title: The first demonstration of a procaryotic glycosylasparaginase.
abstract: Glycosylasparaginase was purified to near homogeneity from intracellular lysates of Flavobacterium meningosepticum. The enzyme is a heterodimer with an estimated molecular weight of 38 kDa and consists of one alpha-subunit (18 kDa) and one beta-subunit (16 kDa). The beta-subunit of the Flavobacterium enzyme has a direct evolutionary relationship to the beta-subunit of mammalian glycosylasparaginases as evidenced by: (1) strong cross-reactivity with antibodies made to the denatured rat beta-subunit, (2) a high degree of homology with the amino-terminus of the corresponding eukaryotic enzymes, and (3) irreversible inactivation with 5-diazo-4-oxo-L-norvaline, a reagent known to react with the catalytic amino-terminal threonine residue on the beta-subunit of a mammalian glycosylasparaginase.
authors.affiliation: Division of Clinical Sciences, Wadsworth Center for Laboratories and Research, New York State Department of Health, Albany.
authors.forename: A L
authors.initials: AL
authors.lastname: Tarentino
authors.forename: T H
authors.initials: TH
authors.lastname: Plummer
mesh_terms: D000581:Amidohydrolases / Q000235:genetics*; D000595:Amino Acid Sequence; D000622:Aminolevulinic Acid / Q000031:analogs & derivatives / Q000494:pharmacology; D001227:Aspartylglucosylaminase / Q000037:antagonists & inhibitors / Q000276:immunology / Q000302:isolation & purification / Q000378:metabolism*; D002240:Carbohydrate Sequence; D003429:Cross Reactions; D005417:Flavobacterium / Q000201:enzymology*; D008969:Molecular Sequence Data; D043524:Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase; D011487:Protein Conformation; D011489:Protein Denaturation; D017421:Sequence Analysis; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity
chemical_list: C002199:5-diazo-4-oxonorvaline; D000622:Aminolevulinic Acid; D000581:Amidohydrolases; D001227:Aspartylglucosylaminase; D043524:Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase