Purification and Properties of Adenosine-5’-Phosphosulfate Kinase from the Marine Red Macroalga Porphyra yezoensis Ueda

N. Kanno, M. Sato, Y. Sato

Research output: Contribution to journalArticlepeer-review

7 Citations (Scopus)

Abstract

Adenosine-5′-phosphosulfate kinase (ATP: adenylylsulfate-3′-phosphotransferase, EC 2.7.1.25) was purified from the thalli of the marine alga Porphyra yezoensis by means of salt fractionation, affinity, gel filtration, and ion exchange chromatography. The native enzyme had a Mr of about 61000. Dissociation yielded a form of Mr about 31000. The maximum enzyme activity was at pH 7.0, and requires a divalent metal ion. Triphosphates of adenosine, cytidine, guanine, inosine, and uridine were active as the phosphate donor substrate. Adenosine-5′-phosphosulfate exhibited potent substrate inhibition; the optimal concentration was 3.0 μM in the presence of excess ATP and Mg2+. Michaelis constants for APS and ATP were 0.45 μM and 0.46 mM, respectively.

Original languageEnglish
Pages (from-to)369-374
Number of pages6
JournalBotanica Marina
Volume33
Issue number4
DOIs
Publication statusPublished - 1990 Jan 1

ASJC Scopus subject areas

  • Ecology, Evolution, Behavior and Systematics
  • Aquatic Science
  • Plant Science

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