FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W1968943434> ?p ?o ?g. }

• W1968943434 endingPage "490" @default.
• W1968943434 startingPage "483" @default.
• W1968943434 abstract "L-Arginine:glycine amidinotransferase catalyzes the committed step in the biosynthesis of creatine. Eight active-site mutants, D170N, D254N, H303V, D305A, R322E, S355A, C407S, and C410A of recombinant human L-arginine:glycine amidinotransferase were prepared by site-directed mutagenesis and enzymatically characterized. The crystal structures of the three mutants D170N, D254N, and C407S have been determined at 0.28-nm, 0.29-nm and 0.236-nm resolution, respectively. The mutation of active-site residues which are involved in substrate-binding yielded inactive mutants. Substitution of Asp254, which is not directly involved in substrate binding but is thought to transfer protons in concert with the His303 imidazole group, results in a strongly (2000-fold) reduced activity. However, the substitution of Cys410, a residue near the active site but not involved in catalysis or substrate binding, by Ala does not change the kinetic properties with respect to the wild-type enzyme. The loss of enzymatic activity of the D170N, D254N, C407S and likely all other mutants is solely due to the inserted point mutations, affecting substrate binding or transition-state stabilization, and not due to major conformational rearrangements of the protein. These results show that a His-Asp pair on one side of the substrate and a Cys on the other side are key residues for activity and are part of a disjoint triad. The imidazole ring of the His is proposed to act as a general acid/general base during catalysis whereas the Cys acts as a nucleophile analogous to Cys25 of papain-like cysteine proteinases." @default.
• W1968943434 created "2016-06-24" @default.
• W1968943434 creator A5049264802 @default.
• W1968943434 creator A5063495689 @default.
• W1968943434 creator A5078350905 @default.
• W1968943434 date "1997-07-15" @default.
• W1968943434 modified "2023-10-04" @default.
• W1968943434 title "Substrate Binding and Catalysis by L-arginine: Glycine Amidinotransferase - A Mutagenesis and Crystallographic Study" @default.
• W1968943434 cites W145972182 @default.
• W1968943434 cites W1482613827 @default.
• W1968943434 cites W1496660279 @default.
• W1968943434 cites W1519040251 @default.
• W1968943434 cites W1546896179 @default.
• W1968943434 cites W1580463159 @default.
• W1968943434 cites W1591055956 @default.
• W1968943434 cites W1605278057 @default.
• W1968943434 cites W1642041575 @default.
• W1968943434 cites W1836923993 @default.
• W1968943434 cites W1839550468 @default.
• W1968943434 cites W1969222787 @default.
• W1968943434 cites W1973181401 @default.
• W1968943434 cites W1973932773 @default.
• W1968943434 cites W1975015319 @default.
• W1968943434 cites W1975085160 @default.
• W1968943434 cites W1978674468 @default.
• W1968943434 cites W1980525207 @default.
• W1968943434 cites W1984541502 @default.
• W1968943434 cites W1994809856 @default.
• W1968943434 cites W2000596617 @default.
• W1968943434 cites W2004789938 @default.
• W1968943434 cites W2005200435 @default.
• W1968943434 cites W2010597910 @default.
• W1968943434 cites W2011435358 @default.
• W1968943434 cites W2011836912 @default.
• W1968943434 cites W2014694459 @default.
• W1968943434 cites W2018873178 @default.
• W1968943434 cites W2028231353 @default.
• W1968943434 cites W2028436089 @default.
• W1968943434 cites W2040049703 @default.
• W1968943434 cites W2042990275 @default.
• W1968943434 cites W2047067740 @default.
• W1968943434 cites W2068567739 @default.
• W1968943434 cites W2100059026 @default.
• W1968943434 cites W2116275717 @default.
• W1968943434 cites W2149838069 @default.
• W1968943434 cites W51441518 @default.
• W1968943434 cites W75328843 @default.
• W1968943434 doi "https://doi.org/10.1111/j.1432-1033.1997.00483.x" @default.
• W1968943434 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/9266688" @default.
• W1968943434 hasPublicationYear "1997" @default.
• W1968943434 type Work @default.
• W1968943434 sameAs 1968943434 @default.
• W1968943434 citedByCount "12" @default.
• W1968943434 countsByYear W19689434342012 @default.
• W1968943434 countsByYear W19689434342013 @default.
• W1968943434 countsByYear W19689434342016 @default.
• W1968943434 countsByYear W19689434342017 @default.
• W1968943434 countsByYear W19689434342022 @default.
• W1968943434 crossrefType "journal-article" @default.
• W1968943434 hasAuthorship W1968943434A5049264802 @default.
• W1968943434 hasAuthorship W1968943434A5063495689 @default.
• W1968943434 hasAuthorship W1968943434A5078350905 @default.
• W1968943434 hasBestOaLocation W19689434341 @default.
• W1968943434 hasConcept C103408237 @default.
• W1968943434 hasConcept C104317684 @default.
• W1968943434 hasConcept C107824862 @default.
• W1968943434 hasConcept C143065580 @default.
• W1968943434 hasConcept C16318435 @default.
• W1968943434 hasConcept C181199279 @default.
• W1968943434 hasConcept C185592680 @default.
• W1968943434 hasConcept C18903297 @default.
• W1968943434 hasConcept C2777289219 @default.
• W1968943434 hasConcept C2777468819 @default.
• W1968943434 hasConcept C2778460671 @default.
• W1968943434 hasConcept C2779201268 @default.
• W1968943434 hasConcept C41183919 @default.
• W1968943434 hasConcept C515207424 @default.
• W1968943434 hasConcept C55493867 @default.
• W1968943434 hasConcept C71240020 @default.
• W1968943434 hasConcept C86803240 @default.
• W1968943434 hasConceptScore W1968943434C103408237 @default.
• W1968943434 hasConceptScore W1968943434C104317684 @default.
• W1968943434 hasConceptScore W1968943434C107824862 @default.
• W1968943434 hasConceptScore W1968943434C143065580 @default.
• W1968943434 hasConceptScore W1968943434C16318435 @default.
• W1968943434 hasConceptScore W1968943434C181199279 @default.
• W1968943434 hasConceptScore W1968943434C185592680 @default.
• W1968943434 hasConceptScore W1968943434C18903297 @default.
• W1968943434 hasConceptScore W1968943434C2777289219 @default.
• W1968943434 hasConceptScore W1968943434C2777468819 @default.
• W1968943434 hasConceptScore W1968943434C2778460671 @default.
• W1968943434 hasConceptScore W1968943434C2779201268 @default.
• W1968943434 hasConceptScore W1968943434C41183919 @default.
• W1968943434 hasConceptScore W1968943434C515207424 @default.
• W1968943434 hasConceptScore W1968943434C55493867 @default.
• W1968943434 hasConceptScore W1968943434C71240020 @default.
• W1968943434 hasConceptScore W1968943434C86803240 @default.
• W1968943434 hasIssue "2" @default.

• next