Crystal Structures of Human Δ4-3-Ketosteroid 5β-Reductase (AKR1D1) Reveal the Presence of an Alternative Binding Site Responsible for Substrate Inhibition,-Reference-Cited by-同舟云学术

Crystal Structures of Human Δ4-3-Ketosteroid 5β-Reductase (AKR1D1) Reveal the Presence of an Alternative Binding Site Responsible for Substrate Inhibition,

Published:2008-11-26 Issue:51 Volume:47 Page:13537-13546
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Faucher Frédérick¹,Cantin Line¹,Luu-The Van¹,Labrie Fernand¹,Breton Rock¹

Affiliation:

1. Oncology and Molecular Endocrinology Research Center, Laval University Medical Center (CHUL) and Laval University, Laval, Québec (QC) G1V 4G2, Canada

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi801276h

Reference45 articles.

1. Conversion of Cholesterol to Bile Acids in Rat: Purification and Properties of a Delta4-3-Ketosteroid 5beta-Reductase and a 3alpha-Hydroxysteroid Dehydrogenase. Bile Acids and Steroids 187

2. Enzymatic Conversion of a Delta4-3-Ketosteroid into a 3alpha-Hydroxy-5beta-Steroid: Mechanism and Stereochemistry of Hydrogen Transfer from NADPH. Bile Acids and Steroids 190

3. Synthesis and Metabolism of Cholest-4-ene-7α, 12α-diol-3-one and 5β-Cholestane-7α,12α-diol-3-one

4. 3-OXO-Δ4 BILE ACIDS IN LIVER DISEASE

5. Mutations in SRD5B1 (AKR1D1), the gene encoding 4-3-oxosteroid 5 -reductase, in hepatitis and liver failure in infancy

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