2.3.1.239: 10-deoxymethynolide synthase
This is an abbreviated version!
For detailed information about 10-deoxymethynolide synthase, go to the full flat file.
Word Map on EC 2.3.1.239
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2.3.1.239
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venezuelae
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macrolactone
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14-membered
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thioesterase
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narbonolide
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macrolide
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synthases
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6-deoxyerythronolide
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cyclization
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triketide
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hexaketide
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erythromycin
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n-acetylcysteamine
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macrocyclization
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te
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ketosynthase
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ketoreductase
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plasmid-based
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synthesis
- 2.3.1.239
- venezuelae
-
macrolactone
-
14-membered
-
thioesterase
- narbonolide
-
macrolide
- synthases
-
6-deoxyerythronolide
-
cyclization
-
triketide
-
hexaketide
- erythromycin
- n-acetylcysteamine
-
macrocyclization
- te
-
ketosynthase
- ketoreductase
-
plasmid-based
- synthesis
Reaction
+ 5 (2S)-methylmalonyl-CoA + 5 NADPH + 5 H+ = + 6 CoA + 6 CO2 + 5 NADP+ + 2 H2O
Synonyms
methymycin/picromycin polyketide synthase, picromycin/methymycin PKS, picromycin/methymycin polyketide synthase, PICS, PikAI, PikAIII, PikAIV, pikromycin PKS, pikromycin polyketide synthase, type I polyketide synthase PikAIV
ECTree
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Engineering
Engineering on EC 2.3.1.239 - 10-deoxymethynolide synthase
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additional information
multimodular separation can lead to only a modest decrease in the overall production of the final polyketide production. PikAI is a multimodular component of the pikromyin polyketide synthase and houses both the loading domain and the first two extension modules, joined by short intraprotein linkers. PikAI can be separated into two proteins at either of these linkers, only when matched pairs of docking domains from a heterologous modular phoslactomycin PKS are used in place of the intraprotein linker. In both cases the yields of pikromycin produced by the Streptomyces venezuelae mutant are 50% of that of a Streptomyces venezuelae strain expressing the native trimodular PikAI. Expression of module 2 as a monomodular protein fused to a heterologous N-terminal docking domain is also observed to give almost a tenfold improvement in the in vivo generation of pikromycin from a synthetic diketide intermediate
additional information
-
multimodular separation can lead to only a modest decrease in the overall production of the final polyketide production. PikAI is a multimodular component of the pikromyin polyketide synthase and houses both the loading domain and the first two extension modules, joined by short intraprotein linkers. PikAI can be separated into two proteins at either of these linkers, only when matched pairs of docking domains from a heterologous modular phoslactomycin PKS are used in place of the intraprotein linker. In both cases the yields of pikromycin produced by the Streptomyces venezuelae mutant are 50% of that of a Streptomyces venezuelae strain expressing the native trimodular PikAI. Expression of module 2 as a monomodular protein fused to a heterologous N-terminal docking domain is also observed to give almost a tenfold improvement in the in vivo generation of pikromycin from a synthetic diketide intermediate
additional information
PikAI is a multimodular component of the pikromyin polyketide synthase and houses both the loading domain and the first two extension modules, joined by short intraprotein linkers. PikAI can be separated into two proteins at either of these linkers, only when matched pairs of docking domains from a heterologous modular phoslactomycin polyketide synthase are used in place of the intraprotein linker. In both cases the yields of pikromycin produced by the Streptomyces venezuelae mutant are 50% of that of a Streptomyces venezuelae strain expressing the native trimodular PikAI. This observation provides evidence that such separations do not dramatically impact the efficiency of the entire in vivo biosynthetic process. Expression of module 2 as a monomodular protein fused to a heterologous N-terminal docking domain is also observed to give almost a tenfold improvement in the in vivo generation of pikromycin from a synthetic diketide intermediate. These results demonstrate the utility of docking domains to manipulate biosynthetic processes catalyzed by modular polyketide synthases and the quest to generate novel polyketide products
additional information
-
PikAI is a multimodular component of the pikromyin polyketide synthase and houses both the loading domain and the first two extension modules, joined by short intraprotein linkers. PikAI can be separated into two proteins at either of these linkers, only when matched pairs of docking domains from a heterologous modular phoslactomycin polyketide synthase are used in place of the intraprotein linker. In both cases the yields of pikromycin produced by the Streptomyces venezuelae mutant are 50% of that of a Streptomyces venezuelae strain expressing the native trimodular PikAI. This observation provides evidence that such separations do not dramatically impact the efficiency of the entire in vivo biosynthetic process. Expression of module 2 as a monomodular protein fused to a heterologous N-terminal docking domain is also observed to give almost a tenfold improvement in the in vivo generation of pikromycin from a synthetic diketide intermediate. These results demonstrate the utility of docking domains to manipulate biosynthetic processes catalyzed by modular polyketide synthases and the quest to generate novel polyketide products
additional information
-
multimodular separation can lead to only a modest decrease in the overall production of the final polyketide production. PikAI is a multimodular component of the pikromyin polyketide synthase and houses both the loading domain and the first two extension modules, joined by short intraprotein linkers. PikAI can be separated into two proteins at either of these linkers, only when matched pairs of docking domains from a heterologous modular phoslactomycin PKS are used in place of the intraprotein linker. In both cases the yields of pikromycin produced by the Streptomyces venezuelae mutant are 50% of that of a Streptomyces venezuelae strain expressing the native trimodular PikAI. Expression of module 2 as a monomodular protein fused to a heterologous N-terminal docking domain is also observed to give almost a tenfold improvement in the in vivo generation of pikromycin from a synthetic diketide intermediate
-
additional information
-
PikAI is a multimodular component of the pikromyin polyketide synthase and houses both the loading domain and the first two extension modules, joined by short intraprotein linkers. PikAI can be separated into two proteins at either of these linkers, only when matched pairs of docking domains from a heterologous modular phoslactomycin polyketide synthase are used in place of the intraprotein linker. In both cases the yields of pikromycin produced by the Streptomyces venezuelae mutant are 50% of that of a Streptomyces venezuelae strain expressing the native trimodular PikAI. This observation provides evidence that such separations do not dramatically impact the efficiency of the entire in vivo biosynthetic process. Expression of module 2 as a monomodular protein fused to a heterologous N-terminal docking domain is also observed to give almost a tenfold improvement in the in vivo generation of pikromycin from a synthetic diketide intermediate. These results demonstrate the utility of docking domains to manipulate biosynthetic processes catalyzed by modular polyketide synthases and the quest to generate novel polyketide products
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