@article { ISI:A1997WA56400061,
	title = {Identification of Glu-268 as the catalytic nucleophile of human lysosomal beta-galactosidase precursor by mass spectrometry},
	journal = {JOURNAL OF BIOLOGICAL CHEMISTRY},
	volume = {272},
	number = {1},
	year = {1997},
	month = {JAN 3},
	pages = {396-400},
	abstract = {Human lysosomal beta-galactosidase catalyzes the hydrolysis of beta-galactosides via a double displacement mechanism involving a covalent glycosyl enzyme intermediate. By use of the slow substrate 2,4-dinitrophenyl-2-deoxy-2-fluoro- beta-D-galactopyranoside, a glycosyl enzyme intermediate has been trapped on the enzyme. This has allowed the catalytic nucleophile to be identified as Glu-268 by peptic and tryptic digestion of the inactivated enzyme followed by high performance liquid chromatography-electrospray ionization tandem mass spectrometry of the peptide mixture. This glutamic acid is fully conserved in a sequence-related family of enzymes (Family 35), consistent with its essential role.},
	issn = {0021-9258},
	author = {MCCARTER, JD and Burgoyne, DL and MIAO, SC and Zhang, SQ and Callahan, JW and Withers, SG}
}
