Role of thioltransferases on the modulation of rat liver S-adenosylmethionine synthetase activity by glutathione

FEBS Letters
M L Martínez-Chantar, M A Pajares

Abstract

Rat liver S-adenosylmethionine synthetase, high- and low-Mr forms, are regulated in vitro by the GSH/GSSG ratio at pH 8. The inhibition and oxidation constants for both forms have been calculated in the presence of thioltransferases. The mechanism of the reaction appeared to involve the formation of intramolecular disulfides. Increases of 3- to 4-fold in the oxidation constants for both S-adenosylmethionine synthetase isoenzymes in the presence of protein disulfide isomerase suggested the possibility of a thiol-disulfide exchange regulatory mechanism for this enzyme in vivo. The significance of these results is discussed on the light of the data available relating glutathione changes and modulation of enzyme activities, either in vivo and in vitro.

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Citations

Dec 22, 1999·European Journal of Biochemistry·M L Martínez-Chantar, M A Pajares
Oct 16, 2013·Antioxidants & Redox Signaling·Miguel DelgadoMaría Angeles Pajares
Feb 23, 2010·Journal of Biochemical and Molecular Toxicology·Tomoyuki TeradaTsutomu Nishihara
Jun 30, 2000·Protein Expression and Purification·M C López-VaraM A Pajares
May 23, 2014·Frontiers in Pharmacology·José L García-Giménez, Federico V Pallardó
Jul 29, 2016·Journal of Biochemistry·Jette PretzelEsther Jortzik
Aug 23, 2016·PloS One·Claudia PérezMaría A Pajares
Dec 1, 2017·Antioxidants & Redox Signaling·María A Pajares, Dolores Pérez-Sala
Mar 27, 2020·Frontiers in Pharmacology·María A PajaresDolores Pérez-Sala
Dec 24, 2002·The Journal of Biological Chemistry·Gabino F Sanchez-PerezMaria A Pajares

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