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EC Number Protein Variants Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.102D101 catalytic site mutant, complete loss of activity -, 751319
Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.102D103 catalytic site mutant, complete loss of activity -, 751319
Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.102D111A mutation abolishes primase and polymerase activity while leaving DNA-binding activity unaffected 751687
Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.102D111A the mutant protein is deficient and DNA polymerase activity and primase activity, ATPase activity is unaffected 719357
Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.102D111N residue is essential for viability 751324
Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.102D113N residue is essential for viability 751324
Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.102D114A/E116A mutant in two potential metal bindig sites, inactive 751551
Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.102D171A mutation severely reduces primase and abolishes polymerase activity while leaving DNA-binding activity unaffected 751687
Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.102D235E mutation of aspartic acid by glutamic acid in DNA primase small (catalytic) subunit PriS may occur naturally due to a misrepair on the DNA replication and by a substitution of the third nucleotide of the codons GAU and GAC to GAA to GAG, corresponding to aspartic acid and glutamic acid, respectively. The in silico analysis suggests that these mutations in PriL may cause destabilization on its structure interfering with replication mechanisms of Saccharolobus solfataricus. In addition, the mutation may alter the interactions with other molecules, such as salt bridges -, 760313
Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.102D241E mutation of aspartic acid by glutamic acid in DNA primase small (catalytic) subunit PriS may occur naturally due to a misrepair on the DNA replication and by a substitution of the third nucleotide of the codons GAU and GAC to GAA to GAG, corresponding to aspartic acid and glutamic acid, respectively. The in silico analysis suggests that these mutations in PriL may cause destabilization on its structure interfering with replication mechanisms of Saccharolobus solfataricus. In addition, the mutation may alter the interactions with other molecules, such as salt bridges -, 760313
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