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DNA polymerase I (or Pol I) is an enzyme that participates in the process of prokaryotic DNA replication. Discovered by Arthur Kornberg in 1956, [1] it was the first known DNA polymerase (and the first known of any kind of polymerase). It was initially characterized in E. coli and is ubiquitous in prokaryotes.
The exonuclease domain is a DEDDy-type DnaQ-like domain common to the B-DNA polymerase family. [39] This domain has a beta hairpin structure that helps in switching between the polymerase and exonuclease active sites in case of nucleotide misincorporation. Motifs A and C, which are the most conserved of the polymerase domain.
The Klenow fragment is a large protein fragment produced when DNA polymerase I from E. coli is enzymatically cleaved by the protease subtilisin.First reported in 1970, [1] it retains the 5' → 3' polymerase activity and the 3’ → 5’ exonuclease activity for removal of precoding nucleotides and proofreading, but loses its 5' → 3' exonuclease activity.
DNA polymerase's rapid catalysis due to its processive nature. Processivity is a characteristic of enzymes that function on polymeric substrates. In the case of DNA polymerase, the degree of processivity refers to the average number of nucleotides added each time the enzyme binds a template.
18973 Ensembl ENSG00000177084 ENSMUSG00000007080 UniProt Q07864 Q9WVF7 RefSeq (mRNA) NM_006231 NM_011132 RefSeq (protein) NP_006222 NP_035262 Location (UCSC) Chr 12: 132.62 – 132.69 Mb Chr 5: 110.43 – 110.49 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse DNA polymerase epsilon catalytic subunit is an enzyme that in humans is encoded by the POLE gene. It is the central catalytic ...
In prokaryotes, the FEN enzyme is found as an N-terminal domain of DNA polymerase I, but some prokaryotes appear to encode a second homologue. [ 1 ] [ 2 ] [ 3 ] The endonuclease activity of FENs was initially identified as acting on a DNA duplex which has a single-stranded 5' overhang on one of the strands [ 4 ] (termed a "5' flap", hence the ...
Multiple DNA polymerases have specialized roles in the DNA replication process. In E. coli, which replicates its entire genome from a single replication fork, the polymerase DNA Pol III is the enzyme primarily responsible for DNA replication and forms a replication complex with extremely high processivity.
The polymerase is a monomeric protein with two distinct functional domains. Site-directed mutagenesis experiments support the proposition that this protein displays a structural and functional similarity to the Klenow fragment of the Escherichia coli Polymerase I enzyme; [3] it comprises a C-terminal polymerase domain and a spatially separated N-terminal domain with a 3'-5' exonuclease activity.