| Zinc-ion-dependent acid phosphatase exhibits magnesium-ion-dependent myo-inositol-1-phosphatase activity. | |
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MedLine Citation:
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PMID: 8799493 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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We have purified bovine brain Zn(2+)-dependent acid phosphatase (Zn(2+)-APase), which requires Zn2+ ions to hydrolyze the substrate p-nitrophenyl phosphate (pNPP) in an acidic environment. The substrate specificity and metal requirement of Zn(2+)-APase at a physiological pH was also studied. The enzyme exhibited hydrolytic activity on myo-inositol-1- and -2-monophosphates, 2'-adenosine monophosphate, 2'-guanosine monophosphate, and the alpha- and beta-glycerophosphates, glucose-1-phosphate, and fructose-6-phosphate in 50 mM Tris-HCl buffer (pH 7.4) in the presence of Mg2+ ions, but not on pNPP and phosphotyrosine. Zn2+, Mn2+ and Co2+ ions were less effective for activation. Among the above substrates, myo-inositol-1-phosphate was the most susceptible to hydrolysis by the enzyme in the presence of 3 mM Mg2+ ions. The enzyme exhibited an optimum pH at around 8 for myo-inositol-1-phosphate in the presence of 3 mM Mg2+ ions. The Mg(2+)-dependent myo-inositol-1-phosphatase activity of the enzyme was significantly inhibited by Li+ ions. The Zn(2+)-dependent p-nitrophenyl phosphatase activity and Mg(2+)-dependent myo-inositol-1-phosphatase activity of the purified enzyme fraction exhibited similar behavior on Sephadex G-100 and Mono Q colomns. These findings suggest that Zn(2+)-APase also exhibits Mg(2+)-dependent myo-inositol-1-phosphatase activity under physiological conditions. |
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Authors:
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S Fujimoto; I Okano; Y Tanaka; Y Sumida; J Tsuda; N Kawakami; S Shimohama |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Biological & pharmaceutical bulletin Volume: 19 ISSN: 0918-6158 ISO Abbreviation: Biol. Pharm. Bull. Publication Date: 1996 Jun |
Date Detail:
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Created Date: 1997-01-02 Completed Date: 1997-01-02 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 9311984 Medline TA: Biol Pharm Bull Country: JAPAN |
Other Details:
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Languages: eng Pagination: 882-5 Citation Subset: IM |
Affiliation:
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Department of Environmental Biochemistry, Kyoto Pharmaceutical University, Japan. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Acid Phosphatase
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metabolism* Animals Brain / enzymology* Cattle Hydrogen-Ion Concentration Hydrolysis Inositol Phosphates / chemistry Magnesium / metabolism Nitrophenols / chemistry Organophosphorus Compounds / chemistry Phosphoric Monoester Hydrolases / metabolism* Substrate Specificity Zinc / metabolism* |
| Chemical | |
Reg. No./Substance:
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0/Inositol Phosphates; 0/Nitrophenols; 0/Organophosphorus Compounds; 15421-51-9/inositol 1-phosphate; 330-13-2/nitrophenylphosphate; 7439-95-4/Magnesium; 7440-66-6/Zinc; EC 3.1.3.-/Phosphoric Monoester Hydrolases; EC 3.1.3.2/Acid Phosphatase; EC 3.1.3.25/myo-inositol-1 (or 4)-monophosphatase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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