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  • Title: Site-directed mutagenesis of the conserved tyrosine 151 of human placental NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase yields a catalytically inactive enzyme.
    Author: Ensor CM, Tai HH.
    Journal: Biochem Biophys Res Commun; 1991 Apr 30; 176(2):840-5. PubMed ID: 2025296.
    Abstract:
    NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase (15-PGDH) is a key enzyme involved in the biological inactivation of the prostaglandins. The cDNA for human placental 15-PGDH has been expressed in Escherichia coli. Site-directed mutagenesis was used to convert a highly conserved tyrosine at position 151 in 15-PGDH to an alanine. The DNA coding for this alanine mutant 15-PGDH was expressed in E. coli. Western blot analysis indicated that this mutant protein was expressed in amounts comparable to the wild type enzyme in bacteria, however no 15-PGDH activity could be detected. This result indicates that tyrosine 151 in 15-PGDH is essential for activity.
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