GO:0050221 prostaglandin E2 9-reductase activity: Mechanism, Genes and Research Methods
Research-grade guide for scientists and biopharma professionals
Key Takeaways
• GO:0050221 (prostaglandin E2 9-reductase activity) catalyzes the NADPH-dependent reduction of prostaglandin E2 to prostaglandin F2alpha, interconverting two bioactive prostanoids.
• The activity is widely distributed in reproductive tissues, including human decidua vera, fetal membranes, bovine placenta, ovine preovulatory follicles, and rabbit corpus luteum.
• Enzymes carrying this activity belong to the aldo-keto reductase and carbonyl reductase superfamilies, with the rabbit corpus luteum enzyme also exhibiting 20alpha-hydroxysteroid dehydrogenase activity.
• Nitric oxide inhibits prostaglandin E2 9-ketoreductase activity in human fetal membranes, linking redox signaling to prostanoid metabolism.
• Altered 9-ketoreductase activity has been associated with bovine retained placenta, suggesting a role in reproductive pathology.
• Studying GO:0050221 requires integrating enzyme assays, gene editing, and expression profiling across reproductive and inflammatory model systems.
Description
Prostaglandin E2 9-reductase activity (GO:0050221) is a molecular function that catalyzes the reversible conversion of prostaglandin E2 (PGE2) to prostaglandin F2alpha (PGF2alpha) using NADPH as a cofactor. This reaction is central to the regulation of prostanoid balance in reproductive tissues, where PGE2 and PGF2alpha often exert opposing biological effects. The enzyme activity has been detected in human decidua vera, human fetal membranes, bovine term placenta, ovine preovulatory follicles, and rabbit corpus luteum, indicating a conserved role in reproductive physiology. Because prostanoids are key mediators of inflammation, luteolysis, and parturition, understanding GO:0050221 is important for researchers studying reproductive biology and inflammatory disease. The activity is also of interest because it can be catalyzed by enzymes of the aldo-keto reductase and carbonyl reductase families, which have broad substrate specificities and are involved in drug metabolism and detoxification. This article summarizes the definition, mechanism, key genes, disease associations, and research methods relevant to GO:0050221, based on published literature.
prostaglandin E2 9-reductase activity At A Glance
| GO ID | GO:0050221 |
|---|---|
| GO term | prostaglandin E2 9-reductase activity |
| Ontology | molecular_function |
| Synonym | 9-ketoprostaglandin reductase activity; PGE2 9-ketoreductase activity; PGE2-9-OR; prostaglandin E2-9-oxoreductase activity |
| Major function | Catalyzes the NADPH-dependent reduction of prostaglandin E2 to prostaglandin F2alpha |
| Reaction direction | Reversible; NADP+ + PGF2alpha = NADPH + PGE2 |
| Cofactor | NADP+/NADPH |
| Subcellular location | Cytosol (typical for aldo-keto reductases and carbonyl reductases) |
| Tissue distribution | Human decidua vera, fetal membranes, bovine placenta, ovine follicles, rabbit corpus luteum |
| Enzyme families | Aldo-keto reductase superfamily; carbonyl reductase family |
What Is GO:0050221?
According to the Gene Ontology, GO:0050221 (prostaglandin E2 9-reductase activity) is defined as the catalysis of the reaction: (5Z,13E)-(15S)-9-alpha,11-alpha,15-trihydroxyprosta-5,13-dienoate (PGF2alpha) + NADP+ = (5Z,13E)-(15S)-11-alpha,15-dihydroxy-9-oxoprosta-5,13-dienoate (PGE2) + NADPH. In other words, it is an oxidoreductase activity that interconverts PGE2 and PGF2alpha, using NADP+/NADPH as the electron carrier. The term is also known as 9-ketoprostaglandin reductase, PGE2 9-ketoreductase, or PGE2-9-OR. This activity is distinct from other prostanoid-metabolizing enzymes because it specifically acts at the C9 keto group of the prostanoid cyclopentane ring.
Why Is prostaglandin E2 9-reductase activity Important in Cell Biology?
GO:0050221 is important because it controls the balance between PGE2 and PGF2alpha, two prostanoids with often opposing roles in reproduction, inflammation, and vascular tone. In reproductive tissues, this balance influences luteolysis, parturition, and placental function, and its dysregulation has been linked to conditions such as retained placenta in cattle. The activity is also relevant to pharmacology because enzymes with 9-ketoreductase activity, such as carbonyl reductase, can metabolize xenobiotics and contribute to drug resistance. Furthermore, nitric oxide-mediated inhibition of this activity in human fetal membranes suggests a link between redox signaling and prostanoid metabolism in pregnancy. Understanding GO:0050221 therefore has implications for reproductive biology, inflammatory disease, and drug metabolism research.
• Regulates the PGE2/PGF2alpha ratio, which is critical for luteolysis and parturition.
• Detected in human decidua vera, suggesting a role in early pregnancy maintenance.
• Nitric oxide inhibits the activity in human fetal membranes, linking inflammation to prostanoid imbalance.
• Altered activity is associated with bovine retained placenta, a reproductive disorder.
• Enzymes with this activity belong to the aldo-keto reductase superfamily, which is involved in steroid and drug metabolism.
• Carbonyl reductase exhibits prostaglandin 9-ketoreductase activity and paraquat resistance, connecting it to oxidative stress responses.
• A novel porcine carbonyl reductase activated by glutathione also shows 9-ketoreductase activity, indicating species diversity.
• The activity is present in ovine preovulatory follicles, suggesting a role in ovulation.
• Bovine term placenta expresses the activity, implicating it in fetal-maternal signaling.
• The reaction is reversible, allowing tissues to buffer prostanoid levels according to redox state.
Molecular Mechanism of prostaglandin E2 9-reductase activity
Substrate recognition and binding
In simple terms: The enzyme grabs PGE2 and holds it in place so it can be converted to PGF2alpha.
The enzyme binds prostaglandin E2 (PGE2) as a substrate, positioning the C9 keto group for reduction. This binding is stereospecific, as the reaction converts the 9-keto group to a 9-alpha-hydroxy group, yielding prostaglandin F2alpha (PGF2alpha). The enzyme also binds NADPH, which provides the hydride ion for the reduction. In the reverse direction, the enzyme binds PGF2alpha and NADP+ to oxidize the 9-alpha-hydroxy group back to a keto group. Substrate specificity studies indicate that the enzyme prefers prostaglandins with a 9-keto group, but some related enzymes can also act on other carbonyl compounds.
Catalytic mechanism and cofactor usage
In simple terms: NADPH donates a hydrogen to the substrate, turning PGE2 into PGF2alpha.
The catalytic mechanism involves hydride transfer from NADPH to the C9 carbon of PGE2, reducing the keto group to a hydroxyl. This is a typical oxidoreductase reaction catalyzed by aldo-keto reductases and carbonyl reductases, which use a conserved tyrosine residue as a general acid/base. The reaction is reversible, and the direction depends on the local NADP+/NADPH ratio. In the reverse reaction, NADP+ accepts a hydride from the 9-alpha-hydroxy group of PGF2alpha, regenerating PGE2 and NADPH. The enzyme from rabbit corpus luteum has been shown to be a member of the aldo-keto reductase superfamily and also exhibits 20alpha-hydroxysteroid dehydrogenase activity, indicating broad substrate tolerance.
Enzyme families and structural features
In simple terms: Different enzymes from the same family can perform this reaction, and they share a similar 3D shape.
Prostaglandin E2 9-reductase activity is not confined to a single protein; it can be catalyzed by multiple enzymes. The rabbit corpus luteum enzyme belongs to the aldo-keto reductase superfamily and features 20alpha-hydroxysteroid dehydrogenase activity. Human carbonyl reductase, a member of the short-chain dehydrogenase/reductase family, also demonstrates prostaglandin 9-ketoreductase activity. A novel porcine carbonyl reductase activated by glutathione has been characterized and shown to be related to carbonyl reductase 1 and 3alpha/beta-hydroxysteroid dehydrogenase. These enzymes share a common alpha/beta-barrel fold and a catalytic tetrad, but differ in tissue distribution and regulation.
Regulation by redox state and nitric oxide
In simple terms: The reaction can be turned up or down by the cell's redox balance and by signaling molecules like nitric oxide.
The activity of prostaglandin E2 9-reductase is sensitive to the cellular redox environment because it depends on NADPH availability. Nitric oxide (NO) has been shown to inhibit 9-ketoreductase activity in human fetal membranes, likely through modification of cysteine residues or depletion of NADPH. This inhibition may shift prostanoid production toward PGE2, which is relevant for inflammatory and pregnancy-related processes. Additionally, the enzyme from bovine placenta shows changes in activity associated with retained placenta, suggesting regulation by local factors. The glutathione-activated porcine carbonyl reductase indicates that cellular thiol status can also modulate activity.
Key Genes Involved in GO:0050221 prostaglandin E2 9-reductase activity
The following genes and proteins have been experimentally linked to prostaglandin E2 9-reductase activity or its regulation.
| Gene | Major Role | Research Relevance |
|---|---|---|
| CBR1 | Carbonyl reductase 1; exhibits prostaglandin 9-ketoreductase activity | Human enzyme with broad substrate specificity; linked to paraquat resistance |
| AKR1C1 | Aldo-keto reductase family member; may contribute to 9-ketoreductase activity | Involved in steroid and prostanoid metabolism |
| AKR1C2 | Aldo-keto reductase family member; 3alpha-hydroxysteroid dehydrogenase activity | Related to 9-ketoreductase in rabbit corpus luteum |
| AKR1C3 | Aldo-keto reductase; prostaglandin F synthase activity | Can interconvert PGE2 and PGF2alpha |
| AKR1B1 | Aldo-keto reductase; may reduce prostaglandins | Potential contributor to 9-ketoreductase activity |
| PTGS1 | Cyclooxygenase-1; upstream of PGE2 synthesis | Provides substrate for 9-ketoreductase |
| PTGS2 | Cyclooxygenase-2; inducible upstream of PGE2 synthesis | Links inflammation to 9-ketoreductase substrate supply |
| PTGES | Prostaglandin E synthase; produces PGE2 | Substrate provider for 9-ketoreductase |
| PTGFR | PGF2alpha receptor; mediates PGF2alpha effects | Downstream target of 9-ketoreductase product |
| PTGER1-4 | PGE2 receptors; mediate PGE2 effects | Opposing effects to PGF2alpha |
| NOS2 | Inducible nitric oxide synthase; produces NO | NO inhibits 9-ketoreductase in fetal membranes |
| NOS3 | Endothelial nitric oxide synthase; produces NO | May regulate 9-ketoreductase in reproductive tissues |
| CBR3 | Carbonyl reductase 3; related to CBR1 | Potential 9-ketoreductase activity |
| AKR1A1 | Aldo-keto reductase; may act on prostaglandins | Candidate for 9-ketoreductase activity |
| HSD11B1 | 11beta-hydroxysteroid dehydrogenase; related to AKR superfamily | May share substrate overlap |
| GSTA1 | Glutathione S-transferase; may activate carbonyl reductase | Glutathione-activated 9-ketoreductase in pig |
| NQO1 | NAD(P)H quinone dehydrogenase; redox partner | May influence NADPH availability |
How Is prostaglandin E2 9-reductase activity Regulated?
Prostaglandin E2 9-reductase activity is regulated at multiple levels. The reaction depends on the availability of NADPH, so enzymes that generate NADPH, such as glucose-6-phosphate dehydrogenase and malic enzyme, can indirectly influence activity. Nitric oxide inhibits the activity in human fetal membranes, likely through S-nitrosylation or depletion of NADPH. In bovine placenta, activity changes in retained versus non-retained placenta suggest regulation by local hormonal or inflammatory signals. The glutathione-activated porcine carbonyl reductase indicates that cellular thiol status can modulate activity, possibly through glutathionylation. Additionally, expression levels of carbonyl reductase and aldo-keto reductase genes can be regulated by transcription factors such as Nrf2, which controls antioxidant responses.
prostaglandin E2 9-reductase activity and Human Disease
| Gene | Disease / Biology | Potential Experimental Model |
|---|---|---|
| CBR1 | Cancer drug resistance; oxidative stress | CBR1 knockout cancer cell lines; overexpression models |
| AKR1C3 | Prostate cancer; prostaglandin metabolism | Point mutation of catalytic residues; knock-in of cancer variants |
| NOS2 | Inflammation; preterm labor | NOS2 knockout mice; NO donor treatment in fetal membrane cells |
| PTGS2 | Inflammation; cancer | PTGS2 knockout; overexpression in epithelial cells |
| PTGFR | Reproductive disorders; luteolysis | PTGFR knockout mice; knock-in of human variants |
Reproductive disorders and retained placenta
Prostaglandin E2 9-reductase activity has been implicated in bovine retained placenta, a condition where the fetal membranes are not expelled after parturition. Kankofer et al. (2002) found that 9-keto reductase activity was altered in bovine retained placenta compared to non-retained placenta, suggesting a role in the pathogenesis of this disorder. The enzyme may influence the PGE2/PGF2alpha ratio, which is critical for placental detachment and uterine involution. In humans, 9-ketoreductase activity in decidua vera and fetal membranes may be relevant to preterm labor and membrane rupture.
Inflammation and nitric oxide signaling
Nitric oxide (NO) inhibits prostaglandin E2 9-ketoreductase activity in human fetal membranes, linking inflammatory signaling to prostanoid metabolism. This inhibition may shift the balance toward PGE2, which promotes vasodilation and inflammation, and away from PGF2alpha, which promotes uterine contraction. In conditions characterized by high NO production, such as infection or inflammation, this shift could contribute to pathological outcomes in pregnancy. The enzyme carbonyl reductase, which exhibits 9-ketoreductase activity, is also involved in detoxification of reactive carbonyls, so its inhibition may exacerbate oxidative stress.
Cancer and drug metabolism
Carbonyl reductase 1 (CBR1), which exhibits prostaglandin 9-ketoreductase activity, is known to metabolize anthracycline anticancer drugs and contribute to drug resistance. Overexpression of CBR1 in cancer cells can reduce the efficacy of doxorubicin and other substrates. Additionally, prostaglandins are known to influence tumor progression, and the PGE2/PGF2alpha balance may affect angiogenesis and immune evasion. Therefore, enzymes with 9-ketoreductase activity could be potential targets for modulating chemotherapy response and tumor microenvironment.
From prostaglandin E2 9-reductase activity-Related Genes to Experimental Models
| Research Question | Suitable Model |
|---|---|
| Does CBR1 mediate 9-ketoreductase activity in human cells? | CBR1 knockout HEK293 or HeLa cells; rescue with wild-type or catalytic mutant |
| How does NO regulate 9-ketoreductase in fetal membranes? | Human fetal membrane explants treated with NO donors; NOS2 knockout mice |
| What is the role of AKR1C3 in prostaglandin interconversion? | AKR1C3 point mutation (Y55F) knock-in cell lines; enzyme assays |
| Does glutathione activate porcine carbonyl reductase? | Overexpression of porcine CBR1 in E. coli; site-directed mutagenesis of cysteine residues |
| Is 9-ketoreductase activity altered in retained placenta? | Bovine placental tissue from retained vs. non-retained cases; primary trophoblast cultures |
| Can 9-ketoreductase activity be targeted to modulate drug resistance? | CBR1 overexpression in cancer cell lines; CRISPR knockout; drug sensitivity assays |
How to Study the prostaglandin E2 9-reductase activity Process
| Method | What It Measures | Typical Application |
|---|---|---|
| NADPH oxidation assay | Enzyme activity via absorbance at 340 nm | Kinetic characterization of purified enzyme |
| Radioactive TLC assay | Conversion of 3H-PGE2 to 3H-PGF2alpha | Tissue homogenate activity |
| LC-MS/MS | Quantification of prostanoids | Prostanoid profiling in cells and tissues |
| qRT-PCR | mRNA expression of candidate genes | Gene expression analysis in disease models |
| Western blot | Protein expression and modification | Validation of knockout or overexpression |
| CRISPR knockout | Loss-of-function of candidate genes | Identifying responsible enzymes |
| Site-directed mutagenesis | Effect of point mutations on activity | Mechanistic studies of catalytic residues |
| Immunohistochemistry | Tissue localization of enzymes | Reproductive tissue studies |
Enzyme activity assays
The most direct method to measure prostaglandin E2 9-reductase activity is a spectrophotometric assay monitoring NADPH oxidation at 340 nm or NADP+ reduction. Radioactive assays using 3H-PGE2 and thin-layer chromatography can separate PGE2 from PGF2alpha. High-performance liquid chromatography (HPLC) coupled with mass spectrometry can quantify prostanoids with high sensitivity and specificity. These assays are typically performed on tissue homogenates, cell lysates, or purified recombinant enzymes.
Gene expression analysis
Quantitative RT-PCR and RNA-seq can measure mRNA levels of candidate genes such as CBR1, AKR1C1, AKR1C2, and AKR1C3 in tissues or cells. Western blotting and immunohistochemistry can detect protein expression and localization. These methods help correlate enzyme activity with gene expression in different physiological and pathological states, such as retained placenta or fetal membrane inflammation.
CRISPR-based functional studies
CRISPR-Cas9 knockout of candidate genes (e.g., CBR1, AKR1C3) followed by enzyme activity assays can identify which enzymes are responsible for 9-ketoreductase activity in a given cell type. Point mutations of catalytic residues (e.g., tyrosine to phenylalanine) can abolish activity and confirm mechanism. Knock-in of disease-associated variants can model altered activity. Overexpression of wild-type or mutant enzymes can test gain-of-function effects.
Prostanoid profiling and metabolomics
Liquid chromatography-tandem mass spectrometry (LC-MS/MS) can quantify a panel of prostanoids, including PGE2, PGF2alpha, and their metabolites, in biological samples. This approach provides a comprehensive view of how 9-ketoreductase activity affects the broader prostanoid network. Stable isotope-labeled internal standards improve quantification. Metabolomic profiling can also reveal changes in related pathways, such as steroid hormone metabolism, when the enzyme is knocked out or overexpressed.
How CRISPR Can Be Used to Study GO:0050221 prostaglandin E2 9-reductase activity
Knockout
CRISPR-Cas9 knockout of candidate genes such as CBR1 or AKR1C3 can be used to determine which enzymes contribute to prostaglandin E2 9-reductase activity in a specific cell type. For example, knocking out CBR1 in HEK293 cells followed by enzyme assays can confirm its role in PGE2 reduction. Knockout models can also be used to study the consequences of loss of activity on prostanoid profiles and cellular phenotypes, such as drug sensitivity or inflammatory responses.
Point Mutation
Point mutations of catalytic residues, such as the conserved tyrosine in aldo-keto reductases, can abolish 9-ketoreductase activity. CRISPR-mediated knock-in of such mutations allows researchers to study the enzyme's mechanism in a physiological context. For example, mutating Y55 in AKR1C3 to phenylalanine can eliminate activity and reveal its contribution to prostanoid metabolism. Point mutations can also model naturally occurring variants that affect enzyme function.
Knock-in
Knock-in of disease-associated variants or tagged versions of the enzyme can be achieved using CRISPR-Cas9 and homology-directed repair. For instance, knocking in a FLAG-tagged CBR1 allows for immunoprecipitation and localization studies. Knock-in of human orthologs into mouse models can humanize the system for drug testing. This approach is valuable for studying species-specific differences in 9-ketoreductase activity, such as the glutathione-activated porcine enzyme.
Overexpression
CRISPR activation (CRISPRa) or lentiviral overexpression can be used to increase expression of candidate genes like CBR1 or AKR1C3. Overexpression models can test whether increased 9-ketoreductase activity alters prostanoid balance and cellular phenotypes, such as proliferation or drug resistance. These models are also useful for producing recombinant enzyme for biochemical studies. Overexpression in cancer cell lines can mimic the elevated CBR1 levels seen in some tumors.
How EDITGENE Supports prostaglandin E2 9-reductase activity Research
Researchers studying prostaglandin E2 9-reductase activity-related genes often need to determine whether a candidate gene is causally involved in prostanoid metabolism, reproductive physiology, or disease. EDITGENE provides a comprehensive suite of CRISPR-based services to enable such studies, from gene knockout to precise point mutations and overexpression.
Contact EDITGENE today to design your custom CRISPR model for prostaglandin E2 9-reductase activity research.
Related Products
| Product name | Cat.No. | Species | Gene ID | |
|---|---|---|---|---|
| CBR1 Knockout HEK293 Cell Line | EDJ-KQ4203 | Human | 873 | Details Get a Quote |
| CBR1 Knockout A-549 Cell Line | EDJ-KQ26672 | Human | 873 | Details Get a Quote |
| CBR1 Knockout HeLa Cell Line | EDJ-KQ26673 | Human | 873 | Details Get a Quote |
| CBR1 Knockout HCT 116 Cell Line | EDJ-KQ69763 | Human | 873 | Details Get a Quote |
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Frequently Asked Questions About prostaglandin E2 9-reductase activity
What is prostaglandin E2 9-reductase activity?
It is a molecular function (GO:0050221) that catalyzes the NADPH-dependent conversion of prostaglandin E2 to prostaglandin F2alpha, and the reverse reaction.
What genes are involved in prostaglandin E2 9-reductase activity?
Genes such as CBR1, AKR1C1, AKR1C2, AKR1C3, and other aldo-keto reductases and carbonyl reductases have been associated with this activity.
Which tissues express prostaglandin E2 9-reductase activity?
It has been detected in human decidua vera, fetal membranes, bovine placenta, ovine preovulatory follicles, and rabbit corpus luteum.
How is prostaglandin E2 9-reductase activity regulated?
It is regulated by NADPH availability, nitric oxide, glutathione, and possibly hormonal signals; NO inhibits the activity in fetal membranes.
What diseases are linked to prostaglandin E2 9-reductase activity?
Altered activity has been associated with bovine retained placenta, and the enzyme CBR1 is linked to cancer drug resistance.
What is the reaction catalyzed by prostaglandin E2 9-reductase?
It reduces the C9 keto group of PGE2 to a hydroxyl, forming PGF2alpha, using NADPH as a cofactor.
How can I measure prostaglandin E2 9-reductase activity in the lab?
Common methods include NADPH oxidation assays, radioactive TLC, and LC-MS/MS for prostanoid quantification.
What is the role of nitric oxide in prostaglandin E2 9-reductase activity?
Nitric oxide inhibits the activity in human fetal membranes, potentially shifting prostanoid balance toward PGE2.
Can CRISPR be used to study prostaglandin E2 9-reductase activity?
Yes, CRISPR knockout, point mutation, knock-in, and overexpression models can identify responsible enzymes and study their function.
Which enzyme families catalyze prostaglandin E2 9-reductase activity?
The aldo-keto reductase superfamily and carbonyl reductase family, including CBR1 and AKR1C3, are known to catalyze this activity.
Conclusion
Prostaglandin E2 9-reductase activity (GO:0050221) is a key enzymatic function that regulates the balance between PGE2 and PGF2alpha, with important roles in reproductive physiology, inflammation, and drug metabolism. The activity is catalyzed by multiple enzymes from the aldo-keto reductase and carbonyl reductase families, and is regulated by redox state and nitric oxide. Dysregulation has been linked to reproductive disorders and cancer drug resistance. Continued research using CRISPR-based models and advanced prostanoid profiling will further elucidate its mechanistic and pathological roles.
References
- 1. Niesert S et al.. 1986. Prostaglandin E2 9-ketoreductase activity in human decidua vera tissue.. Am J Obstet Gynecol 155(6):1348-52 PMID: 3466547
- 2. Kelner MJ et al.. 1997. Heterologous expression of carbonyl reductase: demonstration of prostaglandin 9-ketoreductase activity and paraquat resistance.. Life Sci 61(23):2317-22 PMID: 9408054
- 3. Kankofer M et al.. 1999. Prostaglandin E2 9-keto reductase from bovine term placenta.. Prostaglandins Leukot Essent Fatty Acids 61(1):29-32 PMID: 10477039
- 4. Farina MG et al.. 2006. Nitric oxide (NO) inhibits prostaglandin E2 9-ketoreductase (9-KPR) activity in human fetal membranes.. Prostaglandins Other Lipid Mediat 79(3-4):260-70 PMID: 16647639
- 5. Murdoch WJ et al.. 1988. Prostaglandin E2-9-ketoreductase activity of preovulatory ovine follicles.. J Anim Sci 66(11):2924-9 PMID: 3225245
- 6. Wintergalen N et al.. 1995. Prostaglandin-E2 9-reductase from corpus luteum of pseudopregnant rabbit is a member of the aldo-keto reductase superfamily featuring 20 alpha-hydroxysteroid dehydrogenase activity.. Eur J Biochem 234(1):264-70 PMID: 8529651
- 7. Kankofer M et al.. 2002. Prostaglandin E(2) 9-keto reductase activity in bovine retained and not retained placenta.. Prostaglandins Leukot Essent Fatty Acids 66(4):413-7 PMID: 12054911
- 8. Endo S et al.. 2023. Characterization of a novel porcine carbonyl reductase activated by glutathione: Relationship to carbonyl reductase 1, 3α/β-hydroxysteroid dehydrogenase and prostaglandin 9-ketoreductase.. Chem Biol Interact 381:110572 PMID: 37247810
