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Heterologous expression and characterization of a proxidomal ascorbate peroxidase from <Emphasis Type="Italic">Populus tomentosa</Emphasis>
Authors:Hai Lu  Rui-Li Han  Xiang-Ning Jiang
Institution:(1) College of Life Sciences and Biotechnology 162#, Beijing Forestry University, Beijing Haidian district Qinghua east road No.35, Beijing, 100083, P.R. China
Abstract:The present study reported for the first time, cloning, expression and characteristics of a Proxidomal APX gene (PpAPX) from Populus tomentosa. The PpAPX gene encodes a protein of 287 amino acid residues with a calculated molecular mass of 31.58 kDa. The over-expressed recombinant PpAPX protein showed high activity towards the substrates ascorbate aicd (ASA) and H2O2. At fixed ASA concentrations, the K m and V max values were 0.12 ± 0.01 mM and 23.4 ± 4.2 mmol/min mg for H2O2. And at fixed H2O2 concentrations, the K m and V max values were 0.53 ± 0.04 mM and 20.0 ± 2.3 mmol/min mg for ASA.
Keywords:Ascorbate peroxidases  Enzyme activity            Populus tomentosa            Protein structure
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