FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2038652228> ?p ?o ?g. }

• W2038652228 endingPage "27401" @default.
• W2038652228 startingPage "27395" @default.
• W2038652228 abstract "A complete amino acid structure of rat liver mercaptopyruvate sulfurtransferase (MST, EC 2.8.1.2) was determined by sequence analysis of cDNA and purified enzyme. The enzyme consists of 296 amino acid residues with a calculated molecular mass of 32,808 Da. Sequence identity in cDNA and the deduced amino acid sequence are 65 and 60% respectively, between rat MST and rhodanese. By their entire sequence similarity MST and rhodanese are confirmed to be evolutionarily related enzymes (Nagahara, N., Okazaki, T., and Nishino, T. (1995) J. Biol. Chem. 270, 16230-16235). The conversion of MST to rhodanese was attempted, and the role of amino acid residues was studied by site-directed mutagenesis with the isolated cDNA of rat liver MST. There is a strong possibility that Cys247 is a catalytic site of MST. Arg187 is suggested to be a binding site of both mercaptopyruvate and thiosulfate in MST. Arg196, which is missed in rhodanese, is important for catalysis in MST. On the other hand, the substitution of Arg for Gly248 or Lys for Ser249 facilitates catalysis of thiosulfate in MST. It is concluded that Arg187 and Arg196 of rat MST are critical residues in determining substrate specificity for mercaptopyruvate. On the other hand, Arg185, Arg247, and Lys248 of rat rhodanese are critical residues in determining substrate specificity for thiosulfate. A complete amino acid structure of rat liver mercaptopyruvate sulfurtransferase (MST, EC 2.8.1.2) was determined by sequence analysis of cDNA and purified enzyme. The enzyme consists of 296 amino acid residues with a calculated molecular mass of 32,808 Da. Sequence identity in cDNA and the deduced amino acid sequence are 65 and 60% respectively, between rat MST and rhodanese. By their entire sequence similarity MST and rhodanese are confirmed to be evolutionarily related enzymes (Nagahara, N., Okazaki, T., and Nishino, T. (1995) J. Biol. Chem. 270, 16230-16235). The conversion of MST to rhodanese was attempted, and the role of amino acid residues was studied by site-directed mutagenesis with the isolated cDNA of rat liver MST. There is a strong possibility that Cys247 is a catalytic site of MST. Arg187 is suggested to be a binding site of both mercaptopyruvate and thiosulfate in MST. Arg196, which is missed in rhodanese, is important for catalysis in MST. On the other hand, the substitution of Arg for Gly248 or Lys for Ser249 facilitates catalysis of thiosulfate in MST. It is concluded that Arg187 and Arg196 of rat MST are critical residues in determining substrate specificity for mercaptopyruvate. On the other hand, Arg185, Arg247, and Lys248 of rat rhodanese are critical residues in determining substrate specificity for thiosulfate." @default.
• W2038652228 created "2016-06-24" @default.
• W2038652228 creator A5011237103 @default.
• W2038652228 creator A5076749307 @default.
• W2038652228 date "1996-11-01" @default.
• W2038652228 modified "2023-09-30" @default.
• W2038652228 title "Role of Amino Acid Residues in the Active Site of Rat Liver Mercaptopyruvate Sulfurtransferase" @default.
• W2038652228 cites W1205458192 @default.
• W2038652228 cites W1482128126 @default.
• W2038652228 cites W1488707055 @default.
• W2038652228 cites W1500638303 @default.
• W2038652228 cites W1502696656 @default.
• W2038652228 cites W1541049200 @default.
• W2038652228 cites W1557324813 @default.
• W2038652228 cites W1560922443 @default.
• W2038652228 cites W1567974798 @default.
• W2038652228 cites W1605210732 @default.
• W2038652228 cites W1961691428 @default.
• W2038652228 cites W1968799270 @default.
• W2038652228 cites W1971440804 @default.
• W2038652228 cites W1977844783 @default.
• W2038652228 cites W1987723857 @default.
• W2038652228 cites W1988422745 @default.
• W2038652228 cites W1996406766 @default.
• W2038652228 cites W1996636367 @default.
• W2038652228 cites W1999631090 @default.
• W2038652228 cites W2000108740 @default.
• W2038652228 cites W2000362364 @default.
• W2038652228 cites W2001444438 @default.
• W2038652228 cites W2012794505 @default.
• W2038652228 cites W2034673370 @default.
• W2038652228 cites W2035715857 @default.
• W2038652228 cites W2036750146 @default.
• W2038652228 cites W2036931150 @default.
• W2038652228 cites W2045689345 @default.
• W2038652228 cites W2065981914 @default.
• W2038652228 cites W2067514936 @default.
• W2038652228 cites W2069925061 @default.
• W2038652228 cites W2074122548 @default.
• W2038652228 cites W2100837269 @default.
• W2038652228 cites W2125625153 @default.
• W2038652228 cites W2129884633 @default.
• W2038652228 cites W2156076210 @default.
• W2038652228 cites W2249033317 @default.
• W2038652228 cites W2416399609 @default.
• W2038652228 cites W305296815 @default.
• W2038652228 cites W4294216491 @default.
• W2038652228 cites W59751624 @default.
• W2038652228 cites W74669722 @default.
• W2038652228 cites W935364044 @default.
• W2038652228 doi "https://doi.org/10.1074/jbc.271.44.27395" @default.
• W2038652228 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/8910318" @default.
• W2038652228 hasPublicationYear "1996" @default.
• W2038652228 type Work @default.
• W2038652228 sameAs 2038652228 @default.
• W2038652228 citedByCount "113" @default.
• W2038652228 countsByYear W20386522282012 @default.
• W2038652228 countsByYear W20386522282013 @default.
• W2038652228 countsByYear W20386522282014 @default.
• W2038652228 countsByYear W20386522282015 @default.
• W2038652228 countsByYear W20386522282016 @default.
• W2038652228 countsByYear W20386522282017 @default.
• W2038652228 countsByYear W20386522282018 @default.
• W2038652228 countsByYear W20386522282019 @default.
• W2038652228 countsByYear W20386522282020 @default.
• W2038652228 countsByYear W20386522282021 @default.
• W2038652228 countsByYear W20386522282022 @default.
• W2038652228 countsByYear W20386522282023 @default.
• W2038652228 crossrefType "journal-article" @default.
• W2038652228 hasAuthorship W2038652228A5011237103 @default.
• W2038652228 hasAuthorship W2038652228A5076749307 @default.
• W2038652228 hasBestOaLocation W20386522281 @default.
• W2038652228 hasConcept C104317684 @default.
• W2038652228 hasConcept C167625842 @default.
• W2038652228 hasConcept C178790620 @default.
• W2038652228 hasConcept C181199279 @default.
• W2038652228 hasConcept C185592680 @default.
• W2038652228 hasConcept C187882448 @default.
• W2038652228 hasConcept C2779033446 @default.
• W2038652228 hasConcept C2779201268 @default.
• W2038652228 hasConcept C2780637352 @default.
• W2038652228 hasConcept C2781090017 @default.
• W2038652228 hasConcept C41183919 @default.
• W2038652228 hasConcept C515207424 @default.
• W2038652228 hasConcept C518881349 @default.
• W2038652228 hasConcept C55493867 @default.
• W2038652228 hasConcept C86803240 @default.
• W2038652228 hasConceptScore W2038652228C104317684 @default.
• W2038652228 hasConceptScore W2038652228C167625842 @default.
• W2038652228 hasConceptScore W2038652228C178790620 @default.
• W2038652228 hasConceptScore W2038652228C181199279 @default.
• W2038652228 hasConceptScore W2038652228C185592680 @default.
• W2038652228 hasConceptScore W2038652228C187882448 @default.
• W2038652228 hasConceptScore W2038652228C2779033446 @default.
• W2038652228 hasConceptScore W2038652228C2779201268 @default.
• W2038652228 hasConceptScore W2038652228C2780637352 @default.
• W2038652228 hasConceptScore W2038652228C2781090017 @default.
• W2038652228 hasConceptScore W2038652228C41183919 @default.

• next