Kphpif1 helicase and use thereof
By modifying or linking the 1B and 2B domains of Klebsiella phage E1 helicase with amino acids, the problem of excessively fast sequencing speed of polynucleotides in nanopore sequencing was solved, achieving stable control and high-precision sequencing of polynucleotides.
Patent Information
- Authority / Receiving Office
- WO · WO
- Patent Type
- Applications
- Filing Date
- 2024-12-30
- Publication Date
- 2026-07-09
AI Technical Summary
In existing nanopore sequencing technologies, the perforation speed of polynucleotides is too fast, resulting in short nucleotide current levels that are difficult to distinguish and have low accuracy. This is especially true when sequencing long nucleotide sequences, where helicase shedding cannot be controlled.
A DNA-dependent ATPase (KphE1) helicase mutant from Klebsiella pneumoniae phage E1 is provided, which enhances the stability and control of polynucleotides by introducing new amino acids or linker molecules into the 1B and 2B domains.
It enables the controllable movement of polynucleotides in nanopores, improves the current range and decoding accuracy, enhances sequencing efficiency, and reduces shedding, especially in long nucleic acid sequencing.
Smart Images
Figure CN2024143728_09072026_PF_FP_ABST