Specificity of guanylic RNases to polynucleotide substrates
Language English Country United States Media print
Document type Journal Article
PubMed
1904722
DOI
10.1016/0006-291x(91)91835-z
PII: 0006-291X(91)91835-Z
Knihovny.cz E-resources
- MeSH
- Aspergillus oryzae enzymology MeSH
- Endoribonucleases metabolism MeSH
- Ribonuclease T1 metabolism MeSH
- Kinetics MeSH
- Penicillium enzymology MeSH
- Polynucleotides metabolism MeSH
- Ribonuclease P MeSH
- Ribonucleases metabolism MeSH
- RNA, Catalytic metabolism MeSH
- Streptomyces aureofaciens enzymology MeSH
- Substrate Specificity MeSH
- Publication type
- Journal Article MeSH
- Names of Substances
- Endoribonucleases MeSH
- Ribonuclease T1 MeSH
- Polynucleotides MeSH
- ribonuclease S MeSH Browser
- Ribonuclease P MeSH
- Ribonucleases MeSH
- RNA, Catalytic MeSH
Kinetic parameters kcat and KM were measured for cleavage of poly I, poly A, poly U, poly C and poly I poly C by guanyl-specific RNases Sa, Pb1 and T1 and compared with that of guanyl-preferential RNase Bi. Catalytic efficiencies of the investigated enzymes to polynucleotide substrates vary considerably. The structural basis for specificity of these RNases is discussed. A hypothesis is suggested that Ser-56 plays an important role in recognition of poly A by RNase Bi.
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