Cloning and characterization of NEU2, a human gene homologous to rodent soluble sialidases

Sialidases (EC 3.2.1.18) are a group of glycohydrolytic enzymes, widely dis tributed in nature, that cleave sialic acid residues from the oligosacchari de components of glycoconjugates. All of the sialidase enzymes thus far cha racterized share an Asp block, repeated three to five times in the primary structure, and an F/YRIP sequence motif that is part of the active site. Us ing a sequence homology-based approach, we have identified a novel human ge ne, named NEU2, mapping to chromosome 2q37. The nucleotide sequence analysi s of the gene has shown that it contains only one intron of about 1.25 kb, and the longest open reading frame encodes a protein of 380 amino acids, wi th a two-Asp block consensus, and the YRIP sequence. In the putative promot er sequence there are a classical TATAA box and four E boxes, which are con sensus binding sites for muscle-specific transcription factors. Northern bl ot analysis revealed expression of the NEU2 transcript only in skeletal mus cle. (C) 1999 Academic Press.