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Glycosylation and phosphorylation of arylsulfatase A. 1994

H J Sommerlade, and T Selmer, and A Ingendoh, and V Gieselmann, and K von Figura, and K Neifer, and B Schmidt
Georg-August-Universität, Zentrum für Biochemie und Molekulare Zellbiologie, Abteilung Biochemie II, Göttingen, Federal Republic of Germany.

The glycosylation and phosphorylation of the lysosomal enzyme arylsulfatase A was analyzed by a combination of metabolic labeling, tryptic fragmentation, mass spectrometry, and radiosequencing. The results demonstrate that all three potential N-glycosylation sites at Asn residues 158, 184, and 350 are utilized in arylsufatase A and carry high mannose or hybride type oligosaccharides. Phosphorylation of mannose residues is restricted to oligosaccharides at the first and third N-glycosylation site (Asn-158 and Asn-350). Both are phosphorylated with comparable efficiency. An earlier study had shown that a mutant arylsulfatase A containing only the second N-glycosylation site at Asn-184 folds correctly and is phosphorylated (Gieselmann, V., Schmidt, B., and von Figura, K. (1992) J. Biol. Chem. 267, 13262-13266). The lack of phosphorylation at Asn-184 in wild type arylsulfatase A therefore indicates that in vivo the presence of oligosaccharides can interfere with phosphorylation of other sites or that phosphorylation occurs in an ordered manner whereby phosphorylation of one site can affect the phosphorylation of another site.

UI MeSH Term Description Entries
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D010766 Phosphorylation The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety. Phosphorylations
D002478 Cells, Cultured Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others. Cultured Cells,Cell, Cultured,Cultured Cell
D002553 Cerebroside-Sulfatase An enzyme that catalyzes the hydrolysis of cerebroside 3-sulfate (sulfatide) to yield a cerebroside and inorganic sulfate. A marked deficiency of arylsulfatase A, which is considered the heat-labile component of cerebroside sulfatase, has been demonstrated in all forms of metachromatic leukodystrophy (LEUKODYSTROPHY, METACHROMATIC). EC 3.1.6.8. Arylsulfatase A,Sulfatidate Sulfatase,Cerebroside Sulfatase,Sulfatase, Sulfatidate
D002851 Chromatography, High Pressure Liquid Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed. Chromatography, High Performance Liquid,Chromatography, High Speed Liquid,Chromatography, Liquid, High Pressure,HPLC,High Performance Liquid Chromatography,High-Performance Liquid Chromatography,UPLC,Ultra Performance Liquid Chromatography,Chromatography, High-Performance Liquid,High-Performance Liquid Chromatographies,Liquid Chromatography, High-Performance
D006031 Glycosylation The synthetic chemistry reaction or enzymatic reaction of adding carbohydrate or glycosyl groups. GLYCOSYLTRANSFERASES carry out the enzymatic glycosylation reactions. The spontaneous, non-enzymatic attachment of reducing sugars to free amino groups in proteins, lipids, or nucleic acids is called GLYCATION (see MAILLARD REACTION). Protein Glycosylation,Glycosylation, Protein
D006224 Cricetinae A subfamily in the family MURIDAE, comprising the hamsters. Four of the more common genera are Cricetus, CRICETULUS; MESOCRICETUS; and PHODOPUS. Cricetus,Hamsters,Hamster
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D006868 Hydrolysis The process of cleaving a chemical compound by the addition of a molecule of water.
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein

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