Difference between revisions of "Part:BBa K731000"
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CysE is an enzyme involved in cysteine biosynthesis, also known as SAT. It catalyzes the acetylation of serine to give O-acetylserine, a precursor for the biosynthesis of cysteine. Some O-acetylserine is also converted to N-acetylserine, which in turn triggers the assimilation of sulfate through specific genes.
 
CysE is an enzyme involved in cysteine biosynthesis, also known as SAT. It catalyzes the acetylation of serine to give O-acetylserine, a precursor for the biosynthesis of cysteine. Some O-acetylserine is also converted to N-acetylserine, which in turn triggers the assimilation of sulfate through specific genes.
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<p>This part has been successfully operated while controlled by araC-pBAD both in pSB1C3 (<a href="https://parts.igem.org/Part:BBa_K731020">K731020</a>) and the low copy vector pSB3C5, in which it was characterized.<br/>
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This part was cloned by the iGEM Trento 2012 team for the creation of an aerobically engineered pathway for the removal of the black crust disfiguring marble stones. Further information about this part and its characterization can be found in the <a href="http://2012.igem.org/Team:UNITN-Trento">iGEM Trento 2012 wiki</a>.</p>
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===Usage and Biology===
 
===Usage and Biology===
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<p>In <em>Escherichia coli</em> conversion of L-serine to L-cysteine is mediated by the action of two enzymes: serine acetyltransferase <a href="#fn:1" id="fnref:1" title="see footnote" class="footnote">[1]</a> catalyses the activation of L-serine by acetyl-CoA. Its product, 0-acetyl-L-serine (OAS), is then subsequently converted to L-cysteine by 0-acetyl-L-serine(thio1)lyase.<br/>
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The synthesis of OAS-(thio1)-lyase and of the enzymes involved in sulphate uptake and reduction is regulated by induction as well as by repression <a href="#fn:2" id="fnref:2" title="see footnote" class="footnote">[2]</a>.
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The expression of cysE (the SAT structural gene), on the other hand, is constitutive whereas the catalytic activity of the gene product, SAT, is sensitive to feedback inhibition by L-cysteine <a href="#fn:3" id="fnref:3" title="see footnote" class="footnote">[3]</a>.</p>
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<h3 style="text-align:center; margin-bottom:10px">Please head over to <a href="https://parts.igem.org/Part:BBa_K731020">K731020</a> for documentation on characterization of this Part.</h3>
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<p>EC 2.3.1.30 <a href="#fnref:1" title="return to article" class="reversefootnote">&#160;&#8617;</a></p>
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<p>Jones-Mortimer, 1968; Jones-Mortimer et al., 1968; Kredich, 1971. <a href="#fnref:2" title="return to article" class="reversefootnote">&#160;&#8617;</a></p>
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<p>Kredich &amp; Tomkins, 1966. <a href="#fnref:3" title="return to article" class="reversefootnote">&#160;&#8617;</a></p>
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<span class='h3bb'>Sequence and Features</span>
 
<span class='h3bb'>Sequence and Features</span>

Revision as of 10:21, 16 September 2012

CysE (Serine Acetyltransferase)

CysE is an enzyme involved in cysteine biosynthesis, also known as SAT. It catalyzes the acetylation of serine to give O-acetylserine, a precursor for the biosynthesis of cysteine. Some O-acetylserine is also converted to N-acetylserine, which in turn triggers the assimilation of sulfate through specific genes.

This part has been successfully operated while controlled by araC-pBAD both in pSB1C3 (K731020) and the low copy vector pSB3C5, in which it was characterized.
This part was cloned by the iGEM Trento 2012 team for the creation of an aerobically engineered pathway for the removal of the black crust disfiguring marble stones. Further information about this part and its characterization can be found in the iGEM Trento 2012 wiki.

Usage and Biology

In Escherichia coli conversion of L-serine to L-cysteine is mediated by the action of two enzymes: serine acetyltransferase [1] catalyses the activation of L-serine by acetyl-CoA. Its product, 0-acetyl-L-serine (OAS), is then subsequently converted to L-cysteine by 0-acetyl-L-serine(thio1)lyase.
The synthesis of OAS-(thio1)-lyase and of the enzymes involved in sulphate uptake and reduction is regulated by induction as well as by repression [2]. The expression of cysE (the SAT structural gene), on the other hand, is constitutive whereas the catalytic activity of the gene product, SAT, is sensitive to feedback inhibition by L-cysteine [3].

Please head over to K731020 for documentation on characterization of this Part.

  1. EC 2.3.1.30  ↩

  2. Jones-Mortimer, 1968; Jones-Mortimer et al., 1968; Kredich, 1971.  ↩

  3. Kredich & Tomkins, 1966.  ↩

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
    INCOMPATIBLE WITH RFC[25]
    Illegal AgeI site found at 698
  • 1000
    COMPATIBLE WITH RFC[1000]