Evidence of Allosteric Coupling between Substrate Binding and Adx Recognition in the Vitamin D Carbon-24 Hydroxylase CYP24A1-Reference-Cited by-同舟云学术

Evidence of Allosteric Coupling between Substrate Binding and Adx Recognition in the Vitamin D Carbon-24 Hydroxylase CYP24A1

Published:2020-04-07 Issue:15 Volume:59 Page:1537-1548
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Kumar Amit¹,Wilderman P. Ross²,Tu Chengjian³,Shen Shichen³,Qu Jun³^ORCID,Estrada D. Fernando¹^ORCID

Affiliation:

1. Department of Biochemistry, Jacobs School of Medicine, University at Buffalo, 955 Main Street, Buffalo, New York 14203, United States

2. Department of Pharmaceutical Sciences, School of Pharmacy, University of Connecticut, 69 North Eagleville Road, Storrs, Connecticut 06269, United States

3. Department of Pharmaceutical Sciences, School of Pharmacy, University at Buffalo, 318 Pharmacy Building, Buffalo, New York 14214, United States

Funder

National Institute of General Medical Sciences

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.0c00107

Reference41 articles.

1. Cytochrome P450-mediated metabolism of vitamin D

2. Liver mitochondrial cytochrome P450 CYP27 and recombinant-expressed human CYP27 catalyze 1 alpha-hydroxylation of 25-hydroxyvitamin D3.

3. Isolation and expression of human 1,25-dihydroxyvitamin D3 24-hydroxylase cDNA.

4. Identification of a new C-23 oxidation pathway of metabolism for 1,25-dihydroxyvitamin D3 present in intestine and kidney.

5. Dual metabolic pathway of 25-hydroxyvitamin D3 catalyzed by human CYP24

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