Part:BBa_K4759005
Fdr_0978
The P450 enzymes are redox-dependent proteins, through which they 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, enzyme with different RPs can achieve the reconstruction and promotion of reactivity. This strategy has been widely used in the bacterial class I P450 system. ferredoxin reductase from Synechococcus elongates PCC7942
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]
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