ReviewThe Journal of steroid biochemistry and molecular biology2015
Promiscuity and diversity in 3-ketosteroid reductases.
Review in The Journal of steroid biochemistry and molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 43 citations in OpenAlex.
- Brain Metabolism of Allopregnanolone and Isoallopregnanolone in Male Rat Brain.International journal of molecular sciences · 2025Article
- Specific and potent inhibition of steroid hormone pre-receptor regulator AKR1C2 by perfluorooctanoic acid: Implications for androgen metabolism.The Journal of steroid biochemistry and molecular biology · 2025Article
- Long read sequencing characterises a novel structural variant, revealing underactive AKR1C1 with overactive AKR1C2 as a possible cause of severe chronic fatigue.Journal of translational medicine · 2023Article
- Deletion of the gene encoding prostamide/prostaglandin F synthase reveals an important role in regulating intraocular pressure.Prostaglandins, leukotrienes, and essential fatty acids · 2021Article
- Multi-Omics Driven Metabolic Network Reconstruction and Analysis of Lignocellulosic Carbon Utilization inFrontiers in bioengineering and biotechnology · 2020Article
- AKR1C3 (type 5 17β-hydroxysteroid dehydrogenase/prostaglandin F synthase): Roles in malignancy and endocrine disorders.Molecular and cellular endocrinology · 2019Review
- Alternative (backdoor) androgen production and masculinization in the human fetus.PLoS biology · 2019Article
- C-4 sterol demethylation enzymes distinguish bacterial and eukaryotic sterol synthesis.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Functional Analogy in Human Metabolism: Enzymes with Different Biological Roles or Functional Redundancy?Genome biology and evolution · 2017Article
- Current physico-biochemistry in steroid research and status of structural biology for steroid-converting enzymes.The Journal of steroid biochemistry and molecular biology · 2016Review
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Many steroid hormones contain a Δ(4)-3-ketosteroid functionality that undergoes sequential reduction by 5α- or 5β- steroid reductases to produce 5α- or 5β-dihydrosteroids; and a subsequent 3-keto-reduction to produce a series of isomeric tetrahydrosteroids. Apart from steroid 5α-reductase all the remaining enzymes involved in the two step reduction process in humans belong to the aldo-keto reductase (AKR) superfamily. The enzymes involved in 3-ketosteroid reduction are AKR1C1-AKR1C4. These enzymes are promiscuous and also catalyze 20-keto- and 17-keto-steroid reduction. Interest in these reactions exist since they regulate steroid hormone metabolism in the liver, and in steroid target tissues, they may regulate steroid hormone receptor occupancy. In addition many of the dihydrosteroids are not biologically inert. The same enzymes are also involved in the metabolism of synthetic steroids e.g., hormone replacement therapeutics, contraceptive agents and inhaled glucocorticoids, and may regulate drug efficacy at their cognate receptors. This article reviews these reactions and the structural basis for substrate diversity in AKR1C1-AKR1C4, ketosteroid reductases. This article is part of a Special Issue entitled 'Steroid/Sterol signaling'.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.