MOLECULAR-CLONING OF MOUSE ACID BETA-GALACTOSIDASE CDNA - SEQUENCE, EXPRESSION OF CATALYTIC ACTIVITY AND COMPARISON WITH THE HUMAN ENZYME

A full-length cDNA coding for mouse lysosomal acid β-galatosidase has been isolated on the basis of homology with the human gene. Catalytic activity toward 4-methylumbelliferyl β-D-galactoside in the COS-1 cell expression system provided positive proof for its authenticity. The sequence analysis showed that the degree of similarity between the human and mouse enzymes was approximately 70% in the nucleotide sequence and nearly 80% in the amino acid sequence. The deduced primary amino acid sequences of the enzymes from the two species indicated that, of the seven possible N-glycosylation sites in the human enzyme, five are conserved in the mouse enzyme. Three additional possible N-glycosylation sites, not present in the human enzyme, are found in the primary amino acid sequence of the mouse enzyme. All seven cysteine residues in the mouse enzyme are conserved in the human enzyme. Although the nucleotide sequence could be aligned to 60% identity with the E. coli β-galactosidase, similarity in the amino acid sequence was minimal. © 1990 Academic Press, Inc.