An alkaline phosphatase from Thermus sp strain Rt41A |
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| Institution: | 1. Tecnologico de Monterrey, Campus Monterrey, Ave. Eugenio Garza Sada 2501, CP 64849, Monterrey, NL, Mexico;2. BioMEMS and Biointeractive Systems Research Group, Electrical and Computer Engineering Department, Tecnológico de Monterrey, Av. Eugenio Garza Sada 2501 Sur, CP 64849, Monterrey, NL, Mexico;3. ICRA, Catalan Institute for Water Research, Parc Científic i Tecnològic de la Universitat de Girona, Edifici Jaume Casademont, 15, 17003 Girona, Spain |
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| Abstract: | - 1.1. A thermostable orthophosphoric monoester phosphohydrolase (EC 3.1.3.1) from Thermus sp strain Rt41A has been purified 400-fold to give a specific activity of 25 U/mg at 60°C in IM diethanolamine (pH 11.1).
- 2.2. The enzyme has a Mr of 160,000 and is trimeric.
- 3.3. The half-life of the enzyme is 5 min at 85°C.
- 4.4. The enzyme has a wide specificity for a number of phosphate monoesters.
- 5.5. The Hm of the enzyme is pH dependent, so the pH optimum of the enzyme is affected by the substrate concentration.
- 6.6. The enzyme is inhibited 50% by 20 mM Ca2+ or Mg2+.
- 7.7. The Ki for phosphate, EDTA-di sodium salt and arsenate (in 1 M diethanolamine, pH 11.1) is approx 1.2, 1.6 and 4mM respectively.
- 8.8. Urea (200 mM) is not inhibitory.
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