Difference between revisions of "Part:BBa K1483001:Design"

 
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__NOTOC__
 
__NOTOC__
 
<partinfo>BBa_K1483001 short</partinfo>
 
<partinfo>BBa_K1483001 short</partinfo>
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===Design Notes===
 
===Design Notes===
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Part in RFC25, in order to ease fusion with other parts, for example immobilisation tags.
+
Part in RFC25, in order to ease fusion with other parts, for example immobilisation tags. Codon usage was modified for optimal expression in <i>E. coli</i> K12 and common restriction sites were removed.  
  
  
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===Source===
 
===Source===
  
−
The protein encoded by this sequence naturally occurs in Clostridium perfringens. This sequence was optimized for codon usage in E. coli K12 and synthesized.
+
The protein encoded by this sequence naturally occurs in <i>Clostridium perfringens</i>. This sequence was optimized for codon usage in <i>E. coli</i> K12 and obtained by in-vitro gene synthesis.  
  
 
===References===
 
===References===
 +
<p>
 +
Kinetic properties and structural characteristics of the enzyme were charcterised by Shaikh and Anderson.
 +
</p>
 +
<p>
 +
[http://hdl.handle.net/2429/43027 Shaikh F. "Towards universal blood : mechanistic studies on blood group cleaving glycosidases"]
 +
</p>
 +
<p>
 +
[http://www.jbc.org/content/280/9/7720.short Anderson, Kimberly M., et al. "A Clostridial Endo-β-galactosidase That Cleaves Both Blood Group A and B Glycotopes THE FIRST MEMBER OF A NEW GLYCOSIDE HYDROLASE FAMILY, GH98." Journal of Biological Chemistry 280.9 (2005): 7720-7728.]
 +
</p>

Revision as of 20:14, 14 October 2014

Endo-β-Galactosidase


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]


Design Notes

Part in RFC25, in order to ease fusion with other parts, for example immobilisation tags. Codon usage was modified for optimal expression in E. coli K12 and common restriction sites were removed.


Source

The protein encoded by this sequence naturally occurs in Clostridium perfringens. This sequence was optimized for codon usage in E. coli K12 and obtained by in-vitro gene synthesis.

References

Kinetic properties and structural characteristics of the enzyme were charcterised by Shaikh and Anderson.

[http://hdl.handle.net/2429/43027 Shaikh F. "Towards universal blood : mechanistic studies on blood group cleaving glycosidases"]

[http://www.jbc.org/content/280/9/7720.short Anderson, Kimberly M., et al. "A Clostridial Endo-β-galactosidase That Cleaves Both Blood Group A and B Glycotopes THE FIRST MEMBER OF A NEW GLYCOSIDE HYDROLASE FAMILY, GH98." Journal of Biological Chemistry 280.9 (2005): 7720-7728.]