DNA Polymerases: An Insight into Their Active Sites and Catalytic Mechanism.

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dc.contributor.authorPalanivelu, P
dc.date.accessioned2015-04-24T10:53:44Z
dc.date.available2015-04-24T10:53:44Z
dc.date.issued2013-07
dc.description.abstractTo analyze the active sites of various prokaryotic and eukaryotic DNA polymerases and propose a plausible mechanism of action for the polymerases with the Escherichia coli DNA polymerase I as a model system. Study Design: Bioinformatics, Biochemical and X-ray crystallographic data were analyzed. Place and Duration of Study: Department of Molecular Microbiology, School of Biotechnology, Madurai Kamaraj University, Madurai – 625 021, India. From 2007 to 2012. Methodology: The advanced version of T-COFFEE was used to analyze both prokaryotic and eukaryotic DNA polymerase sequences. Along with this bioinformatics data, X-ray crystallographic and biochemical data were used to confirm the possible amino acids in the active sites of different types of polymerases from various sources. Results: Multiple sequence analyses of various polymerases from different sources show only a few highly conserved motifs among these enzymes except eukaryotic epsilon polymerases where a large number of highly conserved sequences are found. Possible catalytic/active site regions in all these polymerases show a highly conserved catalytic amino acid K/R and the YG/A pair. A distance conservation is also observed between the active sites. Furthermore, two highly conserved Ds and DXD motifs are also observed. Conclusion: The highly conserved amino acid K/R acts as the proton abstractor in catalysis and the YG/A pair acts as a “steric gate” in selection of only dNTPS for polymerization reactions. The two highly conserved Ds act as the “charge shielder” of dNTPs and orient the alpha phosphate of incoming dNTPs to the 3’-OH end of the growing primer.en_US
dc.identifier.citationPalanivelu P. DNA Polymerases: An Insight into Their Active Sites and Catalytic Mechanism. International Journal of Biochemistry Research & Review 2013 Jul-Sept ; 3 (3) : 206-247.en_US
dc.identifier.urihttps://imsear.searo.who.int/handle/123456789/157848
dc.language.isoenen_US
dc.source.urihttps://www.sciencedomain.org/abstract.php?iid=231&id=3&aid=1432en_US
dc.subjectDNA polymerasesen_US
dc.subjectT-COFFEEen_US
dc.subjectconserved motifsen_US
dc.subjectactive sitesen_US
dc.subjectE. coli DNA polymerase Ien_US
dc.subjectpolymerase active siteen_US
dc.subjectpolymerization mechanismen_US
dc.subjectexonuclease active siteen_US
dc.subjectproof-reading mechanismen_US
dc.titleDNA Polymerases: An Insight into Their Active Sites and Catalytic Mechanism.en_US
dc.typeArticleen_US
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