Difference between revisions of "Part:BBa K4759005"

Revision as of 16:41, 2 October 2023

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

Assembly Compatibility:

10
INCOMPATIBLE WITH RFC[10]
Illegal PstI site found at 281
Illegal PstI site found at 607
Illegal PstI site found at 922
12
INCOMPATIBLE WITH RFC[12]
Illegal PstI site found at 281
Illegal PstI site found at 607
Illegal PstI site found at 922
21
INCOMPATIBLE WITH RFC[21]
Illegal BglII site found at 1037
23
INCOMPATIBLE WITH RFC[23]
Illegal PstI site found at 281
Illegal PstI site found at 607
Illegal PstI site found at 922
25
INCOMPATIBLE 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
1000
COMPATIBLE WITH RFC[1000]

@@ Line 3: / Line 3: @@
 <partinfo>BBa_K4759005 short</partinfo>
 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 [3].
+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.