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Methionine 500, the site of covalent attachment of an active site-directed reagent of beta-galactosidase

Fowler, A.V.; Zabin, I.; Sinnott, M.L.; Zabin, I.

Journal of Biological Chemistry 253(15): 5283-5285

1978


ISSN/ISBN: 0021-9258
PMID: 97290
Accession: 038958093

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The site of attachment to beta-galactosidase of the active site-directed inhibitor, beta-D-galactopyranosylmethyl p-nitrophenyl triazene, was determined. When the enzyme is completely inactivated, 1 mol of the galactopyranosylmethyl group is bound per mol of monomer with retention of the tetrameric structure. After reaction with the [14C]methyl reagent, labeled peptides were isolated and analyzed. The radioactive label was found to be covalently bound to methionine residue 500.

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