Inhibition of Acid Phosphatase Isoforms Purified from Mature Soybean (Glyczne MAX) Seeds

• Published in: Journal of enzyme inhibition 2000, Vol.15 (4), p.403-410
• Main Authors: Ferreira, Carmen Verissima, Taga, Eulazio Mikio, Aoyama, Hiroshi
• Format: Article
• Language: English
• Subjects: Acid phosphatase; Acid Phosphatase - antagonists & inhibitors; Acid Phosphatase - isolation & purification; Acid Phosphatase - metabolism; Enzyme Inhibitors - pharmacology; Fluorides - pharmacology; Glycine max - enzymology; Inhibitors; Isoenzymes - antagonists & inhibitors; Isoenzymes - isolation & purification; Isoenzymes - metabolism; Kinetics; Molybdenum - pharmacology; Nitrophenols - metabolism; Organophosphorus Compounds - metabolism; Phosphates - pharmacology; Seeds - enzymology; Soybean seed; Vanadates - pharmacology
• ISSN: 1475-6366; 8755-5093; 1475-6374; 1029-2462
• DOI: 10.1080/14756360009040696

The four soybean seed acid phosphatase isoforms AP1, AP2, AP3A and AP3B were competitively inhibited by phosphate, vanadate, fluoride and molybdate, using p-nitrophenylphos-phate as substrate. The four isoforms were not significantly affected by compounds that can interact with SH residues or by pyridoxal phosphate. These results indicated that cysteine and lysine residues are not present in the active site of the four soybean seed acid phosphatase isoforms. The inhibition constant values for phosphate, vanadate, fluoride and molybdate at pH 5.0 were respectively: API (250, 12.8, 1.7, 0.05 μM), AP2 (800,10, 500, 0.025 μM), AP3A (250, 24.2,250, 0.032 μM), AP3B (2400, 36.9,750, 0.05 μM).