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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 3.1.13.1Y313A 100fold reduction of specific activity 709032
Display the word mapDisplay the reaction diagram Show all sequences 3.1.13.1Y253A/F358A 12% of the activity of the enzyme persists, whereas RNA binding affinity is not significantly affected 693048
Display the word mapDisplay the reaction diagram Show all sequences 3.1.13.1Y253A 26% of the activity of the enzyme persists, significantly impairs RNA binding 693048
Display the word mapDisplay the reaction diagram Show all sequences 3.1.13.1D551N abolishes the exonucleolytic activity 700205
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 3.1.13.1C425A 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 3.1.13.1D209N catalytically inactive, is unable to complement RNase II deletion 709993
Display the word mapDisplay the reaction diagram Show all sequences 3.1.13.1more construction of a large set of RNase II truncated proteins and comparison of them to the wild-type regarding their exoribonucleolytic activity and RNA-binding ability. The dissociation constants are determined using different single- or double-stranded substrates. The results obtained reveal that S1 is the most important domain in the establishment of stable RNA–protein complexes, and its elimination results in a drastic reduction on RNA-binding ability. The N-terminal CSD plays a very specific role in RNase II, preventing a tight binding of the enzyme to single-stranded poly(A) chains. The biochemical results obtained with a mutant that lacks both putative RNA-binding domains, reveals the presence of an additional region involved in RNA binding. Such region, is identified by sequence analysis and secondary structure prediction as a third putative RNA-binding domain located at the N-terminal part of RNB catalytic domain 681386
Display the word mapDisplay the reaction diagram Show all sequences 3.1.13.1more construction of deletion mutant DELTArnb. Comparison of the mutant transcriptome with the wild-type, to determine the global effects of the deletion of the exoribonucleases in exponential phase, reveals that the deletion of RNase II significantly affects 187 transcripts. Many of the transcripts are actually down-regulated in the exoribonuclease mutants when compared to the wild-type control. The exoribonuclease also affects some stable RNAs. The RNase II mutant is shown to produce more biofilm than the wild-type control. Differential expression analysis of the transcriptome of exoribonucleases mutants and phenotypes, overview. For example, nirB (Nitrite reductase [NAD(P)H] large subunit) is down-regulated in DELTArnb with a fold-change of 0.36 while in the DELTArnr mutant nirB is up-regulated with a fold-change of 9.11 750198
Display the word mapDisplay the reaction diagram Show all sequences 3.1.13.1more construction of deletion mutant DELTArnb. Comparison of the mutant transcriptome with the wild-type, to determine the global effects of the deletion of the exoribonucleases in exponential phase, reveals that the deletion of RNase R significantly affects 202 transcripts. Many of the transcripts are actually down-regulated in the exoribonuclease mutants when compared to the wild-type control. The exoribonuclease also affects some stable RNAs. The RNase R mutant is shown to produce more biofilm than the wild-type control. Differential expression analysis of the transcriptome of exoribonucleases mutants and phenotypes, overview 750198
Results 1 - 10 of 56 > >>