Heterologous expression and characterization of a proxidomal ascorbate peroxidase from <Emphasis Type="Italic">Populus tomentosa</Emphasis> |
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Authors: | Hai Lu Rui-Li Han Xiang-Ning Jiang |
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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 |
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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. |
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Keywords: | Ascorbate peroxidases Enzyme activity Populus tomentosa Protein structure |
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