3.1.13.1	A815F	degrades RNA duplexes with 7 or 14 nucleotides of ssRNA overhang significantly slower (about 4fold) than the wild-type enzyme	700205	
3.1.13.1	A815W	degrades RNA duplexes with 7 or 14 nucleotides of ssRNA overhang significantly slower (about 3fold) than the wild-type enzyme	700205	
3.1.13.1	C284Y	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	
3.1.13.1	C425A	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	
3.1.13.1	D126N	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	
3.1.13.1	D126N/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	
3.1.13.1	D155M	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	
3.1.13.1	D201N	activity is highly impaired, 0.2% of the specific activity of wild-type enzyme	709032	
3.1.13.1	D201N	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	
3.1.13.1	D201N	site-directed mutagenesis, kinetic constants for enzyme-RNA interaction compared to the wild-type enzyme	716841