Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 4.2.3.125 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)

Cloned (Comment) Organism
expression of wild-type and mutant Cop3 in Escherichia coli strain JM109 Coprinopsis cinerea

Protein Variants

Protein Variants Comment Organism
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
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

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information steady-state kinetics, overview 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 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
-
?
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 ?
-
?

Organism

Organism UniProt Comment Textmining
Coprinopsis cinerea
-
-
-

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
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

Synonyms

Synonyms Comment Organism
Cop3
-
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
-
assay at Coprinopsis cinerea

General Information

General Information Comment Organism
additional information role of the active site H-alpha1 loop in catalysis, overview Coprinopsis cinerea