Difference between revisions of "Part:BBa K3468016:Design"
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===References=== | ===References=== | ||
| + | [1]Zhou K, Zang J, Chen H, Wang W, Wang H, Zhao G. On-Axis Alignment of Protein Nanocage Assemblies from 2D to 3D through the Aromatic Stacking Interactions of Amino Acid Residues. ACS Nano. 2018 Nov 27;12(11):11323-11332. | ||
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| + | [2]Luan ZJ, Yu HL, Ma BD, Chen Q, Xu JH. Dramatically improved performance of an esterase for cilastatin synthesis by cap domain engineering. Ind. Eng. Chem. Res., 2016, 55, 12167–12172. | ||
Latest revision as of 12:47, 27 October 2020
PETase Q127L
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
Design Notes
By observing and comparing the structure of PETase, appropriate mutations were constructed and the forces between the residues were modified. By finding suitable sites around M128, L131, and V156 for mutations, the hydrophobic interaction between the residues was enhanced and the hydrophobic core was created, so Q127L was designed.
Source
Ideonalla sakaiensis
References
[1]Zhou K, Zang J, Chen H, Wang W, Wang H, Zhao G. On-Axis Alignment of Protein Nanocage Assemblies from 2D to 3D through the Aromatic Stacking Interactions of Amino Acid Residues. ACS Nano. 2018 Nov 27;12(11):11323-11332.
[2]Luan ZJ, Yu HL, Ma BD, Chen Q, Xu JH. Dramatically improved performance of an esterase for cilastatin synthesis by cap domain engineering. Ind. Eng. Chem. Res., 2016, 55, 12167–12172.