17beta-hydroxysteroid dehydrogenase (HSD)/17-ketosteroid reductase (KSR) family; nomenclature and main characteristics of the 17HSD/KSR enzymes

Peltoketo, H; Luu-The, V; Simard, J; Adamski, J

doi:10.1677/jme.0.0230001

Cited by 309Steroid Chemistry and BiochemistrySexual Differentiation and DisordersEstrogen and related hormone effects

17beta-hydroxysteroid dehydrogenase (HSD)/17-ketosteroid reductase (KSR) family; nomenclature and main characteristics of the 17HSD/KSR enzymes

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Peltoketo, H, Luu-The, V, Simard, J, Adamski, J·1999·Journal of Molecular Endocrinology

DOI 10.1677/jme.0.0230001

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Abstract

A number of enzymes possessing 17beta-hydroxysteroid dehydrogenase/17-ketosteroid reductase (17HSD/KSR) activities have been described and cloned, but their nomenclature needs specification. To clarify the present situation, descriptions of the eight cloned 17HSD/KSRs are given and guidelines for the classification of novel 17HSD/KSR enzymes are presented.

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There are at least 14 human 17βHSD isoforms; these isoforms vary widely in size, structure, substrate specificity, cofactor utilization, and physiological functions.
“There are at least 14 human 17␤HSD isoforms; these isoforms vary widely in size, structure, substrate specificity, cofactor utilization, and physiological functions (502).”
From The Molecular Biology, Biochemistry, and Physiology of Human Steroidogenesis and Its Disorders (2011) · cites this paper as [502]
The Introduction (page unavailable) says that eight 17HSD/KSR types had been cloned, not that there were at least 14 human isoforms. The Similarity/Diversity section (page unavailable) supports differences in structure, substrate specificity and cofactor specificity, but the cited paper does not support the claimed count. (LLM, conf=0.90)
Experimental — accuracy not yet measured
The widespread tissue distribution and broad substrate specificity of 17βHSD2 suggests that its role in human physiology is to protect tissues from excessive exposure to active steroid hormones by oxidation to inactive 17-ketosteroids.
“The widespread tissue distribution and broad substrate specificity of 17␤HSD2 suggests that its role in human physiology is to protect tissues from excessive exposure to active steroid hormones by oxidation to inactive 17-ketosteroids (502).”
From The Molecular Biology, Biochemistry, and Physiology of Human Steroidogenesis and Its Disorders (2011) · cites this paper as [502]
The 17HSD/KSR2 section says the enzyme is widely expressed, converts several active steroids to less active forms, and has been suggested to protect tissues from excessive steroid action. It describes the products as “less active,” not inactive, so that part of the claim overstates the source. No page number is available in our copy. (LLM, conf=0.86)
Experimental — accuracy not yet measured
Estrone undergoes 16α-hydroxylation and HSD17B1 catalyzed reduction, while 17β-estradiol only requires 16α-hydroxylation to yield estriol.
“Estrone undergoes 16α-hydroxylation and HSD17B1 catalyzed reduction, while 17β-estradiol only requires 16α-hydroxylation [[311], [312], [313], [314]].”
From Human steroid biosynthesis, metabolism and excretion are differentially reflected by serum and urine steroid metabolomes: a comprehensive review (2019) · cites this paper as [311]

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[57]57. Maxwell MM, Nearing J & Aziz N 1995 Ke 6 gene. Sequence and organization and aberrant regulation in murine polycystic kidney disease. Journal of Biological Chemistry 270 25213-25219.
[64]64. Mustonen MVJ, Poutanen MH, Isomaa VV, Vihko PT & Vihko RK 1997b Cloning of mouse 17 -hydroxysteroid dehydrogenase type 2, and analysing expression of the mRNAs for types 1, 2, 3, 4 and 5 in mouse embryos and adult tissues. Biochemical Journal 325 199-205.

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Authors: Peltoketo, H., Luu-The, V, Simard, J., & Adamski, J.
Affiliations: University of Oulu (FI)
Centre hospitalier de l'Université Laval (CA)
Helmholtz Munich (DE)
ORCID: Peltoketo, H
Simard, J
Adamski, J
Venue: Journal of Molecular Endocrinology
Publisher: Bioscientifica
Published: 1999-08-01
Volume: 23
Issue: 1
Pages: 1-11
ISSN: 0952-5041 (ISSN-L)
1479-6813
DOI: 10.1677/jme.0.0230001
OpenAlex: W2116838171
Semantic Scholar: 09af775fcb4aa1e427eb5e859c6ee8074a5ccf34
Cited by: 302
References: 101
Citations by year: 2026: 2 · 2025: 4 · 2024: 4 · 2023: 5 · 2022: 3 · 2021: 2 · 2020: 7 · 2019: 4 · 2018: 3 · 2017: 5 · 2016: 8 · 2015: 11 · 2014: 9 · 2013: 6 · 2012: 8
FWCI: 1.68
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Journal of Molecular Endocrinology (publishedVersion)
PubMed (publishedVersion)
Funders: World Health Organization
Deutsche Forschungsgemeinschaft
Medical Research Council Canada
Medical Research Council
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Steroid Chemistry and Biochemistry
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Sexual Differentiation and Disorders
Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Estrogen and related hormone effects
Keywords: 17β-hydroxysteroid dehydrogenase, enzyme nomenclature, enzyme classification, steroid metabolism
MeSH terms: Animals, Humans, Terminology as Topic, 17-Hydroxysteroid Dehydrogenases

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17beta-hydroxysteroid dehydrogenase (HSD)/17-ketosteroid reductase (KSR) family; nomenclature and main characteristics of the 17HSD/KSR enzymes

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