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Literature summary for 4.2.3.127 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
Search for more literature for 4.2.3.127

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant Cop4 in Escherichia coli strain JM109 Coprinopsis cinerea

Protein Variants

Protein Variants Comment Organism
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
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
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
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
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

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.011
-
 (2E,6E)-farnesyl diphosphate wild-type enzyme, and mutants H235P and N239L, pH 8.0, 30°C Coprinopsis cinerea
0.048
-
 (2E,6E)-farnesyl diphosphate Cop6 loop graft mutant Cop6L4, pH 8.0, 30°C Coprinopsis cinerea
0.0707
-
 (2E,6E)-farnesyl diphosphate mutant K233I, pH 8.0, 30°C Coprinopsis cinerea

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Coprinopsis cinerea
additional information the enzyme contains the metal-binding DDXXD motif Coprinopsis cinerea

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(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
-
 ?

Organism

Organism UniProt Comment Textmining
Coprinopsis cinerea A8NU13
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(2E,6E)-farnesyl diphosphate
-
 Coprinopsis cinerea beta-copaene + diphosphate
-
 ?
(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
-
 ?

Subunits

Subunits Comment Organism
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

Synonyms

Synonyms Comment Organism
Cop4
-
 Coprinopsis cinerea

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Coprinopsis cinerea

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
 Coprinopsis cinerea

pH Range

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

General Information

General Information Comment Organism
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