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• W2059553453 abstract "The effect of mutations in the highly conserved Y-GG/A motif of B-type DNA polymerases was studied in the DNA polymerase from the hyperthermophilic euryarchaeon Thermococcus aggregans. This motif plays a critical role in the balance between the synthesis and degradation of the DNA chain. Five different mutations of the tyrosine at position 387 (Tyr387→Phe, Tyr387→Trp, Tyr387→His, Tyr387→Asn and Tyr387→Ser) revealed that an aromatic ring system is crucial for the synthetic activity of the enzyme. Amino acids at this position lacking the ring system (Ser and Asn) led to a significant decrease in polymerase activity and to enhanced exonuclease activity, which resulted in improved enzyme fidelity. Exchange of tyrosine to phenylalanine, tryptophan or histidine led to phenotypes with wild-type-like fidelity but enhanced PCR performance that could be related to a higher velocity of polymerisation. With the help of a modelled structure of T.aggregans DNA polymerase, the biochemical data were interpreted proposing that the conformation of the flexible loop containing the Y-GG/A motif is an important factor for the equilibrium between DNA polymerisation and exonucleolysis." @default.
• W2059553453 created "2016-06-24" @default.
• W2059553453 creator A5037956695 @default.
• W2059553453 date "2000-10-15" @default.
• W2059553453 modified "2023-09-27" @default.
• W2059553453 title "PCR performance of the B-type DNA polymerase from the thermophilic euryarchaeon Thermococcus aggregans improved by mutations in the Y-GG/A motif" @default.
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• W2059553453 doi "https://doi.org/10.1093/nar/28.20.3910" @default.
• W2059553453 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/110800" @default.
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