Stereospecific reduction of 5β-reduced steroids by human ketosteroid reductases of the AKR (aldo–keto reductase) superfamily: role of AKR1C1-AKR1C4 in the metabolism of testosterone and progesterone via the 5β-reductase pathway
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Active sex hormones such as testosterone and progesterone are metabolized to tetrahydrosteroids in the liver to terminate hormone action. One main metabolic pathway, the 5β-pathway, involves 5β-steroid reductase (AKR1D1, where AKR refers to the aldo-keto reductase superfamily), which catalyses the reduction of the 4-ene structure, and ketosteroid reductases (AKR1C1-AKR1C4), which catalyse the subsequent reduction of the 3-oxo group. The activities of the four human AKR1C enzymes on 5β-dihydrotestosterone, 5β-pregnane-3,20-dione and 20α-hydroxy-5β-pregnan-3-one, the intermediate 5β-dihydrosteroids on the 5β-pathway of testosterone and progesterone metabolism, were investigated. Product characterization by liquid chromatography-MS revealed that the reduction of the 3-oxo group of the three steroids predominantly favoured the formation of the corresponding 3α-hydroxy steroids. The stereochemistry was explained by molecular docking. Kinetic properties of the enzymes identified AKR1C4 as the major enzyme responsible for the hepatic formation of 5β-tetrahydrosteroid of testosterone, but indicated differential routes and roles of human AKR1C for the hepatic formation of 5β-tetrahydrosteroids of progesterone. Comparison of the kinetics of the AKR1C1-AKR1C4-catalysed reactions with those of AKR1D1 suggested that the three intermediate 5β-dihydrosteroids derived from testosterone and progesterone are unlikely to accumulate in liver, and that the identities and levels of 5β-reduced metabolites formed in peripheral tissues will be governed by the local expression of AKR1D1 and AKR1C1-AKR1C3.
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Further reduction of 5β-DHT to etiocholanone is catalyzed by AKR1C enzymes, with AKR1C4 most efficient, followed by AKR1C2, AKR1C3 and AKR1C1.
“Further reduction of 5β-DHT to etiocholanone is catalyzed by the AKR1C enzymes, where AKR1C4 is the most efficient enzyme, followed by AKR1C2, AKR1C3 and AKR1C1”
From Role of aldo-keto reductase family 1 (AKR1) enzymes in human steroid metabolism (2014) · cites this paper as [36]
5β-reduced steroids are predominantly converted to the 3α-hydroxy epimer because the 5β-reduced bent conformation sterically does not allow binding in the AKR1C active site for 3β-reduction.
“5β-reduced steroids are predominantly converted to the 3α-hydroxy epimer as the 5β-reduced bent confirmation of the A/B-ring sterically does not allow binding in the AKR1C active site for 3β-reduction [102,103].”
From Human steroid biosynthesis, metabolism and excretion are differentially reflected by serum and urine steroid metabolomes: a comprehensive review (2019) · cites this paper as [103]
Alternatively, progesterone can first be reduced to 20α-hydroxyprogesterone, which can then be further 5β-reduced by AKR1D1 and 3α-reduced by AKR1C1-4.
“Alternatively, progesterone can first be reduced to 20α-hydroxyprogesterone, which can then be further 5β-reduced by AKR1D1 and 3α-reduced by AKR1C1–4 [103].”
From Human steroid biosynthesis, metabolism and excretion are differentially reflected by serum and urine steroid metabolomes: a comprehensive review (2019) · cites this paper as [103]
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Green, K. D., Thomason, G. K., & Czuba, L. C. (2026) · Drug Metabolism and Disposition · doi:10.1016/j.dmd.2026.100340
Garbacik, S. R. (2014) · UKnowledge (University of Kentucky)
- Authors
- Jin, Y., Mesaros, A. C., Blair, I. A., & Penning, T. M.
- Affiliations
- University of Pennsylvania (US)
- Corresponding author
- Jin, Yi
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 2011-06-14
- Volume
- 437
- Issue
- 1
- Pages
- 53-61
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- PMC
- PMC3825703
- OpenAlex
- W1977316205
- Cited by
- 49
- References
- 44
- Citations by year
- 2026: 4 · 2025: 4 · 2024: 4 · 2021: 2 · 2020: 3 · 2019: 2 · 2018: 3 · 2017: 8 · 2016: 4 · 2015: 1 · 2014: 6 · 2013: 3 · 2012: 4
- FWCI
- 2.15
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Biochemical Journal (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Cancer Institute (R01 CA 90744, R01CA090744)
- National Institute of Diabetes and Digestive and Kidney Diseases (R01-DK47015, R01DK047015)
- National Institute of Environmental Health Sciences (P30 ES015857, R01ES015857, P30ES013508)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Aldose Reductase and Taurine
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Steroid Chemistry and Biochemistry
- Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Pharmacology › Pharmacogenetics and Drug Metabolism
- Keywords
- AKR1D1, aldo-keto reductase superfamily, testosterone metabolism, progesterone metabolism, 5β-dihydrotestosterone, stereospecific reduction, hepatic steroid metabolism, enzyme kinetics, molecular docking
- MeSH terms
- Aldo-Keto Reductase Family 1 Member C3, Binding Sites, Catalysis, Humans, Hydroxyprostaglandin Dehydrogenases, Hydroxysteroid Dehydrogenases, Ketosteroids, Kinetics, Oxidation-Reduction, Oxidoreductases, Progesterone, Stereoisomerism, Testosterone, 20-Hydroxysteroid Dehydrogenases, 3-Hydroxysteroid Dehydrogenases, 3-alpha-Hydroxysteroid Dehydrogenase (B-Specific)
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