Difference between revisions of "Part:BBa K4140010"

(Usage)
(Literature Characterization)
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PheP, an intrinsic membrane transporter that employs the proton motive force to antiport L-phenylalanine and L-tyrosine, naturally transports phenylalanine across membranes via phenylalanine-specific permease. We employ the component to increase the intracellular concentration of phenylalanine, which improves the permeability of cells to phenylalanine and triggers our circuit to express PAH
 
PheP, an intrinsic membrane transporter that employs the proton motive force to antiport L-phenylalanine and L-tyrosine, naturally transports phenylalanine across membranes via phenylalanine-specific permease. We employ the component to increase the intracellular concentration of phenylalanine, which improves the permeability of cells to phenylalanine and triggers our circuit to express PAH
  
==Literature Characterization==
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==Characterization of Mutational Landscape==
  
[[File:T--AFCM-EGYPT--CAS2.PNG|thumb|Right|Figure 1.Substrate RNA cleavage assay using wild-type and mutant target RNAs. ]]
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After creating a multiple sequence alignment of the protein sequence and predicting mutational landscapes, the effect of these mutations on the evolutionary fitness of the protein is tested. The prediction of the mutational landscape by saturation mutagenesis of the premease protein. The (H37K) mutation, as depicted in the chart, had the greatest score when compared to other mutations. On the other hand, it's clear that the (A153L) had the least evolutionary fitness for premease protein. As displayed in Figure(1)
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[[File:Permease.png|thumb|Right|Figure 1. (shows the mutational landscape of the Permease protein.) ]]
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==References==
 
==References==

Revision as of 11:44, 3 October 2022


Permease


Part Description

The bacterium Escherichia coli naturally transports phenylalanine across membranes via PheP (Phenylalanine-specific permease). PheP is a single, integral membrane transporter that uses the proton motive force to antiport L-phenylalanine and L-tyrosine. This transporter's activity under natural expression is known to range between 9 and 17,5.

Usage

PheP, an intrinsic membrane transporter that employs the proton motive force to antiport L-phenylalanine and L-tyrosine, naturally transports phenylalanine across membranes via phenylalanine-specific permease. We employ the component to increase the intracellular concentration of phenylalanine, which improves the permeability of cells to phenylalanine and triggers our circuit to express PAH

Characterization of Mutational Landscape

After creating a multiple sequence alignment of the protein sequence and predicting mutational landscapes, the effect of these mutations on the evolutionary fitness of the protein is tested. The prediction of the mutational landscape by saturation mutagenesis of the premease protein. The (H37K) mutation, as depicted in the chart, had the greatest score when compared to other mutations. On the other hand, it's clear that the (A153L) had the least evolutionary fitness for premease protein. As displayed in Figure(1)

Figure 1. (shows the mutational landscape of the Permease protein.)

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References

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    INCOMPATIBLE WITH RFC[12]
    Illegal NheI site found at 37
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]