesizes beta-ylangene not synthesized by wild-type Cop4 Coprinopsis cinerea
4.2.3.127 H235P site-directed mutagenesis, the mutation converts Cop4 into a much more selective enzyme that produces (-)-germacrene D as the major cyclization product with 50% of total sesquiterpenes products. The mutant makes beta-ylangene, which is a diastereomer of beta-copaene and not synthesized by wild-type Cop4 Coprinopsis cinerea
4.2.3.128 H235P site-directed mutagenesis, the mutation converts Cop4 into a much more selective enzyme that produces (-)-germacrene D as the major cyclization product with 50% of total sesquiterpenes products. The mutant makes beta-ylangene, which is a diastereomer of beta-copaene and not synthesized by wild-type Cop4 Coprinopsis cinerea
4.2.3.129 H235P site-directed mutagenesis, no production of sativene, the mutation converts Cop4 into a much more selective enzyme that produces (-)-germacrene D as the major cyclization product with 50% of total sesquiterpenes products. The mutant makes beta-ylangene, which is a diastereomer of beta-copaene and not synthesized by wild-type Cop4 Coprinopsis cinerea
4.2.3.91 N239L the mutant makes (-)-germacrene D as the major cyclization product and also synthesizes beta-ylangene not synthesized by wild-type Cop4 Coprinopsis cinerea
4.2.3.127 N239L site-directed mutagenesis, the mutation converts Cop4 into a much more selective enzyme that produces (-)-germacrene D as the major cyclization product with 50% of total sesquiterpenes products. The mutant makes beta-ylangene, which is a diastereomer of beta-copaene and not synthesized by wild-type Cop4 Coprinopsis cinerea
4.2.3.128 N239L site-directed mutagenesis, no production of beta-cubebene, the mutation converts Cop4 into a much more selective enzyme that produces (-)-germacrene D as the major cyclization product with 50% of total sesquiterpenes products. The mutant makes beta-ylangene, which is a diastereomer of beta-copaene and not synthesized by wild-type Cop4 Coprinopsis cinerea
4.2.3.129 N239L site-directed mutagenesis, no production of sativene, the mutation converts Cop4 into a much more selective enzyme that produces (-)-germacrene D as the major cyclization product with 50% of total sesquiterpenes products. The mutant makes beta-ylangene, which is a diastereomer of beta-copaene and not synthesized by wild-type Cop4 Coprinopsis cinerea
4.2.3.91 K233I the mutation has only a moderate effect on product selectivity Coprinopsis cinerea
4.2.3.127 K233I site-directed mutagenesis, the mutant shows a highly altered product profile compared to the wild-type enzyme with decrease in beta-copaene amounts. Cop4 loop mutant K2331 also becomes more selective for ()-germacrene D under acidic or basic reaction conditions, although less so than the wild-type enzyme Coprinopsis cinerea
4.2.3.128 K233I site-directed mutagenesis, mutation of K233, interacting with the second Asp92 in the DDXXD motif of Cop4, does not significantly change the overall product promiscuity of Cop4, though beta-cubebene 4 does become the major product Coprinopsis cinerea
4.2.3.129 K233I site-directed mutagenesis, mutation of K233, interacting with the second Asp92 in the DDXXD motif of Cop4, does not significantly change the overall product promiscuity of Cop4, though beta-cubebene 4 does become the major product and püroduction of sativene is reduced by 50% compared to the wild-type enzyme Coprinopsis cinerea
4.2.3.91 4L6 the mutant shows a 1000fold-decreased catalytic efficiency compared to the wild type enzyme Coprinopsis cinerea
4.2.3.95 E237L the mutant produces 96% (-)-alpha-cuprenene, 3% gamma-cuprenene and 1% unidentified sesquiterpene products from (2E,6E)-farnesyl diphosphate (59.4% of wild type activity) Coprinopsis cinerea
4.2.3.95 N240L the mutant produces 98% (-)-alpha-cuprenene and 2% gamma-cuprenene from (2E,6E)-farnesyl diphosphate (31% of wild type activity) Coprinopsis cinerea
4.2.3.125 H255P site-directed mutagenesis, modification of the H-alpha1 loop, the mutant shows highly altered product profile compared to the wild-type enzyme, it does no longer produce alpha-muurolene but large amounts of germacrene A (77%), overview Coprinopsis cinerea
4.2.3.126 H255P site-directed mutagenesis, modification of the H-alpha1 loop, the mutant shows highly altered product profile compared to the wild-type enzyme, it does no longer produce gamma-muurolene but large amounts of germacrene A (77%), overview Coprinopsis cinerea
4.2.3.125 K251I site-directed mutagenesis, modification of the H-alpha1 loop, the mutant shows only slightly altered product profile compared to the wild-type enzyme, it produces also beta-copaene, cf. EC 4.2.3.127, overview Coprinopsis cinerea
4.2.3.126 K251I site-directed mutagenesis, modification of the H-alpha1 loop, the mutant shows only slightly altered product profile compared to the wild-type enzyme, it produces also beta-copaene, cf. EC 4.2.3.127, overview Coprinopsis cinerea
4.2.3.127 T236L site-directed mutagenesis, the mutant shows a slightly altered product profile compared to the wild-type enzyme with increase in beta-copaene amounts Coprinopsis cinerea
4.2.3.128 T236L site-directed mutagenesis, the mutant shows a altered product profile compared to the wild-type enzyme with an increase in beta-cubebene synthesis. The mutant does no longer show production of cubebol and (-)-germacrene D compared to the wild-type enzyme Coprinopsis cinerea
4.2.3.129 T236L site-directed mutagenesis, the mutant shows a altered product profile compared to the wild-type enzyme with an increase in sativene synthesis. The mutant does no longer show production of cubebol and (-)-germacrene D compared to the wild-type enzyme Coprinopsis cinerea
4.2.3.127 N238L site-directed mutagenesis, the mutant shows a slightly altered product profile compared to the wild-type enzyme with increase in beta-copaene amounts Coprinopsis cinerea
4.2.3.128 N238L site-directed mutagenesis, the mutant shows a altered product profile compared to the wild-type enzyme with a slight reduction in beta-cubebene synthesis. The mutant does no longer show production of cubebol and has reduced (-)-germacrene D synthesis activity compared to the wild-type enzyme, synthesis of beta-cubebene, beta-copaene, delta-cadinene, and alpha-cubebene Coprinopsis cinerea
4.2.3.129 N238L site-directed mutagenesis, the mutant shows a altered product profile compared to the wild-type enzyme with only slight reduction in beta-cubebene synthesis, sativene levels are similar to the wild-type. The mutant does no longer show production of cubebol and has reduced (-)-germacrene D synthesis activity compared to the wild-type enzyme, synthesis of beta-cubebene, beta-copaene, delta-cadinene, and alpha-cubebene Coprinopsis cinerea

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.2.3.125 additional information
-
additional information steady-state kinetics, overview Coprinopsis cinerea
4.2.3.126 additional information
-
additional information steady-state kinetics, overview Coprinopsis cinerea
4.2.3.95 0.0125
-
(2E,6E)-farnesyl diphosphate mutant enzyme C236A, in 50 mM Tris-HCl, 10 mM MgCl2 (pH 8.0), at 30°C Coprinopsis cinerea
4.2.3.95 0.04
-
(2E,6E)-farnesyl diphosphate mutant enzyme N240L, in 50 mM Tris-HCl, 10 mM MgCl2 (pH 8.0), at 30°C Coprinopsis cinerea
4.2.3.127 0.011
-
(2E,6E)-farnesyl diphosphate wild-type enzyme, and mutants H235P and N239L, pH 8.0, 30°C Coprinopsis cinerea
4.2.3.128 0.011
-
(2E,6E)-farnesyl diphosphate wild-type enzyme, and mutants H235P and N239L, pH 8.0, 30°C Coprinopsis cinerea
4.2.3.129 0.011
-
(2E,6E)-farnesyl diphosphate wild-type enzyme, and mutants H235P and N239L, pH 8.0, 30° Coprinopsis cinerea
4.2.3.127 0.048
-
(2E,6E)-farnesyl diphosphate Cop6 loop graft mutant Cop6L4, pH 8.0, 30°C Coprinopsis cinerea
4.2.3.128 0.048
-
(2E,6E)-farnesyl diphosphate Cop6 loop graft mutant Cop6L4, pH 8.0, 30°C Coprinopsis cinerea
4.2.3.129 0.048
-
(2E,6E)-farnesyl diphosphate Cop6 loop graft mutant Cop6L4, pH 8.0, 30° Coprinopsis cinerea
4.2.3.95 0.0076
-
(2E,6E)-farnesyl diphosphate wild type enzyme, in 50 mM Tris-HCl, 10 mM MgCl2 (pH 8.0), at 30°C Coprinopsis cinerea
4.2.3.127 0.0707
-
(2E,6E)-farnesyl diphosphate mutant K233I, pH 8.0, 30°C Coprinopsis cinerea
4.2.3.128 0.0707
-
(2E,6E)-farnesyl diphosphate mutant K233I, pH 8.0, 30°C Coprinopsis cinerea
4.2.3.129 0.0707
-
(2E,6E)-farnesyl diphosphate mutant K233I, pH 8.0, 30° Coprinopsis cinerea
4.2.3.95 0.0136
-
(2E,6E)-farnesyl diphosphate mutant enzyme E237L, in 50 mM Tris-HCl, 10 mM MgCl2 (pH 8.0), at 30°C Coprinopsis cinerea

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.2.3.125 Mg2+ required Coprinopsis cinerea
4.2.3.125 additional information the enzyme contains the metal-binding DDXXD motif Coprinopsis cinerea
4.2.3.126 Mg2+ required Coprinopsis cinerea
4.2.3.127 Mg2+ required Coprinopsis cinerea
4.2.3.127 additional information the enzyme contains the metal-binding DDXXD motif Coprinopsis cinerea
4.2.3.128 Mg2+ required Coprinopsis cinerea
4.2.3.128 additional information the enzyme contains the metal-binding DDXXD motif Coprinopsis cinerea

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.3.125 additional information Coprinopsis cinerea seven different sesquiterpenes products, wild-type Cop3 also shows gamma-muurolene synthase activity, EC 4.2.3.126, and produces 12% gamma-muurolene and 35% gemacrene A, product of germacrene A synthase, EC 4.2.3.23, of total products from (2E,6E)-farnesyl diphosphate, product profiling by GC-MS analysis, overview ?
-
?
4.2.3.125 (2E,6E)-farnesyl diphosphate Coprinopsis cinerea the major cyclization products of Cop3 and its loop mutants are derived from an E,E-germacradienyl cation formed after ionization and 1,10 cyclization of E,E-farnesyl diphosphate. alpha-Muurolene is 30% of the products formed from (2E,6E)-farnesyl diphosphate alpha-muurolene + diphosphate
-
?
4.2.3.126 additional information Coprinopsis cinerea seven different sesquiterpenes products, wild-type Cop3 also shows alpha-muurolene synthase activity, EC 4.2.3.125, and produces 30% alpha-muurolene and 35% gemacrene A, product of germacrene A synthase, EC 4.2.3.23, of total products from (2E,6E)-farnesyl diphosphate, product profiling by GC-MS analysis, overview ?
-
?
4.2.3.126 (2E,6E)-farnesyl diphosphate Coprinopsis cinerea the major cyclization products of Cop3 and its loop mutants are derived from an E,E-germacradienyl cation formed after ionization and 1,10 cyclization of E,E-farnesyl diphosphate. alpha-Muurolene is 30% of the products formed from (2E,6E)-farnesyl diphosphate gamma-muurolene + diphosphate gamma-muurolene is 12% of the products formed from (2E,6E)-farnesyl diphosphate ?
4.2.3.127 (2E,6E)-farnesyl diphosphate Coprinopsis cinerea Cop4 produces 10 different sesquiterpene products with delta-cadinene and beta-copaene as the major products in vivo beta-copaene + diphosphate
-
?
4.2.3.128 (2E,6E)-farnesyl diphosphate Coprinopsis cinerea
-
beta-cubebene + diphosphate
-
?
4.2.3.129 (2E,6E)-farnesyl diphosphate Coprinopsis cinerea
-
(+)-sativene + diphosphate
-
?

Organism

EC Number Organism UniProt Comment Textmining
4.2.3.91 Coprinopsis cinerea
-
-
-
4.2.3.95 Coprinopsis cinerea
-
-
-
4.2.3.125 Coprinopsis cinerea
-
-
-
4.2.3.126 Coprinopsis cinerea
-
-
-
4.2.3.127 Coprinopsis cinerea A8NU13
-
-
4.2.3.128 Coprinopsis cinerea A8NU13
-
-
4.2.3.129 Coprinopsis cinerea A8NU13
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.3.91 additional information Cop4 rearranges a secondary cisoid, allylic cation derived from farnesyl diphophate after isomerization (cis-trans pathway of catalysis) into multiple products, with delta-cadinene and beta-copaene as the major products when expressed in Escherichia coli Coprinopsis cinerea ?
-
?
4.2.3.125 additional information seven different sesquiterpenes products, wild-type Cop3 also shows gamma-muurolene synthase activity, EC 4.2.3.126, and produces 12% gamma-muurolene and 35% gemacrene A, product of germacrene A synthase, EC 4.2.3.23, of total products from (2E,6E)-farnesyl diphosphate, product profiling by GC-MS analysis, overview Coprinopsis cinerea ?
-
?
4.2.3.126 additional information seven different sesquiterpenes products, wild-type Cop3 also shows alpha-muurolene synthase activity, EC 4.2.3.125, and produces 30% alpha-muurolene and 35% gemacrene A, product of germacrene A synthase, EC 4.2.3.23, of total products from (2E,6E)-farnesyl diphosphate, product profiling by GC-MS analysis, overview Coprinopsis cinerea ?
-
?
4.2.3.91 (2E,6E)-farnesyl diphosphate + H2O
-
Coprinopsis cinerea cubebol + diphosphate germacrene D and cubebol are the major products in vitro ?
4.2.3.95 (2E,6E)-farnesyl diphosphate
-
Coprinopsis cinerea (-)-alpha-cuprenene + diphosphate major product is (-)-alpha-cuprenene (98% yield) minor product is gamma-cuprenene (2% yield) ?
4.2.3.129 (2E,6E)-farnesyl diphosphate
-
Coprinopsis cinerea (+)-sativene + diphosphate
-
?
4.2.3.125 (2E,6E)-farnesyl diphosphate
-
Coprinopsis cinerea alpha-muurolene + diphosphate
-
?
4.2.3.125 (2E,6E)-farnesyl diphosphate the major cyclization products of Cop3 and its loop mutants are derived from an E,E-germacradienyl cation formed after ionization and 1,10 cyclization of E,E-farnesyl diphosphate. alpha-Muurolene is 30% of the products formed from (2E,6E)-farnesyl diphosphate Coprinopsis cinerea alpha-muurolene + diphosphate
-
?
4.2.3.127 (2E,6E)-farnesyl diphosphate
-
Coprinopsis cinerea beta-copaene + diphosphate
-
?
4.2.3.127 (2E,6E)-farnesyl diphosphate Cop4 produces 10 different sesquiterpene products with delta-cadinene and beta-copaene as the major products in vivo Coprinopsis cinerea beta-copaene + diphosphate
-
?
4.2.3.128 (2E,6E)-farnesyl diphosphate
-
Coprinopsis cinerea beta-cubebene + diphosphate
-
?
4.2.3.126 (2E,6E)-farnesyl diphosphate
-
Coprinopsis cinerea gamma-muurolene + diphosphate
-
?
4.2.3.126 (2E,6E)-farnesyl diphosphate the major cyclization products of Cop3 and its loop mutants are derived from an E,E-germacradienyl cation formed after ionization and 1,10 cyclization of E,E-farnesyl diphosphate. alpha-Muurolene is 30% of the products formed from (2E,6E)-farnesyl diphosphate Coprinopsis cinerea gamma-muurolene + diphosphate gamma-muurolene is 12% of the products formed from (2E,6E)-farnesyl diphosphate ?

Subunits

EC Number Subunits Comment Organism
4.2.3.125 More structural homology modeling of Cop3 using the crystal structure of aristolochene synthase from Aspergillus terreus. Several polar side chains in the H-alpha1 loops of Cop4 and Cop3 move closer to side chains in the metal-binding DDXXD motif Coprinopsis cinerea
4.2.3.126 More structural homology modeling of Cop3 using the crystal structure of aristolochene synthase from Aspergillus terreus. Several polar side chains in the H-alpha1 loops of Cop4 and Cop3 move closer to side chains in the metal-binding DDXXD motif Coprinopsis cinerea
4.2.3.127 More structural homology modeling of Cop4 using the crystal structure of aristolochene synthase from Aspergillus terreus. Several polar side chains in the H-alpha1 loops of Cop4 and Cop3 move closer to side chains in the metal-binding DDXXD motif Coprinopsis cinerea
4.2.3.128 More structure comparison, homology structural modeling of Cop enzymes, overview. Cop4 has a large active site cavity that undergoes substantial conformational change in the model upon ligand binding Coprinopsis cinerea
4.2.3.129 More structure comparison, homology structural modeling of Cop enzymes, overview. Cop4 has a large active site cavity that undergoes substantial conformational change in the model upon ligand binding Coprinopsis cinerea

Synonyms

EC Number Synonyms Comment Organism
4.2.3.91 Cop4
-
Coprinopsis cinerea
4.2.3.127 Cop4
-
Coprinopsis cinerea
4.2.3.128 Cop4
-
Coprinopsis cinerea
4.2.3.129 Cop4
-
Coprinopsis cinerea
4.2.3.125 Cop3
-
Coprinopsis cinerea
4.2.3.126 Cop3
-
Coprinopsis cinerea
4.2.3.95 Cop6
-
Coprinopsis cinerea
4.2.3.95 (-)-alpha-cuprenene synthase
-
Coprinopsis cinerea

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.2.3.125 30
-
assay at Coprinopsis cinerea
4.2.3.126 30
-
assay at Coprinopsis cinerea
4.2.3.127 30
-
assay at Coprinopsis cinerea
4.2.3.128 25 30 assay at Coprinopsis cinerea
4.2.3.129 25 30 assay at Coprinopsis cinerea

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.2.3.125 8
-
assay at Coprinopsis cinerea
4.2.3.126 8
-
assay at Coprinopsis cinerea
4.2.3.127 8
-
-
Coprinopsis cinerea
4.2.3.128 8
-
assay at Coprinopsis cinerea
4.2.3.129 8
-
about Coprinopsis cinerea

pH Range

EC Number pH Minimum pH Maximum Comment Organism
4.2.3.127 additional information
-
the product profile of the wild-type and mutant enzymes is highly dependent on the pH value, overview Coprinopsis cinerea
4.2.3.127 5 10 mutant enzymes N239L, H235P, and K233I Coprinopsis cinerea
4.2.3.127 8
-
wild-type enzyme Coprinopsis cinerea
4.2.3.128 5 10 mutant enzyme K233I Coprinopsis cinerea
4.2.3.128 8
-
wild-type enzyme and mutant H235P Coprinopsis cinerea

General Information

EC Number General Information Comment Organism
4.2.3.128 physiological function the enzyme belongs to the sesquiterpene synthases that are responsible for the cyclization of farnesyl diphosphate into a myriad of structurally diverse compounds with various biological activities Coprinopsis cinerea
4.2.3.129 physiological function the enzyme belongs to the sesquiterpene synthases that are responsible for the cyclization of farnesyl diphosphate into a myriad of structurally diverse compounds with various biological activities Coprinopsis cinerea
4.2.3.128 evolution the enzyme belongs to the sesquiterpene synthases Coprinopsis cinerea
4.2.3.129 evolution the enzyme belongs to the sesquiterpene synthases Coprinopsis cinerea
4.2.3.125 additional information role of the active site H-alpha1 loop in catalysis, overview Coprinopsis cinerea
4.2.3.126 additional information role of the active site H-alpha1 loop in catalysis, overview Coprinopsis cinerea
4.2.3.127 additional information the product profile of the wild-type and mutant enzymes is highly dependent on the pH value, the loop mutants show a much larger pH activity range, overview Coprinopsis cinerea
4.2.3.128 additional information directed mutations of the H-alpha1 loop have a marked effect on the product profile Cop4, loop mutations in Cop4 also implicate specific residues responsible for the pH sensitivity of the enzyme. In vivo analysis of sesquiterpene product profiles of H-alpha1 loop mutants, overview. Mutation of K233, presumed to interact with the second Asp92 in the DDXXD motif of Cop4, does not significantly change the overall product promiscuity of Cop4, though beta-cubebene, with 27% of total sesquiterpene products, does become the major product Coprinopsis cinerea
4.2.3.129 additional information directed mutations of the H-alpha1 loop have a marked effect on the product profile Cop4, loop mutations in Cop4 also implicate specific residues responsible for the pH sensitivity of the enzyme. In vivo analysis of sesquiterpene product profiles of H-alpha1 loop mutants, overview. Mutation of K233, presumed to interact with the second Asp92 in the DDXXD motif of Cop4, does not significantly change the overall product promiscuity of Cop4, though beta-cubebene, with 27% of total sesquiterpene products, does become the major product Coprinopsis cinerea

KCat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
4.2.3.95 21.3
-
(2E,6E)-farnesyl diphosphate mutant enzyme C236A, in 50 mM Tris-HCl, 10 mM MgCl2 (pH 8.0), at 30°C Coprinopsis cinerea
4.2.3.95 88
-
(2E,6E)-farnesyl diphosphate wild type enzyme, in 50 mM Tris-HCl, 10 mM MgCl2 (pH 8.0), at 30°C Coprinopsis cinerea
4.2.3.95 28.3
-
(2E,6E)-farnesyl diphosphate mutant enzyme E237L, in 50 mM Tris-HCl, 10 mM MgCl2 (pH 8.0), at 30°C Coprinopsis cinerea
4.2.3.95 5.246
-
(2E,6E)-farnesyl diphosphate mutant enzyme N240L, in 50 mM Tris-HCl, 10 mM MgCl2 (pH 8.0), at 30°C Coprinopsis cinerea