Matches in SemOpenAlex for { <https://semopenalex.org/work/W2103447664> ?p ?o ?g. }
- W2103447664 endingPage "901" @default.
- W2103447664 startingPage "893" @default.
- W2103447664 abstract "Staphylococcal nuclease (SNase) is a well-established model for protein folding studies. Its three-dimensional structure has been determined. The enzyme, Ca2+, and DNA or RNA substrate form a ternary complex. Glycine 20 is the second position of the first β-turn of SNase, which may serve as the folding initiation site for the SNase polypeptide. To study the role of Gly20 in the conformational stability and catalysis of SNase, three mutants, in which Gly20 was replaced by alanine, valine, or isoleucine, were constructed and studied by using circular dichroism spectra, intrinsic and ANS-binding fluorescence spectra, stability and activity assays. The mutations have little effect on the conformational integrity of the mutants. However, the catalytic activity is reduced drastically by the mutations, and the stability of the protein is progressively decreased in the order G20A<G20V<G20I. Kinetic analysis indicates that the mutant enzymes G20A and G20V show almost 20-fold higher KmCa values than the wild-type enzyme, and the value for G20I is more than 50-fold higher. KACa values indicate more than 17.5-fold weaker binding of Ca2+ to the G20A and G20V mutants, and more than 39-fold weaker to the G20I mutant, compared to wild-type SNase. The above results suggest that the substitutions at Gly20 cause significantly weaker binding of Ca2+ in both the binary enzyme-Ca2+ complex and the ternary complex. However, there is little difference in the values of KmDNA and KSDNA between the mutants and the wild-type enzyme, suggesting that the substitutions at Gly20 have little effect on the binding of DNA substrates to the enzyme. Consistent with the changes in KmCa and KACa, the mutant enzymes G20A, G20V and G20I show about 103-, 104- and 105-fold lower KCat values than the wild-type enzyme, respectively. These results suggest that Gly20 plays an important role in maintaining a suitable conformation at the active site of the enzyme." @default.
- W2103447664 created "2016-06-24" @default.
- W2103447664 creator A5006075519 @default.
- W2103447664 creator A5016767567 @default.
- W2103447664 creator A5018524821 @default.
- W2103447664 creator A5046759915 @default.
- W2103447664 creator A5071272477 @default.
- W2103447664 creator A5071334202 @default.
- W2103447664 creator A5081141216 @default.
- W2103447664 creator A5089308484 @default.
- W2103447664 date "2004-12-01" @default.
- W2103447664 modified "2023-10-18" @default.
- W2103447664 title "The effects of amino acid replacements of glycine 20 on conformational stability and catalysis of staphylococcal nuclease" @default.
- W2103447664 cites W1482133448 @default.
- W2103447664 cites W1485154593 @default.
- W2103447664 cites W1510229959 @default.
- W2103447664 cites W1525048732 @default.
- W2103447664 cites W1587105456 @default.
- W2103447664 cites W1964944514 @default.
- W2103447664 cites W1966480910 @default.
- W2103447664 cites W1969033628 @default.
- W2103447664 cites W1971827772 @default.
- W2103447664 cites W1975085160 @default.
- W2103447664 cites W1980694228 @default.
- W2103447664 cites W1981296554 @default.
- W2103447664 cites W1988407705 @default.
- W2103447664 cites W1988787136 @default.
- W2103447664 cites W2010599167 @default.
- W2103447664 cites W2023671907 @default.
- W2103447664 cites W2023970782 @default.
- W2103447664 cites W2035014598 @default.
- W2103447664 cites W2050282655 @default.
- W2103447664 cites W2052437655 @default.
- W2103447664 cites W2053129848 @default.
- W2103447664 cites W2054112128 @default.
- W2103447664 cites W2055805017 @default.
- W2103447664 cites W2074756868 @default.
- W2103447664 cites W2084129060 @default.
- W2103447664 cites W2085155760 @default.
- W2103447664 cites W2087516654 @default.
- W2103447664 cites W2096858815 @default.
- W2103447664 cites W2115196876 @default.
- W2103447664 cites W2160336334 @default.
- W2103447664 cites W2163022645 @default.
- W2103447664 cites W2171414493 @default.
- W2103447664 cites W4293247451 @default.
- W2103447664 cites W4323521360 @default.
- W2103447664 cites W986536428 @default.
- W2103447664 doi "https://doi.org/10.1016/j.biochi.2004.10.005" @default.
- W2103447664 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/15667939" @default.
- W2103447664 hasPublicationYear "2004" @default.
- W2103447664 type Work @default.
- W2103447664 sameAs 2103447664 @default.
- W2103447664 citedByCount "6" @default.
- W2103447664 countsByYear W21034476642012 @default.
- W2103447664 countsByYear W21034476642014 @default.
- W2103447664 countsByYear W21034476642015 @default.
- W2103447664 countsByYear W21034476642023 @default.
- W2103447664 crossrefType "journal-article" @default.
- W2103447664 hasAuthorship W2103447664A5006075519 @default.
- W2103447664 hasAuthorship W2103447664A5016767567 @default.
- W2103447664 hasAuthorship W2103447664A5018524821 @default.
- W2103447664 hasAuthorship W2103447664A5046759915 @default.
- W2103447664 hasAuthorship W2103447664A5071272477 @default.
- W2103447664 hasAuthorship W2103447664A5071334202 @default.
- W2103447664 hasAuthorship W2103447664A5081141216 @default.
- W2103447664 hasAuthorship W2103447664A5089308484 @default.
- W2103447664 hasConcept C104317684 @default.
- W2103447664 hasConcept C133571119 @default.
- W2103447664 hasConcept C143065580 @default.
- W2103447664 hasConcept C181199279 @default.
- W2103447664 hasConcept C185592680 @default.
- W2103447664 hasConcept C207583985 @default.
- W2103447664 hasConcept C2777271071 @default.
- W2103447664 hasConcept C2779856020 @default.
- W2103447664 hasConcept C515207424 @default.
- W2103447664 hasConcept C55493867 @default.
- W2103447664 hasConcept C71240020 @default.
- W2103447664 hasConcept C86756495 @default.
- W2103447664 hasConceptScore W2103447664C104317684 @default.
- W2103447664 hasConceptScore W2103447664C133571119 @default.
- W2103447664 hasConceptScore W2103447664C143065580 @default.
- W2103447664 hasConceptScore W2103447664C181199279 @default.
- W2103447664 hasConceptScore W2103447664C185592680 @default.
- W2103447664 hasConceptScore W2103447664C207583985 @default.
- W2103447664 hasConceptScore W2103447664C2777271071 @default.
- W2103447664 hasConceptScore W2103447664C2779856020 @default.
- W2103447664 hasConceptScore W2103447664C515207424 @default.
- W2103447664 hasConceptScore W2103447664C55493867 @default.
- W2103447664 hasConceptScore W2103447664C71240020 @default.
- W2103447664 hasConceptScore W2103447664C86756495 @default.
- W2103447664 hasIssue "12" @default.
- W2103447664 hasLocation W21034476641 @default.
- W2103447664 hasLocation W21034476642 @default.
- W2103447664 hasOpenAccess W2103447664 @default.
- W2103447664 hasPrimaryLocation W21034476641 @default.
- W2103447664 hasRelatedWork W1992246271 @default.
- W2103447664 hasRelatedWork W1992458278 @default.