Part:BBa_K5094005
IsPETase/Thr116Ala/Lys259Glu, double mutations on the amino acids of 116 and 259 in the IsPETase gen
The IsPETaseThr116Ala/Lys259Glu, double mutations on the amino acids of 116 and 259 in the IsPETase gene, amino acid 116 from the polar uncharged side chain of the Threonine switched to the hydrophobic side chain of the alanine, and amino acid 259 from the positive charge of the side chain on lysine to the negative charge of the side chain on the glutamic acid, which would change the properties of the 116 and 259 amino acids, such as the interaction with the substrate or the catalytic function.
IsPETaseThr116Ala/Lys259Glu involves double mutations at amino acids 116 and 259 in the IsPETase gene. In this modification, the polar uncharged threonine at position 116 is replaced by the hydrophobic alanine, while the positively charged lysine at position 259 is substituted with the negatively charged glutamic acid. These changes in amino acid properties may alter substrate interactions and potentially impact the enzyme's catalytic function.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal NgoMIV site found at 220
- 1000COMPATIBLE WITH RFC[1000]
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