Cited by 166Aldose Reductase and TaurineSteroid Chemistry and BiochemistryEstrogen and related hormone effects

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Structural and functional biology of aldo-keto reductase steroid transforming enzymes

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Penning, Trevor M, Wangtrakuldee, Phumvadee, Auchus, Richard J·2019·Endocrine Reviews

DOI 10.1210/er.2018-00089PMC PMC6405412

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Abstract

Aldo-keto reductases (AKRs) are monomeric NAD(P)(H)-dependent oxidoreductases that play pivotal roles in the biosynthesis and metabolism of steroids in humans. AKR1C enzymes acting as 3-ketosteroid, 17-ketosteroid, and 20-ketosteroid reductases are involved in the prereceptor regulation of ligands for the androgen, estrogen, and progesterone receptors and are considered drug targets to treat steroid hormone-dependent malignancies and endocrine disorders. In contrast, AKR1D1 is the only known steroid 5β-reductase and is essential for bile-acid biosynthesis, the generation of ligands for the farnesoid X receptor, and the 5β-dihydrosteroids that have their own biological activity. In this review we discuss the crystal structures of these AKRs, their kinetic and catalytic mechanisms, AKR genomics (gene expression, splice variants, polymorphic variants, and inherited genetic deficiencies), distribution in steroid target tissues, roles in steroid hormone action and disease, and inhibitor design.

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Authors: Penning, T. M., Wangtrakuldee, P., & Auchus, R. J.
Affiliations: University of Pennsylvania (US)
University of Michigan (US)
Corresponding author: Penning, Trevor M
ORCID: Penning, Trevor M
Auchus, Richard J
Venue: Endocrine Reviews
Publisher: The Endocrine Society
Published: 2018-08-20
Volume: 40
Issue: 2
Pages: 447-475
ISSN: 0163-769X (ISSN-L)
1945-7189
DOI: 10.1210/er.2018-00089
PMC: PMC6405412
OpenAlex: W2888187525
Cited by: 164
References: 171
Citations by year: 2026: 30 · 2025: 28 · 2024: 34 · 2023: 27 · 2022: 19 · 2021: 16 · 2020: 7 · 2019: 3
FWCI: 0.76
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Endocrine Reviews (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Institute of Environmental Health Sciences (P30 ES013508)
National Institute of General Medical Sciences (R01GM086596)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Aldose Reductase and Taurine
Physical Sciences › Chemistry › Organic Chemistry › Steroid Chemistry and Biochemistry
Life Sciences › Biochemistry, Genetics and Molecular Biology › Endocrinology › Estrogen and related hormone effects
Keywords: aldo-keto reductase, AKR1D1, steroid metabolism, androgen receptor, estrogen receptor, progesterone receptor, bile acid synthesis, farnesoid X receptor, enzyme crystal structure, catalytic mechanism, enzyme kinetics, splice variants, genetic polymorphism, enzyme inhibitors, endocrine disorders
MeSH terms: Aldo-Keto Reductases, Humans, Hydroxysteroid Dehydrogenases, Oxidoreductases, Steroids

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Structural and functional biology of aldo-keto reductase steroid transforming enzymes

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