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Relaxed thiol subst...
Relaxed thiol substrate specificity of glutathione transferase effected by a non-substrate glutathione derivative
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Principato, Giovanni B (författare)
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- Danielson, U Helena (författare)
- Uppsala universitet,Biokemi
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Mannervik, Bengt (författare)
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(creator_code:org_t)
- 2001-10-19
- 1988
- Engelska.
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Ingår i: FEBS Letters. - : Wiley. - 0014-5793 .- 1873-3468. ; 231:1, s. 155-158
- Relaterad länk:
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https://febs.onlinel...
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visa fler...
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- Rat glutathione transferase 4-4 catalysed the conjugation of 2-mercaptoethanol with 1-chloro-2,4-dinitrobenzene in the presence of S-methyl-glutathione. The reaction was linearly dependent on enzyme concentration and saturation was seen with respect to both 2-mercaptoethanol and S-methyl-glutathione concentration. High concentrations of S-methyl-gluta-thione were inhibitory. The results suggest that the natural substrate glutathione has two distinct functions in the normal catalytic reaction, (i) induction of a catalytically competent conformation of the enzyme and (ii) provision of the substrate sulfhydryl group in the reaction catalyzed.
Nyckelord
- Conformational change
- Thiol substrate specificity
- Reaction mechanism
- Glutathione transferase
- Glutathione derivative
- NATURAL SCIENCES
- NATURVETENSKAP
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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