Difference between revisions of "Part:BBa K4759008"

Latest revision as of 08:03, 10 October 2023

petF

petF codes for ferredoxin, an important electron donor in Synechocystis that mainly works to be the final electron acceptor in the electron transport chain during photosynthesis. The P450 enzymes are redox-dependent proteins that source electrons from reducing cofactors to drive their activities.

Usage and Biology

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

Assembly Compatibility:

10
COMPATIBLE WITH RFC[10]
12
COMPATIBLE WITH RFC[12]
21
COMPATIBLE WITH RFC[21]
23
COMPATIBLE WITH RFC[23]
25
COMPATIBLE WITH RFC[25]
1000
COMPATIBLE WITH RFC[1000]

@@ Line 1: / Line 1: @@
 __NOTOC__
-<partinfo>BBa_K4759003 short</partinfo>
+<partinfo>BBa_K4759008 short</partinfo>
-petF codes for ferredoxin, an important electron donor in Synechocystis that is mainly
+petF codes for ferredoxin, an important electron donor in Synechocystis that mainly
 works to be the final electron acceptor in the electron transport chain during photosynthesis.
-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
+The P450 enzymes are redox-dependent proteins that source electrons from reducing cofactors to drive their activities.
-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.
-<!-- Add more about the biology of this part here
 ===Usage and Biology===
+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.
 <!-- -->