FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W1704874388> ?p ?o ?g. }

• W1704874388 endingPage "5319" @default.
• W1704874388 startingPage "5303" @default.
• W1704874388 abstract "Although the chemical nature of the catalytic mechanism of the serine protease alpha-chymotrypsin (alpha-CT) is largely understood, the influence of the enzyme's structural dynamics on its catalysis remains uncertain. Here we investigate whether alpha-CT's structural dynamics directly influence the kinetics of enzyme catalysis. Chemical glycosylation [Solá RJ & Griebenow K (2006) FEBS Lett 580, 1685-1690] was used to generate a series of glycosylated alpha-CT conjugates with reduced structural dynamics, as determined from amide hydrogen/deuterium exchange kinetics (k(HX)). Determination of their catalytic behavior (K(S), k(2), and k(3)) for the hydrolysis of N-succinyl-Ala-Ala-Pro-Phe p-nitroanilide (Suc-Ala-Ala-Pro-Phe-pNA) revealed decreased kinetics for the catalytic steps (k(2) and k(3)) without affecting substrate binding (K(S)) at increasing glycosylation levels. Statistical correlation analysis between the catalytic (DeltaG( not equal)k(i)) and structurally dynamic (DeltaG(HX)) parameters determined revealed that the enzyme acylation and deacylation steps are directly influenced by the changes in protein structural dynamics. Molecular modelling of the alpha-CT glycoconjugates coupled with molecular dynamics simulations and domain motion analysis employing the Gaussian network model revealed structural insights into the relation between the protein's surface glycosylation, the resulting structural dynamic changes, and the influence of these on the enzyme's collective dynamics and catalytic residues. The experimental and theoretical results presented here not only provide fundamental insights concerning the influence of glycosylation on the protein biophysical properties but also support the hypothesis that for alpha-CT the global structural dynamics directly influence the kinetics of enzyme catalysis via mechanochemical coupling between domain motions and active site chemical groups." @default.
• W1704874388 created "2016-06-24" @default.
• W1704874388 creator A5025863481 @default.
• W1704874388 creator A5060966438 @default.
• W1704874388 date "2006-11-03" @default.
• W1704874388 modified "2023-10-08" @default.
• W1704874388 title "Influence of modulated structural dynamics on the kinetics of α‐chymotrypsin catalysis" @default.
• W1704874388 cites W1025602066 @default.
• W1704874388 cites W1499408335 @default.
• W1704874388 cites W1550344442 @default.
• W1704874388 cites W1568612740 @default.
• W1704874388 cites W1681177208 @default.
• W1704874388 cites W1964100116 @default.
• W1704874388 cites W1965761289 @default.
• W1704874388 cites W1968234676 @default.
• W1704874388 cites W1970547520 @default.
• W1704874388 cites W1970853284 @default.
• W1704874388 cites W1971230604 @default.
• W1704874388 cites W1972758402 @default.
• W1704874388 cites W1973505268 @default.
• W1704874388 cites W1975719838 @default.
• W1704874388 cites W1977258623 @default.
• W1704874388 cites W1977274426 @default.
• W1704874388 cites W1978929408 @default.
• W1704874388 cites W1987680456 @default.
• W1704874388 cites W1987729396 @default.
• W1704874388 cites W1987797420 @default.
• W1704874388 cites W1993871972 @default.
• W1704874388 cites W1995948694 @default.
• W1704874388 cites W1996799833 @default.
• W1704874388 cites W1997779091 @default.
• W1704874388 cites W2001804099 @default.
• W1704874388 cites W2002891661 @default.
• W1704874388 cites W2011805684 @default.
• W1704874388 cites W2012055371 @default.
• W1704874388 cites W2013257331 @default.
• W1704874388 cites W2014277123 @default.
• W1704874388 cites W2019947728 @default.
• W1704874388 cites W2020380965 @default.
• W1704874388 cites W2021646539 @default.
• W1704874388 cites W2022416858 @default.
• W1704874388 cites W2027626583 @default.
• W1704874388 cites W2031109994 @default.
• W1704874388 cites W2035687084 @default.
• W1704874388 cites W2036015372 @default.
• W1704874388 cites W2037822672 @default.
• W1704874388 cites W2040026766 @default.
• W1704874388 cites W2043556481 @default.
• W1704874388 cites W2043901868 @default.
• W1704874388 cites W2044740473 @default.
• W1704874388 cites W2044849008 @default.
• W1704874388 cites W2044877050 @default.
• W1704874388 cites W2046002103 @default.
• W1704874388 cites W2046257141 @default.
• W1704874388 cites W2046714822 @default.
• W1704874388 cites W2047965857 @default.
• W1704874388 cites W2051315164 @default.
• W1704874388 cites W2058206198 @default.
• W1704874388 cites W2063806420 @default.
• W1704874388 cites W2065132442 @default.
• W1704874388 cites W2067767415 @default.
• W1704874388 cites W2068475565 @default.
• W1704874388 cites W2073328513 @default.
• W1704874388 cites W2073538792 @default.
• W1704874388 cites W2077581019 @default.
• W1704874388 cites W2078689274 @default.
• W1704874388 cites W2081125798 @default.
• W1704874388 cites W2083799886 @default.
• W1704874388 cites W2089798830 @default.
• W1704874388 cites W2092956046 @default.
• W1704874388 cites W2093986039 @default.
• W1704874388 cites W2094808269 @default.
• W1704874388 cites W2096921126 @default.
• W1704874388 cites W2102998463 @default.
• W1704874388 cites W2103885137 @default.
• W1704874388 cites W2112574017 @default.
• W1704874388 cites W2117184688 @default.
• W1704874388 cites W2120292029 @default.
• W1704874388 cites W2122326469 @default.
• W1704874388 cites W2122976061 @default.
• W1704874388 cites W2123035826 @default.
• W1704874388 cites W2130479394 @default.
• W1704874388 cites W2131288855 @default.
• W1704874388 cites W2131739285 @default.
• W1704874388 cites W2133067061 @default.
• W1704874388 cites W2133573415 @default.
• W1704874388 cites W2139036153 @default.
• W1704874388 cites W2141504884 @default.
• W1704874388 cites W2145961753 @default.
• W1704874388 cites W2151855710 @default.
• W1704874388 cites W2153049516 @default.
• W1704874388 cites W2160294964 @default.
• W1704874388 cites W2160975112 @default.
• W1704874388 cites W2166905169 @default.
• W1704874388 cites W2004808662 @default.
• W1704874388 doi "https://doi.org/10.1111/j.1742-4658.2006.05524.x" @default.
• W1704874388 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/17076704" @default.
• W1704874388 hasPublicationYear "2006" @default.

• next