FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2053348696> ?p ?o ?g. }

• W2053348696 endingPage "16194" @default.
• W2053348696 startingPage "16187" @default.
• W2053348696 abstract "The hGSTM3 subunit, which is preferentially expressed in germ-line cells, has the greatest sequence divergence among the human mu class glutathione S-transferases. To determine a structural basis for the catalytic differences between hGSTM3-3 and other mu class enzymes, chimeric proteins were designed by modular interchange of the divergent C-terminal domains of hGSTM3 and hGSTM5 subunits. Replacement of 24 residues of the C-terminal segment of either subunit produced chimeric enzymes with catalytic properties that reflected those of the wild-type enzyme from which the C-terminus had been derived. Deletion of the tripeptide C-terminal extension found only in the hGSTM3 subunit had no effect on catalysis. The crystal structure determined for a ligand-free hGSTM3 subunit indicates that an Asn212 residue of the C-terminal domain is near a hydrophobic cluster of side chains formed in part by Ile13, Leu16, Leu114, Ile115, Tyr119, Ile211, and Trp218. Accordingly, a series of point mutations were introduced into the hGSTM3 subunit, and it was indeed determined that a Y119F mutation considerably enhanced the turnover rate of the enzyme for nucleophilic aromatic substitution reactions. A more striking effect was observed for a double mutant (Y119F/N212F) which had a k(cat)/K(m)(CDNB) value of 7.6 x 10(5) s(-)(1) M(-)(1) as compared to 4.9 x 10(3) s(-)(1) M(-)(1) for the wild-type hGSTM3-3 enzyme. The presence of a polar Asn212 in place of a Phe residue found in the cognate position of other mu class glutathione S-transferases, therefore, has a marked influence on catalysis by hGSTM3-3." @default.
• W2053348696 created "2016-06-24" @default.
• W2053348696 creator A5007264361 @default.
• W2053348696 creator A5014722328 @default.
• W2053348696 creator A5043517283 @default.
• W2053348696 date "1999-11-11" @default.
• W2053348696 modified "2023-09-23" @default.
• W2053348696 title "An Asparagine-Phenylalanine Substitution Accounts for Catalytic Differences between hGSTM3-3 and Other Human Class Mu Glutathione <i>S</i>-Transferases^," @default.
• W2053348696 cites W1486158855 @default.
• W2053348696 cites W1489526459 @default.
• W2053348696 cites W1547383512 @default.
• W2053348696 cites W1566237859 @default.
• W2053348696 cites W1572376186 @default.
• W2053348696 cites W2010646940 @default.
• W2053348696 cites W2023287483 @default.
• W2053348696 cites W2028767577 @default.
• W2053348696 cites W2033852172 @default.
• W2053348696 cites W2048414704 @default.
• W2053348696 cites W2064035407 @default.
• W2053348696 cites W2074461690 @default.
• W2053348696 cites W2091894145 @default.
• W2053348696 cites W2110885671 @default.
• W2053348696 cites W2122660076 @default.
• W2053348696 cites W2133048181 @default.
• W2053348696 cites W2151964561 @default.
• W2053348696 cites W2153247725 @default.
• W2053348696 cites W2154011403 @default.
• W2053348696 cites W2167206319 @default.
• W2053348696 cites W2465507770 @default.
• W2053348696 doi "https://doi.org/10.1021/bi991714t" @default.
• W2053348696 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/10587441" @default.
• W2053348696 hasPublicationYear "1999" @default.
• W2053348696 type Work @default.
• W2053348696 sameAs 2053348696 @default.
• W2053348696 citedByCount "23" @default.
• W2053348696 countsByYear W20533486962012 @default.
• W2053348696 countsByYear W20533486962014 @default.
• W2053348696 countsByYear W20533486962015 @default.
• W2053348696 countsByYear W20533486962021 @default.
• W2053348696 countsByYear W20533486962022 @default.
• W2053348696 countsByYear W20533486962023 @default.
• W2053348696 crossrefType "journal-article" @default.
• W2053348696 hasAuthorship W2053348696A5007264361 @default.
• W2053348696 hasAuthorship W2053348696A5014722328 @default.
• W2053348696 hasAuthorship W2053348696A5043517283 @default.
• W2053348696 hasConcept C104292427 @default.
• W2053348696 hasConcept C104317684 @default.
• W2053348696 hasConcept C167392928 @default.
• W2053348696 hasConcept C181199279 @default.
• W2053348696 hasConcept C185592680 @default.
• W2053348696 hasConcept C2775895851 @default.
• W2053348696 hasConcept C515207424 @default.
• W2053348696 hasConcept C55493867 @default.
• W2053348696 hasConcept C71240020 @default.
• W2053348696 hasConceptScore W2053348696C104292427 @default.
• W2053348696 hasConceptScore W2053348696C104317684 @default.
• W2053348696 hasConceptScore W2053348696C167392928 @default.
• W2053348696 hasConceptScore W2053348696C181199279 @default.
• W2053348696 hasConceptScore W2053348696C185592680 @default.
• W2053348696 hasConceptScore W2053348696C2775895851 @default.
• W2053348696 hasConceptScore W2053348696C515207424 @default.
• W2053348696 hasConceptScore W2053348696C55493867 @default.
• W2053348696 hasConceptScore W2053348696C71240020 @default.
• W2053348696 hasIssue "49" @default.
• W2053348696 hasLocation W20533486961 @default.
• W2053348696 hasLocation W20533486962 @default.
• W2053348696 hasOpenAccess W2053348696 @default.
• W2053348696 hasPrimaryLocation W20533486961 @default.
• W2053348696 hasRelatedWork W1581428301 @default.
• W2053348696 hasRelatedWork W1989560554 @default.
• W2053348696 hasRelatedWork W2014288004 @default.
• W2053348696 hasRelatedWork W2059910248 @default.
• W2053348696 hasRelatedWork W2065122081 @default.
• W2053348696 hasRelatedWork W2078894499 @default.
• W2053348696 hasRelatedWork W2150377117 @default.
• W2053348696 hasRelatedWork W2182839848 @default.
• W2053348696 hasRelatedWork W3131068657 @default.
• W2053348696 hasRelatedWork W4230001872 @default.
• W2053348696 hasVolume "38" @default.
• W2053348696 isParatext "false" @default.
• W2053348696 isRetracted "false" @default.
• W2053348696 magId "2053348696" @default.
• W2053348696 workType "article" @default.