Difference between revisions of "Part:BBa K4759005"
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<partinfo>BBa_K4759005 short</partinfo> | <partinfo>BBa_K4759005 short</partinfo> | ||
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− | + | This is a ferredoxin reductase from Synechococcus elongates PCC7942 | |
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===Usage and Biology=== | ===Usage and Biology=== | ||
+ | The P450 enzymes are redox-dependent proteins that source electrons from reducing cofactors to drive their activities. In bacterial systems, the electrostatic interactions | ||
+ | between the ferredoxin (Fdx), P450 heme, and the reductase domains, as well as the negatively and positively charged amino acids on the Fdx iron-sulfur cluster and P450 proximal site, mediate the conformational changes of the Fdx for electron transfer to P450s. In addition, the substrate binding to P450 induces P450 conformational change to increase its preference for Fdx through electrostatic and steric complementarity. | ||
+ | Optimizing protein-to-protein interactions using different methods to improve the electron transfer efficiency of the P450 system, known as "redox chaperone engineering", is one of the important means of engineering P450s, and fruitful progress has been made. | ||
+ | Several studies have confirmed that the combined expression of P450, an enzyme with different RPs can reconstruct and promote reactivity. This strategy has been widely used in the bacterial class I P450 system. | ||
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Latest revision as of 07:47, 10 October 2023
Fdr_0978
This is a ferredoxin reductase from Synechococcus elongates PCC7942
Usage and Biology
The P450 enzymes are redox-dependent proteins that source electrons from reducing cofactors to drive their activities. In bacterial systems, the electrostatic interactions between the ferredoxin (Fdx), P450 heme, and the reductase domains, as well as the negatively and positively charged amino acids on the Fdx iron-sulfur cluster and P450 proximal site, mediate the conformational changes of the Fdx for electron transfer to P450s. In addition, the substrate binding to P450 induces P450 conformational change to increase its preference for Fdx through electrostatic and steric complementarity. Optimizing protein-to-protein interactions using different methods to improve the electron transfer efficiency of the P450 system, known as "redox chaperone engineering", is one of the important means of engineering P450s, and fruitful progress has been made. Several studies have confirmed that the combined expression of P450, an enzyme with different RPs can reconstruct and promote reactivity. This strategy has been widely used in the bacterial class I P450 system.
Sequence and Features
- 10INCOMPATIBLE WITH RFC[10]Illegal PstI site found at 281
Illegal PstI site found at 607
Illegal PstI site found at 922 - 12INCOMPATIBLE WITH RFC[12]Illegal PstI site found at 281
Illegal PstI site found at 607
Illegal PstI site found at 922 - 21INCOMPATIBLE WITH RFC[21]Illegal BglII site found at 1037
- 23INCOMPATIBLE WITH RFC[23]Illegal PstI site found at 281
Illegal PstI site found at 607
Illegal PstI site found at 922 - 25INCOMPATIBLE WITH RFC[25]Illegal PstI site found at 281
Illegal PstI site found at 607
Illegal PstI site found at 922
Illegal NgoMIV site found at 625
Illegal AgeI site found at 697 - 1000COMPATIBLE WITH RFC[1000]