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  • Title: A Newly Identified Glutaminase-Free ʟ-Asparaginase (ʟ-ASPG86) from the Marine Bacterium Mesoflavibacter zeaxanthinifaciens.
    Author: Lee SJ, Lee Y, Park GH, Umasuthan N, Heo SJ, De Zoysa M, Jung WK, Lee DW, Kim H, Kang DH, Oh C.
    Journal: J Microbiol Biotechnol; 2016 Jun 28; 26(6):1115-23. PubMed ID: 26975773.
    Abstract:
    ʟ-Asparaginase (E.C. 3.5.1.1) is an enzyme involved in asparagine hydrolysis and has the potential to effect leukemic cells and various other cancer cells. We identified the Lasparaginase gene (ʟ-ASPG86) in the genus Mesoflavibacter, which consists of a 1,035 bp open reading frame encoding 344 amino acids. Following phylogenetic analysis, the deduced amino acid sequence of ʟ-ASPG86 (ʟ-ASPG86) was grouped as a type I asparaginase with respective homologs in Escherichia coli and Yersinia pseudotuberculosis. The ʟ-ASPG86 gene was cloned into the pET-16b vector to express the respective protein in E. coli BL21 (DE3) cells. Recombinant ʟ-asparaginase (r-ʟ-ASPG86) showed optimum conditions at 37-40oC, pH 9. Moreover, r-ʟ-ASPG86 did not exhibit glutaminase activity. In the metal ions test, its enzymatic activity was highly improved upon addition of 5 mM manganese (3.97-fold) and magnesium (3.35-fold) compared with the untreated control. The specific activity of r-LASPG86 was 687.1 units/mg under optimum conditions (37°C, pH 9, and 5 mM MnSO4).
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