FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W1997307310> ?p ?o ?g. }

• W1997307310 endingPage "684" @default.
• W1997307310 startingPage "673" @default.
• W1997307310 abstract "The first structure of an NAD-dependent tartrate dehydrogenase (TDH) has been solved to 2 Å resolution by single anomalous diffraction (SAD) phasing as a complex with the intermediate analog oxalate, Mg 2+ and NADH. This TDH structure from Pseudomonas putida has a similar overall fold and domain organization to other structurally characterized members of the hydroxy-acid dehydrogenase family. However, there are considerable differences between TDH and these functionally related enzymes in the regions connecting the core secondary structure and in the relative positioning of important loops and helices. The active site in these complexes is highly ordered, allowing the identification of the substrate-binding and cofactor-binding groups and the ligands to the metal ions. Residues from the adjacent subunit are involved in both the substrate and divalent metal ion binding sites, establishing a dimer as the functional unit and providing structural support for an alternating-site reaction mechanism. The divalent metal ion plays a prominent role in substrate binding and orientation, together with several active-site arginines. Functional groups from both subunits form the cofactor-binding site and the ammonium ion aids in the orientation of the nicotinamide ring of the cofactor. A lysyl amino group (Lys192) is the base responsible for the water-mediated proton abstraction from the C2 hydroxyl group of the substrate that begins the catalytic reaction, followed by hydride transfer to NAD. A tyrosyl hydroxyl group (Tyr141) functions as a general acid to protonate the enolate intermediate. Each substrate undergoes the initial hydride transfer, but differences in substrate orientation are proposed to account for the different reactions catalyzed by TDH." @default.
• W1997307310 created "2016-06-24" @default.
• W1997307310 creator A5066190989 @default.
• W1997307310 creator A5079690417 @default.
• W1997307310 date "2010-05-15" @default.
• W1997307310 modified "2023-10-11" @default.
• W1997307310 title "Structural characterization of tartrate dehydrogenase: a versatile enzyme catalyzing multiple reactions" @default.
• W1997307310 cites W1539796472 @default.
• W1997307310 cites W1572417952 @default.
• W1997307310 cites W1591680814 @default.
• W1997307310 cites W1726597626 @default.
• W1997307310 cites W1966463163 @default.
• W1997307310 cites W1968419546 @default.
• W1997307310 cites W1973186501 @default.
• W1997307310 cites W1974984388 @default.
• W1997307310 cites W1980000179 @default.
• W1997307310 cites W1980534387 @default.
• W1997307310 cites W1986408552 @default.
• W1997307310 cites W1986556165 @default.
• W1997307310 cites W1987816347 @default.
• W1997307310 cites W1995536194 @default.
• W1997307310 cites W2005407226 @default.
• W1997307310 cites W2007381478 @default.
• W1997307310 cites W2012369631 @default.
• W1997307310 cites W2018164461 @default.
• W1997307310 cites W2018948641 @default.
• W1997307310 cites W2028961289 @default.
• W1997307310 cites W2038840577 @default.
• W1997307310 cites W2042037311 @default.
• W1997307310 cites W2049704732 @default.
• W1997307310 cites W2054271955 @default.
• W1997307310 cites W2062129432 @default.
• W1997307310 cites W2071136230 @default.
• W1997307310 cites W2079937312 @default.
• W1997307310 cites W2083426861 @default.
• W1997307310 cites W2083437014 @default.
• W1997307310 cites W2094817025 @default.
• W1997307310 cites W2098512408 @default.
• W1997307310 cites W2112200653 @default.
• W1997307310 cites W2144081223 @default.
• W1997307310 doi "https://doi.org/10.1107/s0907444910008851" @default.
• W1997307310 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2879355" @default.
• W1997307310 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/20516620" @default.
• W1997307310 hasPublicationYear "2010" @default.
• W1997307310 type Work @default.
• W1997307310 sameAs 1997307310 @default.
• W1997307310 citedByCount "11" @default.
• W1997307310 countsByYear W19973073102012 @default.
• W1997307310 countsByYear W19973073102014 @default.
• W1997307310 countsByYear W19973073102015 @default.
• W1997307310 countsByYear W19973073102016 @default.
• W1997307310 countsByYear W19973073102017 @default.
• W1997307310 countsByYear W19973073102018 @default.
• W1997307310 countsByYear W19973073102019 @default.
• W1997307310 crossrefType "journal-article" @default.
• W1997307310 hasAuthorship W1997307310A5066190989 @default.
• W1997307310 hasAuthorship W1997307310A5079690417 @default.
• W1997307310 hasBestOaLocation W19973073102 @default.
• W1997307310 hasConcept C107824862 @default.
• W1997307310 hasConcept C181199279 @default.
• W1997307310 hasConcept C185592680 @default.
• W1997307310 hasConcept C18903297 @default.
• W1997307310 hasConcept C197957613 @default.
• W1997307310 hasConcept C2776317432 @default.
• W1997307310 hasConcept C2776376580 @default.
• W1997307310 hasConcept C2777289219 @default.
• W1997307310 hasConcept C2779268744 @default.
• W1997307310 hasConcept C2780543182 @default.
• W1997307310 hasConcept C41183919 @default.
• W1997307310 hasConcept C55493867 @default.
• W1997307310 hasConcept C71240020 @default.
• W1997307310 hasConcept C75520062 @default.
• W1997307310 hasConcept C8010536 @default.
• W1997307310 hasConcept C86803240 @default.
• W1997307310 hasConceptScore W1997307310C107824862 @default.
• W1997307310 hasConceptScore W1997307310C181199279 @default.
• W1997307310 hasConceptScore W1997307310C185592680 @default.
• W1997307310 hasConceptScore W1997307310C18903297 @default.
• W1997307310 hasConceptScore W1997307310C197957613 @default.
• W1997307310 hasConceptScore W1997307310C2776317432 @default.
• W1997307310 hasConceptScore W1997307310C2776376580 @default.
• W1997307310 hasConceptScore W1997307310C2777289219 @default.
• W1997307310 hasConceptScore W1997307310C2779268744 @default.
• W1997307310 hasConceptScore W1997307310C2780543182 @default.
• W1997307310 hasConceptScore W1997307310C41183919 @default.
• W1997307310 hasConceptScore W1997307310C55493867 @default.
• W1997307310 hasConceptScore W1997307310C71240020 @default.
• W1997307310 hasConceptScore W1997307310C75520062 @default.
• W1997307310 hasConceptScore W1997307310C8010536 @default.
• W1997307310 hasConceptScore W1997307310C86803240 @default.
• W1997307310 hasIssue "6" @default.
• W1997307310 hasLocation W19973073101 @default.
• W1997307310 hasLocation W19973073102 @default.
• W1997307310 hasLocation W19973073103 @default.
• W1997307310 hasLocation W19973073104 @default.
• W1997307310 hasOpenAccess W1997307310 @default.
• W1997307310 hasPrimaryLocation W19973073101 @default.
• W1997307310 hasRelatedWork W2037702679 @default.

• next