title: Purification and properties of adenosine 5'-phosphosulfate deaminating enzyme from marine macroalga Gloiopeltis furcata.
abstract: An enzyme which catalyzed the hydrolytic removal of the 6-amino group of adenosine 5'-phosphosulfate (APS) into inosine 5'-phosphosulfate was purified from the marine red macroalga Gloiopeltis furcata by means of salt fractionation, affinity, anion-exchange, and hydrophobic interaction chromatographies. The native enzyme had a Mr of about 285,000. Dissociation yielded a form with a Mr of about 70,000. The enzyme catalyzed the irreversible deamination of adenosine and its 5'-substituted compounds in addition to APS. Thus the enzyme seemed to be a nonspecific adenine nucleotide deaminase. Some properties were determined and compared with those of other nonspecific adenine nucleotide deaminases.
authors.affiliation: Department of Marine Biochemistry, School of Fisheries Sciences, Kitasato University, Japan.
authors.forename: N
authors.initials: N
authors.lastname: Kanno
authors.forename: M
authors.initials: M
authors.lastname: Sato
authors.forename: Y
authors.initials: Y
authors.lastname: Sato
mesh_terms: D000250:Adenosine Phosphosulfate / Q000378:metabolism*; D002413:Cations, Divalent / Q000494:pharmacology; D005591:Chemical Fractionation; D002846:Chromatography, Affinity; D002852:Chromatography, Ion Exchange; D003641:Deamination; D004591:Electrophoresis, Polyacrylamide Gel; D006868:Hydrolysis; D007291:Inosine Monophosphate / Q000031:analogs & derivatives* / Q000378:metabolism; D008970:Molecular Weight; D009709:Nucleotide Deaminases / Q000302:isolation & purification* / Q000378:metabolism; D000461:Rhodophyta / Q000201:enzymology* / Q000302:isolation & purification; D013194:Staining and Labeling; D013379:Substrate Specificity
chemical_list: D002413:Cations, Divalent; D007291:Inosine Monophosphate; C070346:inosine 5'-phosphosulfate; D000250:Adenosine Phosphosulfate; D009709:Nucleotide Deaminases; C019600:adenosine(phosphate) deaminase