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- W2071625124 abstract "This chapter discusses the mutational analysis of bacteriophage φ29 DNA polymerase. The fact that φ29 DNA polymerase is a small (66-kDa) single-subunit enzyme containing well-characterized enzymatic activities 1 makes this polymerase an appropriate system for structure-function studies. φ29 DNA polymerase was included in the group of eukaryotic-type DNA polymerases because of its sensitivity to the nucleotide analogs BuAdATP and BuPdGTP, 23 specific inhibitors of eukaryotic DNA polymerase α. φ29 DNA polymerase contains several regions of amino acid sequence highly conserved in the C-terminal portion of eukaryotic DNA polymerases. It has been proposed that these conserved regions might play an important role in the function of the enzyme, being part of the active site for synthetic activities. Three conserved amino acid segments, named Exo I, Exo II, and Exo lII, are identified in the N-terminal portion of both eukaryotic- type and Pol I-type DNA polymerases. The wild-type φ29 DNA polymerase gene, cloned into M13 derivatives, was used for site-directed mutagenesis." @default.
- W2071625124 created "2016-06-24" @default.
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- W2071625124 date "1995-01-01" @default.
- W2071625124 modified "2023-10-16" @default.
- W2071625124 title "[22] Mutational analysis of bacteriophage φ29 DNA polymerase" @default.
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- W2071625124 doi "https://doi.org/10.1016/0076-6879(95)62024-9" @default.
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