Site-directed mutagenesis of the conserved tyrosine 151 of human placental NAD+-dependent 15-hydroxyprostaglandin dehydrogenase yields a catalytically inactive enzyme

作者: Charles Mark Ensor , Hsin-Hsiung Tai

DOI: 10.1016/S0006-291X(05)80262-1

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摘要: NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase (15-PGDH) is a key enzyme involved in the biological inactivation of prostaglandins. The cDNA for human placental 15-PGDH has been expressed Escherichia coli. Site-directed mutagenesis was used to convert highly conserved tyrosine at position 151 an alanine. DNA coding this alanine mutant E. Western blot analysis indicated that protein amounts comparable wild type bacteria, however no activity could be detected. This result indicates essential activity.

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