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

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...

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Bibliographic Details
Published in:The Journal of biological chemistry 1978-08, Vol.253 (15), p.5283-5285
Main Authors: Fowler, A V, Zabin, I, Sinnott, M L
Format: Article
Language:English
Subjects:
Amino Acid Sequence
beta-Galactosidase - metabolism
Binding Sites
Galactosidases - metabolism
Galactosides
Methionine
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Summary: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.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(17)30367-8