@article{Schieber1992Purif-6550,
  year={1992},
  doi={10.1111/j.1432-1033.1992.tb16952.x},
  title={Purification and properties of prostaglandin 9-ketoreductase from pig and human kidney : identity with human carbonyl reductase},
  number={2},
  volume={206},
  journal={European Journal of Biochemistry},
  pages={491--502},
  author={Schieber, Ardrea and Frank, Rainer W. and Ghisla, Sandro}
}

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    <dcterms:title>Purification and properties of prostaglandin 9-ketoreductase from pig and human kidney : identity with human carbonyl reductase</dcterms:title>
    <dc:contributor>Schieber, Ardrea</dc:contributor>
    <dc:creator>Frank, Rainer W.</dc:creator>
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    <dcterms:abstract xml:lang="eng">Prostaglandin 9-ketoreductase (PG-9-KR) was purified from pig kidney to homogeneity, as judged by SDS/PAGE using an improved procedure. The enzyme is pro-S stereoselective with regard to hydrogen transfer from NADPH with prostaglandin E2 as substrate and reduces its 9-keto group with approximately 90% stereoselectivity to form prostaglandin F2α. Approximately 8% of the prostaglandin F formed has the β-configuration. In addition to catalyzing the interconversion of prostaglandin E2 to F2α, PG-9-KR also oxidizes prostaglandin E2, F2α and D2 to their corresponding, biologically inactive, 15-keto metabolites. Incubation of PG-9-KR with prostaglandin F2α and NAD+ leads to the preferential formation of 15-keto prostaglandin F2α rather than prostaglandin E2. This suggests that the prostaglandin E2/prostaglandin F2α ratio is not determined by the NADP+/NADPH redox couple. The enzyme also reduces various other carbonyl compounds (e.g. 9,10-phen-anthrenequinone) with high efficiency. The catalytic properties measured for PG-9-KR suggest that its in vivo function is unlikely to be to catalyze formation of prostaglandin F2α. The monomeric enzyme has a molecular mass of 32 kDa and exists as four isoforms, as judged by isoelectric focusing. PG-9-KR contains 1.9 mol Zn2+/mol enzyme and no other cofactors. Human kidney PG-9-KR was also purified to homogeneity. The human enzyme has a molecular mass of 34 kDa and also exists as four isoforms. Polyclonal antibodies raised against pig kidney PG-9-KR cross-react with human kidney PG-9-KR and also with human brain carbonyl reductase, as demonstrated by Western blot analysis. Sequence data of tryptic peptides from pig kidney PG-9-KR show &gt;90% identity with human placenta carbonyl reductase. From comparison of several properties (catalytical, structural and immunological properties), it is concluded that PG-9-KR and carbonyl reductase are identical enzymes.</dcterms:abstract>
    <dcterms:bibliographicCitation>First publ. in: European Journal of Biochemistry 206 (1992), 2, pp. 491-502</dcterms:bibliographicCitation>
    <dc:contributor>Ghisla, Sandro</dc:contributor>
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    <dc:contributor>Frank, Rainer W.</dc:contributor>
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