{"database":"biostudies-other","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["143(3)"],"submitter":["Sinnott ML"],"journal":["The Biochemical journal"],"pagination":["751-62"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC1168444"],"abstract":["1. beta-d-Galactopyranosyl pyridinium salts are well-behaved substrates for the beta-galactosidase of Escherichia coli, catalysis occurring by the interaction of the salt itself with the normal active site of the protein. 2. logk(cat.) values for seven such salts show a linear relationship (correlation coefficient=-0.997) with the pK(a) of the parent pyridine. 3. The beta-d-galactopyranosyl derivatives of pyridine and 4-bromoisoquinoline exhibit alpha-deuterium kinetic isotope effects of 1.136+/-0.040 and 1.187+/-0.046 on their enzymic hydrolysis, indicating formation of a galactopyranosyl cation in the rate-limiting step. 4. This behaviour of the pyridinium salts contrasts with the behaviour of aryl galactosides and this contrast can be accommodated by the beta-galactosidase mechanism of Sinnott & Souchard (1973). 5. The alpha-deuterium kinetic isotope effect for the hydrolysis of beta-d-galactopyranosyl azide is 1.098+/-0.033; comparison of the k(cat.) value of the azide with that of a pyridinium salt of the same aglycone pK(a) enables a maximum factor of 70 to be ascribed to the acceleration of the departure of azide by intracomplex general acid catalysis. 6. The possibility of the rate-limiting process in the glycosidase-catalysed hydrolysis of aryl glycosides being a conformation change is considered for a number of glycosidases where correlations of k(cat.) with aglycone acidity, reported in the literature, have been unsuccessful."],"repository":["biostudies-other"],"data_source":["Europe PMC"],"pubmed_authors":["Sinnott ML","Withers SG"],"additional_accession":[]},"is_claimable":false,"name":"The beta-galactosidase-catalysed hydrolyses of beta-d-galactopyranosyl pyridium salts. Rate-limiting generation of an enzyme-bound galactopyranosyl cation in a process dependent only on aglycone acidity.","description":"1. beta-d-Galactopyranosyl pyridinium salts are well-behaved substrates for the beta-galactosidase of Escherichia coli, catalysis occurring by the interaction of the salt itself with the normal active site of the protein. 2. logk(cat.) values for seven such salts show a linear relationship (correlation coefficient=-0.997) with the pK(a) of the parent pyridine. 3. The beta-d-galactopyranosyl derivatives of pyridine and 4-bromoisoquinoline exhibit alpha-deuterium kinetic isotope effects of 1.136+/-0.040 and 1.187+/-0.046 on their enzymic hydrolysis, indicating formation of a galactopyranosyl cation in the rate-limiting step. 4. This behaviour of the pyridinium salts contrasts with the behaviour of aryl galactosides and this contrast can be accommodated by the beta-galactosidase mechanism of Sinnott & Souchard (1973). 5. The alpha-deuterium kinetic isotope effect for the hydrolysis of beta-d-galactopyranosyl azide is 1.098+/-0.033; comparison of the k(cat.) value of the azide with that of a pyridinium salt of the same aglycone pK(a) enables a maximum factor of 70 to be ascribed to the acceleration of the departure of azide by intracomplex general acid catalysis. 6. The possibility of the rate-limiting process in the glycosidase-catalysed hydrolysis of aryl glycosides being a conformation change is considered for a number of glycosidases where correlations of k(cat.) with aglycone acidity, reported in the literature, have been unsuccessful.","dates":{"release":"1974-01-01T00:00:00Z","publication":"1974 Dec","modification":"2019-08-04T08:06:15Z","creation":"2019-08-04T08:06:15Z"},"accession":"S-EPMC1168444","cross_references":{"DOI":["10.1042/bj1430751 "]}}