| Title | Identification of Glu-268 as the catalytic nucleophile of human lysosomal beta-galactosidase precursor by mass spectrometry |
| Publication Type | Journal Article |
| Year of Publication | 1997 |
| Authors | MCCARTER, JD, Burgoyne, DL, MIAO, SC, Zhang, SQ, Callahan, JW, Withers, SG |
| Journal | JOURNAL OF BIOLOGICAL CHEMISTRY |
| Volume | 272 |
| Pagination | 396-400 |
| Date Published | JAN 3 |
| ISSN | 0021-9258 |
| 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. |