An isocitrate lyase of higher plants: analysis and comparison of some molecular properties |
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| Authors: | G Pinzauti E Giachetti G Camici G Manao G Cappugi P Vanni |
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| Institution: | 1. Institute of Research and Development, Duy Tan University, Da Nang 550000, Viet Nam;2. Faculty of Environmental and Chemical Engineering, Duy Tan University, Da Nang 550000, Viet Nam;3. Key Laboratory of Advanced Materials for Energy and Environmental Applications, Lac Hong University, Bien Hoa 810000, Viet Nam;4. Faculty of Environmental Science, Sai Gon University, Ho Chi Minh City 748355, Viet Nam;5. Faculty of Pharmacy, Ton Duc Thang University, Ho Chi Minh City 700000, Viet Nam;1. Laboratory of Modern Biotechnology, School of Forestry and Landscape Architecture, Anhui Agricultural University, Hefei 230036, China;2. National Engineering Laboratory of Crop Stress Resistance Breeding, College of Life Sciences, Anhui Agricultural University, Hefei 230036, China |
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| Abstract: | A new purification procedure for isocitrate lyase from Pinus pinea is reported. The final preparation shows charge homogeneity and a purity degree higher than 95%. It is possible to remove catalase completely by exploiting the high hydrophobicity of isocitrate lyase. The enzyme has a Mr of 264,000 and is likely composed of four subunits, each with a Mr of 66,000. The binding of radioactively labeled oxalate revealed four catalytic sites per oligomer. These data suggest that isocitrate lyase subunits are similar, if not identical. The Michaelis constant for isocitrate is equal to 33 microM; molecular activity is about 2670 mol X min-1 X mol of enzyme-1. The amino acid composition of the enzyme was also determined. Isocitrate lyase appears resistant to proteolysis by carboxypeptidase A. Hydrazinolysis, Edman degradation, and dansyl chloride treatment indicate that both carboxy and amino terminals are probably inaccessible or blocked. |
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