Difference between revisions of "Part:BBa K118016:Design"

Revision as of 21:31, 6 October 2008

glgC16 (glgC with G336D substitution)

Assembly Compatibility:

10
COMPATIBLE WITH RFC[10]
12
COMPATIBLE WITH RFC[12]
21
INCOMPATIBLE WITH RFC[21]
Illegal BamHI site found at 194
23
COMPATIBLE WITH RFC[23]
25
COMPATIBLE WITH RFC[25]
1000
COMPATIBLE WITH RFC[1000]

Design Notes

The mutation G336D was achieved by the substitution of A for G at position 1076 (codon GGC->GAC) using the mutagenesis by blunt-ended ligation (MABEL) technique. The genomic DNA sequence also contains to EcoRI sites, both of which have been mutated out using MABEL.

Source

Escherichia coli JM109 genomic DNA

References

[http://www.pubmedcentral.nih.gov/picrender.fcgi?artid=212844&blobtype=pdf Leung, P., Lee, Y. M., Greenberg, E., Esch, K., Boylan, S. and Preiss, J. (1986). Cloning and expression of the Escherichia coli glgC gene from a mutant containing an ADPglucose pyrophosphorylase with altered allosteric properties. J. Bacteriol. 167, 82-88.]
[http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6WB5-45KKRWW-9P&_user=809099&_rdoc=1&_fmt=&_orig=search&_sort=d&view=c&_acct=C000043939&_version=1&_urlVersion=0&_userid=809099&md5=aa8d0cb9ae204115911c188cbdc31b16f Meyer, C. R., Bork, J. A., Nadler, S., Yirsa, J. and Preiss, J. (1998). Site-Directed Mutagenesis of a Regulatory Site of Escherichia coli ADP-Glucose Pyrophosphorylase: The Role of Residue 336 in Allosteric Behavior. Archives of Biochemistry and Biophysics 353, 152-159.]

@@ Line 13: / Line 13: @@
 ===References===
-[http://www.pubmedcentral.nih.gov/picrender.fcgi?artid=212844&blobtype=pdf <b>Leung, P., Lee, Y. M., Greenberg, E., Esch, K., Boylan, S. and Preiss, J.</b> (1986). Cloning and expression of the Escherichia coli glgC gene from a mutant containing an ADPglucose pyrophosphorylase with altered allosteric properties. <i>J. Bacteriol.</i> <b>167,</b> 82-88.]
+* [http://www.pubmedcentral.nih.gov/picrender.fcgi?artid=212844&blobtype=pdf <b>Leung, P., Lee, Y. M., Greenberg, E., Esch, K., Boylan, S. and Preiss, J.</b> (1986). Cloning and expression of the Escherichia coli glgC gene from a mutant containing an ADPglucose pyrophosphorylase with altered allosteric properties. <i>J. Bacteriol.</i> <b>167,</b> 82-88.]
-[http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6WB5-45KKRWW-9P&_user=809099&_rdoc=1&_fmt=&_orig=search&_sort=d&view=c&_acct=C000043939&_version=1&_urlVersion=0&_userid=809099&md5=aa8d0cb9ae204115911c188cbdc31b16f <b>Meyer, C. R., Bork, J. A., Nadler, S., Yirsa, J. and Preiss, J.</b> (1998). Site-Directed Mutagenesis of a Regulatory Site of Escherichia coli ADP-Glucose Pyrophosphorylase: The Role of Residue 336 in Allosteric Behavior. <i>Archives of Biochemistry and Biophysics</i> <b>353</b>, 152-159.]
+* [http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6WB5-45KKRWW-9P&_user=809099&_rdoc=1&_fmt=&_orig=search&_sort=d&view=c&_acct=C000043939&_version=1&_urlVersion=0&_userid=809099&md5=aa8d0cb9ae204115911c188cbdc31b16f <b>Meyer, C. R., Bork, J. A., Nadler, S., Yirsa, J. and Preiss, J.</b> (1998). Site-Directed Mutagenesis of a Regulatory Site of Escherichia coli ADP-Glucose Pyrophosphorylase: The Role of Residue 336 in Allosteric Behavior. <i>Archives of Biochemistry and Biophysics</i> <b>353</b>, 152-159.]