15-Ketoprostaglandin reductase from human placenta: Purification, kinetics, and inhibitor binding☆
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Human prostaglandin reductase 1 (PGR1): Substrate specificity, inhibitor analysis and site-directed mutagenesis
2015, Chemico-Biological InteractionsCitation Excerpt :Finally, the reduction of the double bond is implicated in the activation of some pro-drugs with an antitumor chemotherapeutic role (i.e. CS-670 [17] and hydroxymethylacylfulvene [18]). Kinetic studies on PGR1 had been reported in various mammals (pig [12], guinea pig [13] and rat [14,17,19]), but only preliminary characterization studies were performed with the human enzyme [2,11]. Here we report a complete kinetic characterization of human PGR1 with LTB4 and different α,β-unsaturated aldehydes and ketones, including 15-keto-PGs. In addition, inhibition analysis is presented using non-steroidal anti-inflammatory drugs (NSAIDs) as potential inhibitors.
Multiplicity of rat liver 15-ketoprostaglandin Δ<sup>13</sup>-reductases
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This work was supported by funds from U.S. Public Health Service Grants HD-07045, HD-07110 (CRP core support), and PHS 5-TO5-GM 01939 (MSTP support for C.W.) and by a grant from the Louis Block Foundation.