國家衛生研究院 NHRI:Item 3990099045/5620
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    Title: An arsenate reductase homologue possessing phosphatase activity from sweet potato (Ipomoea batatas L. Lam): Kinetic studies and characterization
    Authors: Chan, YH;Lin, CY;Pai, SH;Huang, JK;Lin, CT
    Contributors: National Institute of Cancer Research
    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)(5)R) 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 QTOF. The IbArsR lacks arsenate reductase activity but possesses phosphatase activity. The Michaelis constant (K-M) value for p-nitrophenyl phosphate (pNPP) was 11.11 mM. The phosphatase activity was inhibited by 0.5 mM sodium arsenate [As(V)]. The proteins half-life of deactivation at 25 degrees C was 6.1 min, and its inactivation rate constant K-d was 1.1 x 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.
    Date: 2011-04
    Relation: Journal of Agricultural and Food Chemistry. 2011 Apr;59(7):3087-3091.
    Link to: http://dx.doi.org/10.1021/jf1040542
    JIF/Ranking 2023: http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=NHRI&SrcApp=NHRI_IR&KeyISSN=0021-8561&DestApp=IC2JCR
    Cited Times(WOS): https://www.webofscience.com/wos/woscc/full-record/WOS:000289050400046
    Cited Times(Scopus): http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=79953860679
    Appears in Collections:[Others] Periodical Articles

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