Part:BBa_K5094004
The IsPETase Thr116Ala/Met154Thr, double mutations on the amino acids 116 and 154 in the IsPETase ge
The IsPETaseThr116Ala/Met154Thr, double mutations on the amino acids 116 and 154 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 154 from the hydrophobic side chain of the methionine to the polar uncharged side chain of the Threonine, which would change the properties of the 116 and 154 amino acids, such as the interaction with the substrate or the catalytic function.
IsPETaseThr116Ala/Met154Thr involves double mutations at amino acids 116 and 154 in the IsPETase gene. In this modification, the polar uncharged threonine at position 116 is replaced by the hydrophobic alanine, while the hydrophobic methionine at position 154 is substituted with the polar uncharged threonine. 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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