PMID: 1599939May 22, 1992Paper

Chemical modification of human placental glutathione transferase by pyridoxal 5'-phosphate

Biochimica Et Biophysica Acta
M Lo BelloG Federici

Abstract

Incubation of GST pi from human placenta with 8 mM PLP resulted in a rapid loss of activity during the first 10 min, concomitant with a Schiff base formation. This inactivation was probably due to the formation of a reversible adduct between PLP and the enzyme. After sodium borohydride treatment this adduct was reduced and stabilized. Stoichiometry and peptide isolation studies showed that three lysine residues were modified during reaction of GST and PLP. Protection of the enzyme against inactivation was achieved in the presence of 4 mM GSH suggesting that at least one lysyl residue is associated with the substrate binding site. Peptide mapping by digesting the enzyme with trypsin revealed that lysine shielded by GSH is Lys-127. Our results suggest that this residue may play an important role in enzymatic activity.

References

May 1, 1990·Archives of Biochemistry and Biophysics·H AhmadA Kurosky
May 20, 1990·Journal of Molecular Biology·M W ParkerG Federici
Jan 1, 1988·CRC Critical Reviews in Biochemistry·B Mannervik, U H Danielson
Oct 1, 1988·The Biochemical Journal·I G CowellJ B Taylor
Nov 1, 1980·The Biochemical Journal·K G Gould, P C Engel
Jan 1, 1981·Methods in Enzymology·W H Habig, W B Jakoby

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