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Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/27110

Title: An Arsenate Reductase Homologue Possessing Phosphatase Activity from Sweet Potato (Ipomoea batatas [L.] Lam): Kinetic Studies and Characterization
Authors: Ya-Hui Cha;Chao-Yi Lin;Shou-Hsiung Pai;Jenq-Kuen Huang;Chi-Tsai Lin
Contributors: NTOU:Institute of Bioscience and Biotechnology
國立臺灣海洋大學:生物科技研究所
Keywords: sweet potato (Ipomoea batatas [L.] Lam);three-dimensional homology structure (3-D homology structure);expression;arsenate reductase;arsenate [As(V)];phosphatase;p-nitrophenyl phosphate (pNPP)
Date: 2011
Issue Date: 2011-10-21T02:22:46Z
Publisher: Journal of Agricultural and Food Chemistry
Abstract: Abstract:A cDNA encoding a putative arsenate reductase homologue (IbArsR) was cloned from sweet potato (Ib). The deduced protein showed a high level of sequence homology (16−66%) with ArsRs from other organisms. A 3-D homology structure was created based on AtArsR (PDB code 1T3K) from Arabidopsis thaliana. The putative active site of protein tyrosine phosphatase (HC(X)5R) is conserved in all reported ArsRs. IbArsR was overexpressed and purified. The monomeric nature of the enzyme was confirmed by 15% SDS-PAGE and molecular mass determination of the native enzyme via ESI Q-TOF. The IbArsR lacks arsenate reductase activity but possesses phosphatase activity. The Michaelis constant (KM) value for p-nitrophenyl phosphate (pNPP) was 11.11 mM. The phosphatase activity was inhibited by 0.5 mM sodium arsenate [As(V)]. The protein’s half-life of deactivation at 25 °C was 6.1 min, and its inactivation rate constant Kd was 1.1 × 10−1 min−1. The enzyme was active in a broad pH range from 4.0 to 11.0 with optimum activity at pH 10.0. Phosphatase would remove phosphate group from nucleic acid or dephosphorylation of other enzymes as regulation signaling.
Relation: 59(7), pp.3087–3091
URI: http://ntour.ntou.edu.tw/handle/987654321/27110
Appears in Collections:[生命科學暨生物科技學系] 期刊論文

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