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  • Title: The Ala-161-->Thr substitution in Escherichia coli alkaline phosphatase does not result in loss of enzymatic activity although the homologous mutation in humans causes hypophosphatasia.
    Author: Chaidaroglou A, Kantrowitz ER.
    Journal: Biochem Biophys Res Commun; 1993 Jun 30; 193(3):1104-9. PubMed ID: 8323535.
    Abstract:
    The correlation between sequence homology and catalytic importance of a specific amino acid in the E. coli and Liver/Kidney/Bone (L/K/B) human alkaline phosphatase was investigated. For this reason Ala-161 in the E. coli enzyme was substituted with a threonine residue via site-specific mutagenesis. The homologous amino acid in the L/K/B alkaline phosphatase sequence has been shown to cause inactivation of the enzyme. In E. coli alkaline phosphatase the Ala-161-->Thr substitution results in a mutant enzyme with virtually unchanged catalytic properties when compared to the wild-type enzyme. Our results show that Ala-161 in the E. coli alkaline phosphatase does not have an important catalytic role. The results suggest that the three-dimensional topology of the L/K/B alkaline phosphatase may be different from that observed for the enzyme from E. coli.
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