Line 38: | Line 38: | ||
<div class="row"> | <div class="row"> | ||
<div class="col-sm-9 col-xs-12"> | <div class="col-sm-9 col-xs-12"> | ||
− | |||
− | |||
− | |||
− | |||
</div> | </div> | ||
Line 54: | Line 50: | ||
<p style="text-align:left !important; font-size: 15px !important;"><b>Protein Coding Sequence for Amino Acid Deaminase Gene</b><br></p> | <p style="text-align:left !important; font-size: 15px !important;"><b>Protein Coding Sequence for Amino Acid Deaminase Gene</b><br></p> | ||
− | <p style="text-align:left !important; font-size: 15px !important;"> | + | <p style="text-align:left !important; font-size: 15px !important;">K1889006 is a gene coding for an amino acid deaminase gene. It is derived from Proteus mirabilis. It functions to turn phenylalanine into phenylpyruvic acid by removing its amino group, coming from the enzyme family that catalyzes the breakdown of amino acids into alpha-keto acids. In our experiment, this gene is used to turn phenylalanine, a naturally occurring amino acid in E. coli, into phenylpyruvic acid. The phenylpyruvic acid then acts as an attractant to C. elegans.<br><br></p> |
<img src="https://static.igem.org/mediawiki/parts/2/20/Team-Hong_Kong_UCCKE_2016_img24rfjui45t98u5.jpeg" style="width:100%; max-width:600px;"><br><br> | <img src="https://static.igem.org/mediawiki/parts/2/20/Team-Hong_Kong_UCCKE_2016_img24rfjui45t98u5.jpeg" style="width:100%; max-width:600px;"><br><br> |
Latest revision as of 10:18, 3 November 2016
K1889006
Protein Coding Sequence for Amino Acid Deaminase Gene
K1889006 is a gene coding for an amino acid deaminase gene. It is derived from Proteus mirabilis. It functions to turn phenylalanine into phenylpyruvic acid by removing its amino group, coming from the enzyme family that catalyzes the breakdown of amino acids into alpha-keto acids. In our experiment, this gene is used to turn phenylalanine, a naturally occurring amino acid in E. coli, into phenylpyruvic acid. The phenylpyruvic acid then acts as an attractant to C. elegans.
The sequence of the gene was referenced from an article from Journal of Bacteriology, titled “Proteus mirabilis amino acid deaminase: cloning, nucleotide sequence, and characterization of aad.” The DNA sequence was slightly modified to allow its chemical synthesis by IDT while still retaining the original amino acid sequence.
Massad, G., Zhao, H., & Mobley, H. L. (1995). Proteus mirabilis amino acid deaminase: cloning, nucleotide sequence, and characterization of aad. Journal of Bacteriology, 177(20), 5878–5883.