Leibniz Institute DSMZ
DSMZ Digital Diversity
Login
Classic view
All enzymes
Enzyme history
BRENDA support
Any feedback?
Please rate this page
(search_result.php)
😁
😐
😡
(
0
/150)
Send feedback
BRENDA support
Refine search
Search Protein Variants
Protein Variants:
show
10
50
100
results
Don't show organism specific information (fast!)
Search organism in taxonomic tree (slow, choose "exact" as search mode, e.g. "mammalia" for rat,human,monkey,...)
(Not possible to combine with the first option)
Refine your search
Recommended Name:
EC Number:
contains
exact
begins with
ends with
use * as joker
Commentary:
contains
exact
begins with
ends with
use * as joker
Organism
:
contains
exact
begins with
ends with
use * as joker
Reference:
contains
exact
begins with
ends with
use * as joker
Search term:
Results
1
-
2
of
2
download as CSV
download all results as CSV
EC Number
Protein Variants
Commentary
Reference
2.3.1.239
more
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
-
,
729589
2.3.1.239
more
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
-
,
729589
Results
1
-
2
of
2
download as CSV
download all results as CSV