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Sökning: onr:"swepub:oai:DiVA.org:uu-121136" > Structure-activity ...

LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00003042naa a2200301 4500
001oai:DiVA.org:uu-121136
003SwePub
008100318s1987 | |||||||||||000 ||eng|
024a urn:nbn:se:uu:diva-1211362 urn
040 a (SwePub)uu
041 a engb eng
042 9 SwePub
072 7a ref2 swepub-contenttype
072 7a art2 swepub-publicationtype
100a Danielson, U Helenau Uppsala universitet,Biokemi4 aut0 (Swepub:uu)helenads
2451 0a Structure-activity relationships of 4-hydroxyalkenals in the conjugation catalysed by mammalian glutathione transferases
264 1c 1987
338 a print2 rdacarrier
520 a The substrate specificities of 15 cytosolic glutathione transferases from rat, mouse and man have been explored by use of a homologous series of 4-hydroxyalkenals, extending from 4-hydroxypentenal to 4-hydroxypentadecenal. Rat glutathione transferase 8-8 is exceptionally active with the whole range of 4-hydroxyalkenals, from C5 to C15. Rat transferase 1-1, although more than 10-fold less efficient than transferase 8-8, is the second most active transferase with the longest chain length substrates. Other enzyme forms showing high activities with these substrates are rat transferase 4-4 and human transferase mu. The specificity constants, kcat./Km, for the various enzymes have been determined with the 4-hydroxyalkenals. From these constants the incremental Gibbs free energy of binding to the enzyme has been calculated for the homologous substrates. The enzymes responded differently to changes in the length of the hydrocarbon side chain and could be divided into three groups. All glutathione transferases displayed increased binding energy in response to increased hydrophobicity of the substrate. For some of the enzymes, steric limitations of the active site appear to counteract the increase in binding strength afforded by increased chain length of the substrate. Comparison of the activities with 4-hydroxyalkenals and other activated alkenes provides information about the active-site properties of certain glutathione transferases. The results show that the ensemble of glutathione transferases in a given species may serve an important physiological role in the conjugation of the whole range of 4-hydroxyalkenals. In view of its high catalytic efficiency with all the homologues, rat glutathione transferase 8-8 appears to have evolved specifically to serve in the detoxication of these reactive compounds of oxidative metabolism.
650 7a NATURAL SCIENCESx Chemical Sciences0 (SwePub)1042 hsv//eng
650 7a NATURVETENSKAPx Kemi0 (SwePub)1042 hsv//swe
653 a Chemistry
653 a Kemi
700a Esterbauer, Hermann4 aut
700a Mannervik, Bengt4 aut
710a Uppsala universitetb Biokemi4 org
773t Biochemical Journalg 247:3, s. 707-713q 247:3<707-713x 0264-6021x 1470-8728
8564 8u http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-121136x lärosäteslänky Till lärosätets (uu) databas

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