4.2.3.129: (+)-sativene synthase
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For detailed information about (+)-sativene synthase, go to the full flat file.
Reaction
Synonyms
Cop4, sesquiterpene synthase
ECTree
4.2.3.129 (+)-sativene synthaseAdvanced search results
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Engineering on EC 4.2.3.129 - (+)-sativene synthase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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
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
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
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
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
additional information
additional information
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generation of a cop4 defective mutant and a cop4/cop1 double mutant
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
