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J. Biol. Chem., Vol. 266, Issue 21, 13507-13512, Jul, 1991
MM Hermans, MA Kroos, J van Beeumen, BA Oostra and AJ Reuser
The substrate analogue conduritol B epoxide (CBE) is demonstrated to be an
active site-directed inhibitor of human lysosomal alpha-glucosidase. A
competitive mode of inhibition is obtained with glycogen as natural and
4-methylumbelliferyl-alpha-D-glucopyranoside as artificial substrate. The
inactivation of the enzyme is time and concentration dependent and results
in the covalent binding of CBE. Catalytic activity is required for binding
to occur. CBE-labeled peptides containing the catalytic residue of
lysosomal alpha-glucosidase were isolated and identified by microsequencing
and amino acid analysis. The peptides appeared to originate from a protein
domain which is highly conserved among alpha-amylases, maltase,
glucoamylases, and transglucanosylases. Based on the sequence similarity
and the mechanism of CBE binding, Asp-518 is predicted to be the essential
carboxylate in the active site of lysosomal alpha-glucosidase. The
functional importance of Asp-518 and other residues around the catalytic
site was studied by expression of in vitro mutagenized alpha-glucosidase
cDNA in transiently transfected COS cells. Substitution of Asp-513 by
Glu-513 is shown to interfere with the posttranslational modification and
the intracellular transport of the alpha-glucosidase precursor. The
residues Trp-516 and Asp-518 are demonstrated to be critical for catalytic
function.
Human lysosomal alpha-glucosidase. Characterization of the catalytic site
Department of Cell Biology and Genetics, Erasmus University, Rotterdam, The Netherlands.
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