| First Author | Fronda CL | Year | 1999 |
| Journal | Biochem Biophys Res Commun | Volume | 258 |
| Issue | 3 | Pages | 727-31 |
| PubMed ID | 10329453 | Mgi Jnum | J:55763 |
| Mgi Id | MGI:1339382 | Doi | 10.1006/bbrc.1999.0698 |
| Citation | Fronda CL, et al. (1999) Molecular cloning and expression of mouse brain sialidase. Biochem Biophys Res Commun 258(3):727-31 |
| abstractText | Sialidase (EC 3.2.1.18) catalyzes the release of sialic acid from sialo-oligosaccharides, gangliosides, or sialo-glycoproteins. In this investigation, we cloned a novel cDNA for mouse brain sialidase and expressed the cDNA in COS-7 cells. This 1,699 bp cDNA codes for a 41.6 kDa protein consisting of 372 deduced amino acid residues. In COS-7 cells transiently transfected with the cDNA, a 250-fold increase was observed in specific activity toward 2'-(4-methylumbelliferyl)-alpha-D-N-acetylneuraminic acid. Similarity searches of the nonredundant GenBank peptide sequence database by the PSI-BLAST program identified rat, hamster, human, and bacterial sialidases homologous to this mouse brain sialidase. Amino acid sequence identities to rat and hamster sialidases (84% and 77%, respectively) suggest that this form of sialidase is conserved in rodents. Sequence identities to human and mouse lysosomal sialidases (30% and 28%, respectively) indicate that the mouse brain sialidase is distinct from the lysosomal enzyme. Mouse brain sialidase has two amino acid sequence motifs common to bacterial sialidases: the 'F/YRIP' motif and the 'Asp-box' motif. The 'F/YRIP' motif is present near the N terminus while two 'Asp-box' motifs are present downstream. Copyright 1999 Academic Press. |
