FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2074629800> ?p ?o ?g. }

• W2074629800 abstract "To obtain a clearer understanding of the forces involved in transition state stabilization by Escherichia coli cytidine deaminase, we investigated the thermodynamic changes that accompany substrate binding in the ground state and transition state for substrate hydrolysis. Viscosity studies indicate that the action of cytidine deaminase is not diffusion-limited. Thus, K(m) appears to be a true dissociation constant, and k(cat) describes the chemical reaction of the ES complex, not product release. Enzyme-substrate association is accompanied by a loss of entropy and a somewhat greater release of enthalpy. As the ES complex proceeds to the transition state (ES), there is little further change in entropy, but heat is taken up that almost matches the heat that was released with ES formation. As a result, k(cat)/K(m) (describing the overall conversion of the free substrate to ES is almost invariant with changing temperature. The free energy barrier for the enzyme-catalyzed reaction (k(cat)/K(m)) is much lower than that for the spontaneous reaction (k(non)) (DeltaDeltaG = -21.8 kcal/mol at 25 degrees C). This difference, which also describes the virtual binding affinity of the enzyme for the activated substrate in the transition state (S), is almost entirely enthalpic in origin (DeltaDeltaH = -20.2 kcal/mol), compatible with the formation of hydrogen bonds that stabilize the ES complex. Thus, the transition state affinity of cytidine deaminase increases rapidly with decreasing temperature. When a hydrogen bond between Glu-91 and the 3'-hydroxyl moiety of cytidine is disrupted by truncation of either group, k(cat)/K(m) and transition state affinity are each reduced by a factor of 10(4). This effect of mutation is entirely enthalpic in origin (DeltaDeltaH approximately 7.9 kcal/mol), somewhat offset by a favorable change in the entropy of transition state binding. This increase in entropy is attributed to a loss of constraints on the relative motions of the activated substrate within the ES complex. In an Appendix, some objections to the conventional scheme for transition state binding are discussed." @default.
• W2074629800 created "2016-06-24" @default.
• W2074629800 creator A5000679063 @default.
• W2074629800 creator A5012089733 @default.
• W2074629800 creator A5023183400 @default.
• W2074629800 creator A5027346809 @default.
• W2074629800 creator A5055076632 @default.
• W2074629800 date "2000-07-19" @default.
• W2074629800 modified "2023-09-27" @default.
• W2074629800 title "Temperature Effects on the Catalytic Efficiency, Rate Enhancement, and Transition State Affinity of Cytidine Deaminase, and the Thermodynamic Consequences for Catalysis of Removing a Substrate “Anchor”" @default.
• W2074629800 cites W14797220 @default.
• W2074629800 cites W1553661888 @default.
• W2074629800 cites W1578231679 @default.
• W2074629800 cites W1965029170 @default.
• W2074629800 cites W1966947361 @default.
• W2074629800 cites W1968056768 @default.
• W2074629800 cites W1972607828 @default.
• W2074629800 cites W1977794494 @default.
• W2074629800 cites W1982283265 @default.
• W2074629800 cites W1982627620 @default.
• W2074629800 cites W1983753605 @default.
• W2074629800 cites W1984905663 @default.
• W2074629800 cites W1993871972 @default.
• W2074629800 cites W2002501871 @default.
• W2074629800 cites W2009827762 @default.
• W2074629800 cites W2013379723 @default.
• W2074629800 cites W2016873584 @default.
• W2074629800 cites W2041435911 @default.
• W2074629800 cites W2041931011 @default.
• W2074629800 cites W2052194557 @default.
• W2074629800 cites W2052997154 @default.
• W2074629800 cites W2053954005 @default.
• W2074629800 cites W2057498265 @default.
• W2074629800 cites W2067057552 @default.
• W2074629800 cites W2073655863 @default.
• W2074629800 cites W2074868165 @default.
• W2074629800 cites W2075134157 @default.
• W2074629800 cites W2081609898 @default.
• W2074629800 cites W2091002165 @default.
• W2074629800 cites W2093872563 @default.
• W2074629800 cites W2102072648 @default.
• W2074629800 cites W2110092173 @default.
• W2074629800 cites W2141029077 @default.
• W2074629800 cites W2142322696 @default.
• W2074629800 cites W4253172274 @default.
• W2074629800 doi "https://doi.org/10.1021/bi000914y" @default.
• W2074629800 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/10933791" @default.
• W2074629800 hasPublicationYear "2000" @default.
• W2074629800 type Work @default.
• W2074629800 sameAs 2074629800 @default.
• W2074629800 citedByCount "94" @default.
• W2074629800 countsByYear W20746298002012 @default.
• W2074629800 countsByYear W20746298002013 @default.
• W2074629800 countsByYear W20746298002014 @default.
• W2074629800 countsByYear W20746298002015 @default.
• W2074629800 countsByYear W20746298002016 @default.
• W2074629800 countsByYear W20746298002017 @default.
• W2074629800 countsByYear W20746298002018 @default.
• W2074629800 countsByYear W20746298002019 @default.
• W2074629800 countsByYear W20746298002020 @default.
• W2074629800 countsByYear W20746298002021 @default.
• W2074629800 countsByYear W20746298002022 @default.
• W2074629800 countsByYear W20746298002023 @default.
• W2074629800 crossrefType "journal-article" @default.
• W2074629800 hasAuthorship W2074629800A5000679063 @default.
• W2074629800 hasAuthorship W2074629800A5012089733 @default.
• W2074629800 hasAuthorship W2074629800A5023183400 @default.
• W2074629800 hasAuthorship W2074629800A5027346809 @default.
• W2074629800 hasAuthorship W2074629800A5055076632 @default.
• W2074629800 hasConcept C111368507 @default.
• W2074629800 hasConcept C112887158 @default.
• W2074629800 hasConcept C121332964 @default.
• W2074629800 hasConcept C127313418 @default.
• W2074629800 hasConcept C13053905 @default.
• W2074629800 hasConcept C146477669 @default.
• W2074629800 hasConcept C147789679 @default.
• W2074629800 hasConcept C148898269 @default.
• W2074629800 hasConcept C161790260 @default.
• W2074629800 hasConcept C178790620 @default.
• W2074629800 hasConcept C181199279 @default.
• W2074629800 hasConcept C185592680 @default.
• W2074629800 hasConcept C2776985229 @default.
• W2074629800 hasConcept C2777289219 @default.
• W2074629800 hasConcept C2781184954 @default.
• W2074629800 hasConcept C3288061 @default.
• W2074629800 hasConcept C32909587 @default.
• W2074629800 hasConcept C41183919 @default.
• W2074629800 hasConcept C57476982 @default.
• W2074629800 hasConcept C62520636 @default.
• W2074629800 hasConcept C71240020 @default.
• W2074629800 hasConcept C75473681 @default.
• W2074629800 hasConcept C8010536 @default.
• W2074629800 hasConcept C89031862 @default.
• W2074629800 hasConcept C93391505 @default.
• W2074629800 hasConcept C97355855 @default.
• W2074629800 hasConceptScore W2074629800C111368507 @default.
• W2074629800 hasConceptScore W2074629800C112887158 @default.
• W2074629800 hasConceptScore W2074629800C121332964 @default.
• W2074629800 hasConceptScore W2074629800C127313418 @default.
• W2074629800 hasConceptScore W2074629800C13053905 @default.

• next