Linked Life Data

1597188

Source:http://linkedlifedata.com/resource/pubmed/id/1597188

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1992-7-7
pubmed:abstractText
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 F2 alpha. Approximately 8% of the prostaglandin F formed has the beta-configuration. In addition to catalyzing the interconversion of prostaglandin E2 to F2 alpha, PG-9-KR also oxidizes prostaglandin E2, F2 alpha and D2 to their corresponding, biologically inactive, 15-keto metabolites. Incubation of PG-9-KR with prostaglandin F2 alpha and NAD+ leads to the preferential formation of 15-keto prostaglandin F2 alpha rather than prostaglandin E2. This suggests that the prostaglandin E2/prostaglandin F2 alpha ratio is not determined by the NADP+/NADPH redox couple. The enzyme also reduces various other carbonyl compounds (e.g. 9,10-phenanthrenequinone) 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 F2 alpha. 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 greater than 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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
206
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
491-502
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed-meshheading:1597188-Alcohol Oxidoreductases, pubmed-meshheading:1597188-Amino Acid Sequence, pubmed-meshheading:1597188-Amino Acids, pubmed-meshheading:1597188-Animals, pubmed-meshheading:1597188-Blotting, Western, pubmed-meshheading:1597188-Catalysis, pubmed-meshheading:1597188-Chromatography, Gel, pubmed-meshheading:1597188-Chromatography, High Pressure Liquid, pubmed-meshheading:1597188-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:1597188-Humans, pubmed-meshheading:1597188-Hydroxyprostaglandin Dehydrogenases, pubmed-meshheading:1597188-Isoelectric Focusing, pubmed-meshheading:1597188-Kidney, pubmed-meshheading:1597188-Molecular Sequence Data, pubmed-meshheading:1597188-Prostaglandins, pubmed-meshheading:1597188-Sequence Homology, Nucleic Acid, pubmed-meshheading:1597188-Spectrophotometry, Atomic, pubmed-meshheading:1597188-Substrate Specificity, pubmed-meshheading:1597188-Swine
pubmed:year
1992
pubmed:articleTitle
Purification and properties of prostaglandin 9-ketoreductase from pig and human kidney. Identity with human carbonyl reductase.
pubmed:affiliation
University of Konstanz, Faculty of Biology, Federal Republic of Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't