Disease relevance of NAGA

• The 1.9 A structure of alpha-N-acetylgalactosaminidase: molecular basis of glycosidase deficiency diseases [1].
• When enriched CId-1+ splenic T cells from NAGA-immune BALB/c mice were fused with the AKR thymoma BW 5147 cell line, 2 of 72 resulting hybrids, termed CId-1A and CId-1B, were reactive by indirect immunofluorescence with the CId-1 antibody [2].

Psychiatry related information on NAGA

• We have prepared mouse monoclonal antibodies against idiotypic (Id) determinants on chicken antibodies to N-acetylglucosamine (NAGA) and p-aminobenzoic acid (PABA) made by inbred line EL 6(3) birds [3].

High impact information on NAGA

• CId-1, which recognized chicken antibodies to N-acetyl glucosamine (NAGA), and approximately 0.4% of chicken T lymphocytes also reacted with approximately 0.2% of BALB/c splenic Thy-1.2+ cells [2].
• Labeling of the tissue sections was eliminated by chloroform: methanol extraction and reduced by alpha-N-acetylgalactosaminidase digestion, but survived trypsinization [4].
• The structure consisted of a catalytic domain and a C-terminal domain and was essentially the same as that of alpha-N-acetylgalactosaminidase, which is the same member of glycosyl hydrolase family 27 [5].
• The Id determinants were found among antibodies to NAGA and PABA made by outbred and inbred lines of White Leghorn chickens [3].
• Chicken liver alpha-N-acetylgalactosaminidase (alpha AGA) specifically removes terminally alpha-linked alpha-N-acetylgalactosamine from oligosaccharide chains on the surface of group A erythrocytes [6].

Chemical compound and disease context of NAGA

• The monoclonal anti-NAGA Id antibody, termed CId-1, reacted with affinity purified antibodies to NAGA, but not with antibodies specific for PABA, arsanilic acid (Ars), phosphorylcholine (PC), or with normal chicken IgG and IgM [3].

Biological context of NAGA

• The deduced amino acid sequence shows 80% homology with human alpha AGA and about 60% homology with alpha-galactosidases from a number of sources, indicating that these two families of exoglycosidases are evolutionarily related [6].
• The active site residues of alpha-NAGAL are conserved in the closely related enzyme a-galactosidase A (alpha-GAL) [1].
• A cDNA clone encoding the mature polypeptide for the chicken liver alpha-N-acetylgalactosaminidase enzyme was isolated by screening a cDNA library with a synthetic sequence derived from the human alpha-N-acetylgalactosaminidase gene [7].
• Structural studies of alpha-N-acetylgalactosaminidase: effect of glycosylation on the level of expression, secretion efficiency, and enzyme activity [8].
• alpha-N-Acetylgalactosaminidase (alphaNAGAL, EC 3.2.1.49) is an exoglycosidase specific for the hydrolysis of terminal alpha-linked N-acetylgalactosamine from oligosaccharide chains [8].

Associations of NAGA with chemical compounds

• Synthesis and activity of 1-N-iminosugar inhibitors, siastatin B analogues for alpha-N-acetylgalactosaminidase and beta-N-acetylglucosaminidase [9].
• A substitution of Trp-16 with an arginine residue in alpha-N-acetylgalactosaminidase abolished the enzyme activity, which was confirmed by replacing a 600 bp fragment containing the mutation with the corresponding wild-type sequence [10].
• The aim of this study was to identify and characterize C. elegans orthologs to both human lysosomal luminal proteins alpha-GAL and alpha-NAGA [11].
• By expressing site-directed mutants in the methylotrophic yeast strain Pichia pastoris, the role of a tryptophan residue at position 16 in the activity of alpha-galactosidase and alpha-N-acetylgalactosaminidase, two closely related exoglycosidases, was studied [10].

Analytical, diagnostic and therapeutic context of NAGA

• Here, we report the molecular cloning of a alpha AGA cDNA by both library screening and PCR amplification [6].

References