Difference between revisions of "Part:BBa K1978001"

 
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<partinfo>BBa_K1978001 short</partinfo>
 
<partinfo>BBa_K1978001 short</partinfo>
  
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The TorA-GlmS Biobrick consists of a TorA signal linked to GlmS, which is a vitamin B12 binding protein. The TorA signal sequence allows export of fully-folded proteins through the inner membrane via the TAT(Twin-Arginin)export system. This enables export of vitamin B12 out of the cell.
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<p align="justify">The TorA-GlmS Biobrick consists of a TorA signal sequence linked to GlmS, protein capable of binding vitamin B<sub>12</sub>. The TorA signal peptide allows export of fully-folded proteins through the inner membrane via the Tat (Twin-Arginine translocation) system. This construct thus enables export of vitamin B<sub>12</sub> bound to BtuF out of the cytoplasm.
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The TorA sequence codes for a peptide that harbours a twin-arginine motif. This is vital for the recognition by the Tat system. Moreover, an AxA motif is present, which leads to cleavage by the leader peptidase I (Palmer & Berks 2012).
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The TorA sequence codes for an amino-terminal signal peptide that harbours a twin-arginine motif which is vital for the recognition by the Tat system. The TorA signal sequence and the sequence coding for BtuF are connected by a linker of 15 bases, coding for the five amino acids following the signal peptide in trimethylamine-N-oxide reductase from <em>E.coli</em>.</p>
  
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MNNNDLFQASRRRFLAQLGGLTVAGMLGPSLLTPRRATA
 
  
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GlmS is the B12-binding subunit of glutamate mutase (Glm) from Clostridium cochlearium. The mechanism by which the enzyme uses adenosylcobalamin is highly similar to methylmalonyl coenzyme A mutase. Glm catalyzes the reversible rearrangement of (2S)-glutamate to (2S,3S)-3-methylaspartate (Leutbecher et al., 1992). The assembly of the active enzyme, an &#945;2&#946;2 tetramer, is mediated by coenzyme B12. While GlmS as the smaller subunit (14.8 kDa) binds B12, the larger subunit GlmE harbors the substrate binding site (Zelder et al., 1994).
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===Usage and Biology===
  
  
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===Usage and Biology===
 
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<span class='h3bb'>Sequence and Features</span>
 
<span class='h3bb'>Sequence and Features</span>
 
<partinfo>BBa_K1978001 SequenceAndFeatures</partinfo>
 
<partinfo>BBa_K1978001 SequenceAndFeatures</partinfo>

Revision as of 16:00, 20 October 2016


TorA-GlmS

The TorA-GlmS Biobrick consists of a TorA signal sequence linked to GlmS, protein capable of binding vitamin B12. The TorA signal peptide allows export of fully-folded proteins through the inner membrane via the Tat (Twin-Arginine translocation) system. This construct thus enables export of vitamin B12 bound to BtuF out of the cytoplasm. The TorA sequence codes for an amino-terminal signal peptide that harbours a twin-arginine motif which is vital for the recognition by the Tat system. The TorA signal sequence and the sequence coding for BtuF are connected by a linker of 15 bases, coding for the five amino acids following the signal peptide in trimethylamine-N-oxide reductase from E.coli.


Usage and Biology

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]