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Results 1 - 10 of 56 > >>
EC Number Protein Variants Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.1.13.1A815F degrades RNA duplexes with 7 or 14 nucleotides of ssRNA overhang significantly slower (about 4fold) than the wild-type enzyme 700205
Display the word mapDisplay the reaction diagram Show all sequences 3.1.13.1A815W degrades RNA duplexes with 7 or 14 nucleotides of ssRNA overhang significantly slower (about 3fold) than the wild-type enzyme 700205
Display the word mapDisplay the reaction diagram Show all sequences 3.1.13.1C284Y RNase II thermolability of the rnb500 phenotype is due to the Cys284Tyr mutation within the RNB domain, which abolishes activity by increasing protein kinetic instability at the nonpermissive temperature. Expression of RNase II C284Y and the double mutant (D126N and C284Y) does not allow growth at the nonpermissive temperature of 44°C. Structural mapping and partial multiple sequence alignment of RNase II thermosensitive phenotype mutations, overview -, 750548
Display the word mapDisplay the reaction diagram Show all sequences 3.1.13.1C425A cannot be classified as polymorphic in the Japanese population. In the Korean, Mongolian, Ovambo, Turkish, and German DNA no genotype other than homozygotic 425C allele in RNASE2 at each single nucleotide polymorphism site is found 697158
Display the word mapDisplay the reaction diagram Show all sequences 3.1.13.1D126N site-directed mutagenesis, the RNase II mutant exhibits a slightly decreased growth at 44°C suggesting some thermosensitivity which does not account for a major phenotype. This individual mutation is not detrimental for the function of RNase II in vivo. the RNase II D126N variant exhibits substantial catalytic activity -, 750548
Display the word mapDisplay the reaction diagram Show all sequences 3.1.13.1D126N/C284Y site-directed mutagenesis, expression of RNase II C284Y and the double mutant (D126N and C284Y) does not allow growth at the nonpermissive temperature of 44°C -, 750548
Display the word mapDisplay the reaction diagram Show all sequences 3.1.13.1D155M truncated RNase II protein pETIIDELTACSD1DELTAS1 consisting of the nuclease domain alone, but lacking any part of CSD2. Removal of the RNA-binding domains does allow RNase II to proceed further 698974
Display the word mapDisplay the reaction diagram Show all sequences 3.1.13.1D201N activity is highly impaired, 0.2% of the specific activity of wild-type enzyme 709032
Display the word mapDisplay the reaction diagram Show all sequences 3.1.13.1D201N significant loss of activity in degradation of poly(A) (0.2% of that of the wild-type enzyme). Generates a 10-11-nt fragment as a major degradation product, although longer reaction times result in the usual 4-nt fragment as a secondary product 693048
Display the word mapDisplay the reaction diagram Show all sequences 3.1.13.1D201N site-directed mutagenesis, kinetic constants for enzyme-RNA interaction compared to the wild-type enzyme 716841
Results 1 - 10 of 56 > >>