4.2.3.146: cyclooctat-9-en-7-ol synthase
This is an abbreviated version!
For detailed information about cyclooctat-9-en-7-ol synthase, go to the full flat file.
Word Map on EC 4.2.3.146
Reaction
Synonyms
cetB2, CotB2, CYC, diterpene cyclooctatin synthase
ECTree
4.2.3.146 cyclooctat-9-en-7-ol synthaseAdvanced search results
results (
results (Engineering
Engineering on EC 4.2.3.146 - cyclooctat-9-en-7-ol synthase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
F107A
F107G
the mutant enzyme produces cembrene A as single cyclization product
F107L
site-directed mutagenesis, the mutant follows a different reaction mechanism compared to wild-type and produces the different products 3,7-dolabellatriene-9-ol and cyclooctat-6-en-8-ol in addition to cyclooctat-9-en-7-ol
F107Y
F149H
the mutant enzyme produces a single cyclization product
F149L
F149V
the mutant enzyme produces a single cyclization product
F185A
site-directed mutagenesis, the mutant follows a different reaction mechanism compared to wild-type and produces the different products 3,7-dolabellatriene-9-ol and cyclooctat-6-en-8-ol in addition to cyclooctat-9-en-7-ol
N103A
site-directed mutagenesis, the mutant follows a different reaction mechanism compared to wild-type and produces the different product 3,7,12-dolabellatriene instead of cyclooctat-9-en-7-ol
W186F
site-directed mutagenesis, the mutant follows a different reaction mechanism compared to wild-type and produces the different products 3,7-dolabellatriene-9-ol and cyclooctat-6-en-8-ol in addition to cyclooctat-9-en-7-ol
W186H
site-directed mutagenesis, the mutant follows a different reaction mechanism compared to wild-type and produces the different product 3,7,18-dolabellatriene instead of cyclooctat-9-en-7-ol
W186L
site-directed mutagenesis, the mutant follows a different reaction mechanism compared to wild-type and produces the different products cembrane A and 3,7,18-dolabellatriene and only low amounts of cyclooctat-9-en-7-ol
W288G
F107A
F107G
-
the mutant enzyme produces cembrene A as single cyclization product
-
F107L
-
site-directed mutagenesis, the mutant follows a different reaction mechanism compared to wild-type and produces the different products 3,7-dolabellatriene-9-ol and cyclooctat-6-en-8-ol in addition to cyclooctat-9-en-7-ol
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F107Y
F149L
F149V
-
the mutant enzyme produces a single cyclization product
-
N103A
-
site-directed mutagenesis, the mutant follows a different reaction mechanism compared to wild-type and produces the different product 3,7,12-dolabellatriene instead of cyclooctat-9-en-7-ol
-
W186F
-
site-directed mutagenesis, the mutant follows a different reaction mechanism compared to wild-type and produces the different products 3,7-dolabellatriene-9-ol and cyclooctat-6-en-8-ol in addition to cyclooctat-9-en-7-ol
-
W288G
additional information
F107A
mutation results in the formation of a monocyclic cembrene, which structurally bears no resemblance to the parent compound cyclooctat-9-en-7-ol
F107A
site-directed mutagenesis, the mutant follows a different reaction mechanism compared to wild-type and produces the different product cembrane A in addition to cyclooctat-9-en-7-ol
F107Y
site-directed mutagenesis, the mutant follows a different reaction mechanism compared to wild-type and produces the different product cyclooctat-1,7-diene
F149L
cyclisation of geranylgeranyl diphosphate by the the mutant enzyme results in the formation of the non-natural fusicoccane macrocycle cyclooctat-7-en-3-ol
F149L
site-directed mutagenesis, the mutant follows a different reaction mechanism compared to wild-type and produces the different product cyclooctat-7-en-3-ol, no formation of cyclooctat-9-en-7-ol
W288G
site-directed mutagenesis, the mutant follows a different reaction mechanism compared to wild-type and produces the different product 3,7,18-dolabellatriene
W288G
site-directed mutagenesis, the mutant produces (1R,3E,7E,11S,12S)-3,7,18-dolabellatriene instead of the native product cyclooctat-9-en-7-ol. In vivo CotB2 W288G reconstitution in an Escherichia coli based terpene production system, allows efficient production of this olefinic macrocycle
F107A
-
site-directed mutagenesis, the mutant follows a different reaction mechanism compared to wild-type and produces the different product cembrane A in addition to cyclooctat-9-en-7-ol
-
F107A
-
mutation results in the formation of a monocyclic cembrene, which structurally bears no resemblance to the parent compound cyclooctat-9-en-7-ol
-
F107Y
-
site-directed mutagenesis, the mutant follows a different reaction mechanism compared to wild-type and produces the different product cyclooctat-1,7-diene
-
F149L
-
site-directed mutagenesis, the mutant follows a different reaction mechanism compared to wild-type and produces the different product cyclooctat-7-en-3-ol, no formation of cyclooctat-9-en-7-ol
-
F149L
-
cyclisation of geranylgeranyl diphosphate by the the mutant enzyme results in the formation of the non-natural fusicoccane macrocycle cyclooctat-7-en-3-ol
-
W288G
-
site-directed mutagenesis, the mutant follows a different reaction mechanism compared to wild-type and produces the different product 3,7,18-dolabellatriene
-
W288G
-
site-directed mutagenesis, the mutant produces (1R,3E,7E,11S,12S)-3,7,18-dolabellatriene instead of the native product cyclooctat-9-en-7-ol. In vivo CotB2 W288G reconstitution in an Escherichia coli based terpene production system, allows efficient production of this olefinic macrocycle
-
additional information
epoxidation of product (1R,3E,7E,11S,12S)-3,7,18-dolabellatriene from mutant CotB2 W288G by acetic peracid, which is formed in situ by a lipase catalyzed reaction of acetic acid with H2O2, provides efficient access to two monooxidized dolabellanes and to a di-epoxidated dolabellane species. These compounds might act as synthons en-route to other dolabellanes with diversified bioactivities. Almost quantitative 3,7,18-dolabellatriene conversion into the non-natural compound (1R,3E,7E,11S,12S,18R)-dolabella-3,7-diene-20-ol by hydroboration-oxidation with an enantiomeric excess of 94%. Molecular docking of (1R,3E,7E,11S,12S)-3,7,18-dolabellatriene in the P450BM3_F87A and P450BM3_F87A/A328L active site of hydroxylase P450BM3 derived from Bacillus megaterium
additional information
mutational analysis of the atypical aspartate-rich motif of CotB2. Proposed cyclization mechanism for CotB2 and its mutants, overview
additional information
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mutational analysis of the atypical aspartate-rich motif of CotB2. Proposed cyclization mechanism for CotB2 and its mutants, overview
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additional information
-
epoxidation of product (1R,3E,7E,11S,12S)-3,7,18-dolabellatriene from mutant CotB2 W288G by acetic peracid, which is formed in situ by a lipase catalyzed reaction of acetic acid with H2O2, provides efficient access to two monooxidized dolabellanes and to a di-epoxidated dolabellane species. These compounds might act as synthons en-route to other dolabellanes with diversified bioactivities. Almost quantitative 3,7,18-dolabellatriene conversion into the non-natural compound (1R,3E,7E,11S,12S,18R)-dolabella-3,7-diene-20-ol by hydroboration-oxidation with an enantiomeric excess of 94%. Molecular docking of (1R,3E,7E,11S,12S)-3,7,18-dolabellatriene in the P450BM3_F87A and P450BM3_F87A/A328L active site of hydroxylase P450BM3 derived from Bacillus megaterium
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