Difference between revisions of "Part:BBa K2286008"
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In order to test the HheC catalytic activity towards 2,3-DCP, chloride ion method was applied by us. The results show that the catalytic activity of P84A-W249P to 2,3-DCP is 1.15 times than that of W249P. | In order to test the HheC catalytic activity towards 2,3-DCP, chloride ion method was applied by us. The results show that the catalytic activity of P84A-W249P to 2,3-DCP is 1.15 times than that of W249P. | ||
| − | [[File:T--UESTC-China--P84A-W249P-2,3-DCP.png|500px|thumb|center|''' | + | [[File:T--UESTC-China--P84A-W249P-2,3-DCP.png|500px|thumb|center|'''Fig. 1''' The catalytic activity of mutants on 2,3-DCP. Data were measured in 50mM Tris-H2SO4 at pH8.5 and 37℃.]] |
Latest revision as of 02:15, 2 November 2017
HheC- P84A-W249P: halohydrin dehalogenase site-directed mutant
This is the site-directed mutant of halohydrin dehalogenase. Based on the excellent mutant HheC-W249P, We change the alanine to proline in the 84 site. And this sequence is codon-optimized for E.coli.
Sequence and Features
Assembly Compatibility:
- 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 718
- 1000COMPATIBLE WITH RFC[1000]
Characterization
This part is an improvement of BBa_K1199044 (W249P) in the activity of 2,3-DCP degradation. We performed a superimposed mutation on the basis of W249P and obtained a mutant P84A-W249P with a higher activity than W249P.
Activity towards 2，3-DCP
In order to test the HheC catalytic activity towards 2,3-DCP, chloride ion method was applied by us. The results show that the catalytic activity of P84A-W249P to 2,3-DCP is 1.15 times than that of W249P.
