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Characterization of rat and human CYP2J enzymes as Vitamin D 25-hydroxylases

vitamin D is 25-hydroxylated in the liver, before being activated by 1α-hydroxylation in the kidney. Recently, the rat cytochrome P450 2J3 (CYP2J3) has been identified as a principal vitamin D 25-hydroxylase in the rat [Yamasaki T, Izumi S, Ide H, Ohyama Y. Identification of a novel rat microsomal v...

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Published in:Steroids 2006-10, Vol.71 (10), p.849-856
Main Authors: Aiba, Isamu, Yamasaki, Tomoaki, Shinki, Toshimasa, Izumi, Shunsuke, Yamamoto, Keiko, Yamada, Sachiko, Terato, Hiroaki, Ide, Hiroshi, Ohyama, Yoshihiko
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cited_by cdi_FETCH-LOGICAL-c444t-37616938f3af22e3748c50c9d5c4cf1dc3d7662b2cf7e3b6c7596991a8888eec3
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container_end_page 856
container_issue 10
container_start_page 849
container_title Steroids
container_volume 71
creator Aiba, Isamu
Yamasaki, Tomoaki
Shinki, Toshimasa
Izumi, Shunsuke
Yamamoto, Keiko
Yamada, Sachiko
Terato, Hiroaki
Ide, Hiroshi
Ohyama, Yoshihiko
description vitamin D is 25-hydroxylated in the liver, before being activated by 1α-hydroxylation in the kidney. Recently, the rat cytochrome P450 2J3 (CYP2J3) has been identified as a principal vitamin D 25-hydroxylase in the rat [Yamasaki T, Izumi S, Ide H, Ohyama Y. Identification of a novel rat microsomal vitamin D 3 25-hydroxylase. J Biol Chem 2004;279(22):22848–56]. In this study, we examine whether human CYP2J2 that exhibits 73% amino acid homology to rat CYP2J3 has similar catalytic properties. Recombinant human CYP2J2 was overexpressed in Escherichia coli, purified, and assayed for vitamin D 25-hydroxylation activity. We found significant 25-hydroxylation activity toward vitamin D 3 (turnover number, 0.087 min −1), vitamin D 2 (0.16 min −1), and 1α-hydroxyvitamin D 3 (2.2 min −1). Interestingly, human CYP2J2 hydroxylated vitamin D 2, an exogenous vitamin D, at a higher rate than it did vitamin D 3, an endogenous vitamin D, whereas, rat CYP2J3 hydroxylated vitamin D 3 (1.4 min −1) more efficiently than vitamin D 2 (0.86 min −1). Our study demonstrated that human CYP2J2 exhibits 25-hydroxylation activity as well as rat CYP2J3, although the activity of human CYP2J2 is weaker than rat CYP2J3. CYP2J2 and CYP2J3 exhibit distinct preferences toward vitamin D 3 and D 2.
doi_str_mv 10.1016/j.steroids.2006.04.009
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Our study demonstrated that human CYP2J2 exhibits 25-hydroxylation activity as well as rat CYP2J3, although the activity of human CYP2J2 is weaker than rat CYP2J3. CYP2J2 and CYP2J3 exhibit distinct preferences toward vitamin D 3 and D 2.</abstract><cop>New York, NY</cop><pub>Elsevier Inc</pub><pmid>16842832</pmid><doi>10.1016/j.steroids.2006.04.009</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record>
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ispartof Steroids, 2006-10, Vol.71 (10), p.849-856
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subjects 25-Hydroxylase
Animals
Base Sequence
Biological and medical sciences
Cholestanetriol 26-Monooxygenase - chemistry
Cholestanetriol 26-Monooxygenase - metabolism
CYP2J2
CYP2J3
Cytochrome P-450 Enzyme System - chemistry
Cytochrome P-450 Enzyme System - metabolism
DNA Primers
Fundamental and applied biological sciences. Psychology
Humans
Rats
Recombinant Proteins - chemistry
Recombinant Proteins - metabolism
Vertebrates: endocrinology
vitamin D 2
vitamin D 3
title Characterization of rat and human CYP2J enzymes as Vitamin D 25-hydroxylases
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