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

BRENDA support

Literature summary for 4.2.3.127 extracted from

  • Lopez-Gallego, F.; Agger, S.A.; Abate-Pella, D.; Distefano, M.D.; Schmidt-Dannert, C.
    Sesquiterpene synthases Cop4 and Cop6 from Coprinus cinereus: catalytic promiscuity and cyclization of farnesyl pyrophosphate geometric isomers (2010), ChemBioChem, 11, 1093-1106.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.2.3.127

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ dependent on, two consensus sequences - an aspartate rich DDXXD/E and a NSE/DTE motif - located at the entrance of the active site coordinate a trinuclear Mg2+ cluster. In reactions where Mg2+ is replaced with either Mn2+ or K+ is the disappearance of beta-copaene Coprinopsis cinerea
additional information in presence of the divalent cation Mn2+, Cop4 favors a reaction path that ends after one cyclization in (-)-germacrene D 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
-
 beta-copaene + diphosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Coprinopsis cinerea A8NU13
-
-

Reaction

Reaction Comment Organism Reaction ID
(2E,6E)-farnesyl diphosphate = beta-copaene + diphosphate cyclization reaction mechanism, overview Coprinopsis cinerea
a

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 conversion of (E,E)-farnesyl diphosphate proceeds via an (E,E)-germacradienyl carbocation in the case of Cop4. Cyclization of all-trans-farnesyl diphosphate compared to the cyclization of the cis-trans isomer of farnesyl diphosphate serving as a surrogate for the secondary cisoid neryl cation intermediate generated by sesquiterpene synthases capable of isomerizing the C2-C3 bond of all-trans-farnesyl diphosphate. (Z,E)-FPP is cyclized via a (6S)-beta-bisabolene carbocation by Cop4 Coprinopsis cinerea beta-copaene + diphosphate
-
 ?
(E)-geranyl diphosphate the enzyme accepts (E)-geranyl diphosphate as a substrate, but the catalytic efficiency with the shorter prenyl-diphosphate substrate is lower compared to their longer farnesyl diphosphate substrate Coprinopsis cinerea ?
-
 ?
additional information Cop4 is a catalytically promiscuous enzyme that cyclizes (E,E)-farnesyl diphosphate into multiple products, including (-)-germacrene D and cubebol. But changing the pH of the reaction drastically alters the fidelity of Cop4 and makes it a highly selective enzyme Coprinopsis cinerea ?
-
 ?

Subunits

Subunits Comment Organism
More structural homology modeling, hydrogen bond interactions and metal ion coordination in the diphosphate bound closed conformation of the Cop models, overview Coprinopsis cinerea

Synonyms

Synonyms Comment Organism
Cop4
-
 Coprinopsis cinerea
sesquiterpene synthase
-
 Coprinopsis cinerea

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
additional information
-
 lowering the reaction temperature from 25°C to 4°C increases the selectivity of Cop4 for (-)-germacrene D. Increasing the reaction temperature to 37°C has the opposite effect and decreases the fidelity of Cop4. At this temperature Cop4 generates a relative larger fraction of products beta-cubebene, sativene delta-cadinene, and beta-copaene that are derived from a cadinyl cation intermediate Coprinopsis cinerea

pH Range

pH Minimum pH Maximum Comment Organism
additional information
-
 changing the pH of the reaction drastically alters the fidelity of Cop4 and makes it a highly selective enzyme Coprinopsis cinerea