Part:BBa_K3843000
PEA-binding salmon trypsin (1UTM)
Trypsin is a ubiquitous protease in vertebrates due to its central role in digestion. Trypsin cleaves peptide bonds occurring after positively charged amino acids, such as lysine and arginine. 1UTM (pictured below) is a trypsin from Salmo salar (Atlantic salmon). It has a variety of known inhibitors, typically biogenic amines (CITE Ashish's paper). These noncompetitive inhibitors bind to allosteric sites, thereby inactivating trypsin's proteolytic function. Of particular interest to Waterloo iGEM 2021 was the ability of phenylethylamine (PEA), a dopamine precursor, to act as an inhibitor of 1UTM (binding constant CITE). This would allow for 1UTM to be used as a PEA-binding protein. Detection and quantification of phenylethylamine, using 1UTM fused to horseradish peroxidase in a microfluidic flow assay, would give insight into an individual's probability of having ADHD.
IMAGE LINK
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
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