Inhibition of 3(17)alpha-hydroxysteroid dehydrogenase (AKR1C21) by aldose reductase inhibitors

Urmi Dhagat; Satoshi Endo; Akira Hara; Ossama El-Kabbani

Inhibition of 3(17)alpha-hydroxysteroid dehydrogenase (AKR1C21) by aldose reductase inhibitors

Urmi Dhagat, Satoshi Endo, Akira Hara, Ossama El-Kabbani

Medicinal Chemistry

Research output: Contribution to journal › Article › Research › peer-review

12 Citations (Scopus)

Abstract

Mouse 3(17)a-hydroxysteroid clehydrogenase (AKR1C21) is a member of the aldo-keto reductase superfamily that catalyses the oxido-reduction of steroid hormones such as estrogens, androgens and neurosteroids. Inhibitors of aldose reductase (AR), a member of the same superfamily, were evaluated against AKR1C21. Models of the enzyme-inbibitor complexes suggest that Tyr118 and Phe311 are important residues for inhibitor recognition and orientation in the active site of AKR1C21. (C) 2008 Published by Elsevier Ltd.

Original language	English
Pages (from-to)	3245 - 3254
Number of pages	10
Journal	Bioorganic & Medicinal Chemistry
Volume	16
Issue number	6
Publication status	Published - 2008

Cite this

@article{fc5e45a37e13464eb4cf0499565c1873,

title = "Inhibition of 3(17)alpha-hydroxysteroid dehydrogenase (AKR1C21) by aldose reductase inhibitors",

abstract = "Mouse 3(17)a-hydroxysteroid clehydrogenase (AKR1C21) is a member of the aldo-keto reductase superfamily that catalyses the oxido-reduction of steroid hormones such as estrogens, androgens and neurosteroids. Inhibitors of aldose reductase (AR), a member of the same superfamily, were evaluated against AKR1C21. Models of the enzyme-inbibitor complexes suggest that Tyr118 and Phe311 are important residues for inhibitor recognition and orientation in the active site of AKR1C21. (C) 2008 Published by Elsevier Ltd.",

author = "Urmi Dhagat and Satoshi Endo and Akira Hara and Ossama El-Kabbani",

year = "2008",

language = "English",

volume = "16",

pages = "3245 -- 3254",

journal = "Bioorganic \& Medicinal Chemistry",

issn = "0968-0896",

publisher = "Elsevier",

number = "6",

}

TY - JOUR

T1 - Inhibition of 3(17)alpha-hydroxysteroid dehydrogenase (AKR1C21) by aldose reductase inhibitors

AU - Dhagat, Urmi

AU - Endo, Satoshi

AU - Hara, Akira

AU - El-Kabbani, Ossama

PY - 2008

Y1 - 2008

N2 - Mouse 3(17)a-hydroxysteroid clehydrogenase (AKR1C21) is a member of the aldo-keto reductase superfamily that catalyses the oxido-reduction of steroid hormones such as estrogens, androgens and neurosteroids. Inhibitors of aldose reductase (AR), a member of the same superfamily, were evaluated against AKR1C21. Models of the enzyme-inbibitor complexes suggest that Tyr118 and Phe311 are important residues for inhibitor recognition and orientation in the active site of AKR1C21. (C) 2008 Published by Elsevier Ltd.

AB - Mouse 3(17)a-hydroxysteroid clehydrogenase (AKR1C21) is a member of the aldo-keto reductase superfamily that catalyses the oxido-reduction of steroid hormones such as estrogens, androgens and neurosteroids. Inhibitors of aldose reductase (AR), a member of the same superfamily, were evaluated against AKR1C21. Models of the enzyme-inbibitor complexes suggest that Tyr118 and Phe311 are important residues for inhibitor recognition and orientation in the active site of AKR1C21. (C) 2008 Published by Elsevier Ltd.

UR - http://www.sciencedirect.com/science/article/pii/S0968089607010668

M3 - Article

SN - 0968-0896

VL - 16

SP - 3245

EP - 3254

JO - Bioorganic & Medicinal Chemistry

JF - Bioorganic & Medicinal Chemistry

IS - 6

ER -

Inhibition of 3(17)alpha-hydroxysteroid dehydrogenase (AKR1C21) by aldose reductase inhibitors

Abstract

Other files and links

Cite this