Structure-Function Analysis of Vitamin D 24-Hydroxylase (CYP24A1) by Site-Directed Mutagenesis: Amino Acid Residues Responsible for Species-Based Difference of CYP24A1 between Humans and Rats-Reference-Cited by-同舟云学术

Structure-Function Analysis of Vitamin D 24-Hydroxylase (CYP24A1) by Site-Directed Mutagenesis: Amino Acid Residues Responsible for Species-Based Difference of CYP24A1 between Humans and Rats

Published:2006-04-14 Issue:1 Volume:70 Page:120-128
ISSN:0026-895X
Container-title:Molecular Pharmacology
language:en
Short-container-title:Mol Pharmacol

Author:

Hamamoto Hiromi,Kusudo Tatsuya,Urushino Naoko,Masuno Hiroyuki,Yamamoto Keiko,Yamada Sachiko,Kamakura Masaki,Ohta Miho,Inouye Kuniyo,Sakaki Toshiyuki

Publisher

American Society for Pharmacology & Experimental Therapeutics (ASPET)

Subject

Pharmacology,Molecular Medicine

Reference45 articles.

1. METABOLISM OF 2α-PROPOXY-1α,25-DIHYDROXYVITAMIN D3AND 2α-(3-HYDROXYPROPOXY)-1α,25-DIHYDROXYVITAMIN D3BY HUMAN CYP27A1 AND CYP24A1

2. Further Oxidation of Hydroxycalcidiol by Calcidiol 24-Hydroxylase. A Study with the Mature Enzyme Expressed in Escherichia coli

3. Rat cytochrome P450C24 (CYP24A1) and the role of F249 in substrate binding and catalytic activity

4. Human 25-Hydroxyvitamin D3-24-Hydroxylase, a Multicatalytic Enzyme

5. Immunological properties of vitamin D analogues and metabolites

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