PMID: 2485232Jan 1, 1989Paper

Different reactivity of two brain sialyltransferases towards sulfhydryl reagents. Evidence for a thiol group involved in the nucleotide-sugar binding site of the NeuAc alpha 2-3Gal beta 1-3GalNAc alpha(2-6)sialyltransferase

Glycoconjugate Journal
H Baubichon-CortayP Louisot

Abstract

We have studied the amino-acid residues involved in the catalytic activity of two distinct brain sialyltransferases acting on fetuin and asialofetuin. These two enzymes were strongly inhibited by N-bromosuccinimide, a specific blocking reagent for tryptophan residues. This result suggests the involvement of such residues in the catalytic process of the two sialyltransferases. Furthermore, chemical modifications by various sulfhydryl reagents led to a strong inhibition of the fetuin sialyltransferase while the asialofetuin sialyltransferase was only slightly inhibited. For a more thorough understanding of the thiol inactivation mechanism of the fetuin sialyltransferase, we studied in more detail the reactivity of this enzyme with NEM (N-ethylmaleimide), an irreversible reagent. The time-dependent inactivation followed first-order kinetics and these kinetic data afforded presumptive evidence for the binding of 1 mol NEM per mol of enzyme. Only CMP-NeuAc protected the enzyme against NEM inactivation effectively. MnCl2 did not enhance the protective effect of CMP-NeuAc. The modifications of the fetuin sialyltransferase kinetic parameters by NEM showed a competitive mechanism between NEM and CMP-NeuAc. The results suggest the involv...Continue Reading

References

Dec 1, 1973·Analytical Biochemistry·W Schaffner, C Weissmann
Jan 1, 1984·The International Journal of Biochemistry·L J Wong, S S Wong
Jan 1, 1984·The International Journal of Biochemistry·P BroquetP Louisot

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Citations

Jan 1, 1990·The International Journal of Biochemistry·P ReboulP Louisot
Jan 1, 1991·The International Journal of Biochemistry·P BroquetP Louisot

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