FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2016349625> ?p ?o ?g. }

• W2016349625 endingPage "91" @default.
• W2016349625 startingPage "80" @default.
• W2016349625 abstract "In paper [5] a simplified model for the hydrophobic binding sites of trypsin was proposed, showing where 1-amino-n-alkanes and α,ω-diamino-n-alkanes are bound while they competitively inhibit the catalyzed hydrolysis of a substrate ester. In the model, the enzyme has two hydrophobic binding sites separated by an aqueous region which presumably contains the catalytic important residues. The first site binds up to 4 methylene groups of the aliphatic side chain adjacent to the ω-amino group; additional –CH2 groups in the chain extend into the aqueous region. If the chain is larger than 7 carbon atoms, the additional methylene or methyl groups are bound to the second hydrophobic site. This site is found to bind less strongly than the first site. This paper presents a thermodynamic investigation of the binding properties of trypsin in the formation of complexes with cationic esters and amids which bear an ammonium group on either the end of the acid side chain or the end of the alcohol or amine component. Free energy and in addition enthalpy and entropy of binding were measured as a function of the length of the inhibitor molecule and as a function of the position of the ester or amide carbonyl group. It was found that the stability of a complex increases linearly with length of the molecule, and that the magnitude of increase depends on the position of the carbonyl group. Amides always exhibit a smaller increase than esters. Inhibitors with the ammonium group on the alcohol component were bound with about the same stability than the corresponding ω-aminoacidesters. The results are consistent with the model. Positioning of the carbonyl group within the first or second binding site reduces stability due to restricted interaction of the hydrophobic residues on enzyme and inhibitor. Only when the carbonyl group falls into the aqueous region, the free energy for an inhibitor containing the ester group is similar to that for a 1-amino-n-alkane with identical chain length. Enthalpy and entropy as functions of the position of the carbonyl group show minima for the position within the aqueous region. This observation is correlated with the jump of enthalpy and entropy of complex formation of trypsin in the series of 1-amino-n-alkanes reported earlier. It is shown that the magnitude of free energy of complex formation with specific substrates is well estimated on basis of the model. As a consequence, the alternative binding of either the 2-N-acyl group or the alcohol or amine component to the second hydrophobic site may imply a mode of less productive binding. It is emphasized that unproductive binding should be reflected in the Michaelis Menten constants for substrate amides whereas the Michaelis Menten constant for a substrate ester is normally not perturbed." @default.
• W2016349625 created "2016-06-24" @default.
• W2016349625 creator A5039833815 @default.
• W2016349625 creator A5044134666 @default.
• W2016349625 date "1970-09-01" @default.
• W2016349625 modified "2023-10-16" @default.
• W2016349625 title "Hemmung der Trypsinkatalyse durch kationische Carbonsaureester und Amide" @default.
• W2016349625 cites W1170924751 @default.
• W2016349625 cites W1499907727 @default.
• W2016349625 cites W1556232337 @default.
• W2016349625 cites W1561690684 @default.
• W2016349625 cites W157808733 @default.
• W2016349625 cites W1580500739 @default.
• W2016349625 cites W1597344314 @default.
• W2016349625 cites W174449120 @default.
• W2016349625 cites W176868179 @default.
• W2016349625 cites W1964904206 @default.
• W2016349625 cites W1996226023 @default.
• W2016349625 cites W2009681750 @default.
• W2016349625 cites W2053798150 @default.
• W2016349625 cites W2063319286 @default.
• W2016349625 cites W2081986034 @default.
• W2016349625 cites W2090924238 @default.
• W2016349625 cites W2157776156 @default.
• W2016349625 cites W3119590325 @default.
• W2016349625 cites W32342942 @default.
• W2016349625 cites W4243716175 @default.
• W2016349625 doi "https://doi.org/10.1111/j.1432-1033.1970.tb01056.x" @default.
• W2016349625 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/5456132" @default.
• W2016349625 hasPublicationYear "1970" @default.
• W2016349625 type Work @default.
• W2016349625 sameAs 2016349625 @default.
• W2016349625 citedByCount "13" @default.
• W2016349625 crossrefType "journal-article" @default.
• W2016349625 hasAuthorship W2016349625A5039833815 @default.
• W2016349625 hasAuthorship W2016349625A5044134666 @default.
• W2016349625 hasConcept C131779359 @default.
• W2016349625 hasConcept C178790620 @default.
• W2016349625 hasConcept C183882617 @default.
• W2016349625 hasConcept C184651966 @default.
• W2016349625 hasConcept C185592680 @default.
• W2016349625 hasConcept C188027245 @default.
• W2016349625 hasConcept C204921945 @default.
• W2016349625 hasConcept C2777454769 @default.
• W2016349625 hasConcept C2778439535 @default.
• W2016349625 hasConcept C2781066024 @default.
• W2016349625 hasConcept C32909587 @default.
• W2016349625 hasConcept C521977710 @default.
• W2016349625 hasConcept C71240020 @default.
• W2016349625 hasConcept C90260826 @default.
• W2016349625 hasConceptScore W2016349625C131779359 @default.
• W2016349625 hasConceptScore W2016349625C178790620 @default.
• W2016349625 hasConceptScore W2016349625C183882617 @default.
• W2016349625 hasConceptScore W2016349625C184651966 @default.
• W2016349625 hasConceptScore W2016349625C185592680 @default.
• W2016349625 hasConceptScore W2016349625C188027245 @default.
• W2016349625 hasConceptScore W2016349625C204921945 @default.
• W2016349625 hasConceptScore W2016349625C2777454769 @default.
• W2016349625 hasConceptScore W2016349625C2778439535 @default.
• W2016349625 hasConceptScore W2016349625C2781066024 @default.
• W2016349625 hasConceptScore W2016349625C32909587 @default.
• W2016349625 hasConceptScore W2016349625C521977710 @default.
• W2016349625 hasConceptScore W2016349625C71240020 @default.
• W2016349625 hasConceptScore W2016349625C90260826 @default.
• W2016349625 hasIssue "1" @default.
• W2016349625 hasLocation W20163496251 @default.
• W2016349625 hasLocation W20163496252 @default.
• W2016349625 hasOpenAccess W2016349625 @default.
• W2016349625 hasPrimaryLocation W20163496251 @default.
• W2016349625 hasRelatedWork W1981078824 @default.
• W2016349625 hasRelatedWork W1985697497 @default.
• W2016349625 hasRelatedWork W2069219306 @default.
• W2016349625 hasRelatedWork W2082309963 @default.
• W2016349625 hasRelatedWork W2767655563 @default.
• W2016349625 hasRelatedWork W2775008479 @default.
• W2016349625 hasRelatedWork W2792948240 @default.
• W2016349625 hasRelatedWork W2951027541 @default.
• W2016349625 hasRelatedWork W3124659720 @default.
• W2016349625 hasRelatedWork W4320081172 @default.
• W2016349625 hasVolume "16" @default.
• W2016349625 isParatext "false" @default.
• W2016349625 isRetracted "false" @default.
• W2016349625 magId "2016349625" @default.
• W2016349625 workType "article" @default.