Identification of UBIAD1 as a novel human menaquinone-4 biosynthetic enzyme

被引:0
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作者
Kimie Nakagawa
Yoshihisa Hirota
Natsumi Sawada
Naohito Yuge
Masato Watanabe
Yuri Uchino
Naoko Okuda
Yuka Shimomura
Yoshitomo Suhara
Toshio Okano
机构
[1] Kobe Pharmaceutical University,Department of Hygienic Sciences
[2] 4-19-1,undefined
[3] Motoyamakita-machi,undefined
[4] Higashinada-ku,undefined
[5] Kobe 658-8558,undefined
[6] Japan,undefined
来源
Nature | 2010年 / 468卷
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摘要
Vitamin K, an important factor in blood clotting and bone metabolism, is present in the diet principally as phylloquinone (PK) from plants. One form of the vitamin, menaquinone-4 or MK-4, has a highly specific tissue distribution in the brain, kidney and pancreas in humans and in rats, suggestive of local synthesis from phylloquinone. An enzyme catalysing that synthesis has now been identified: UbiA prenyltransferase containing 1 (UBIAD1) is a human homologue of an Escherichia coli enzyme. Previously its function was unclear, although it is a candidate gene in Schnyder crystalline corneal dystrophy. The discovery of a human MK-4 enzyme able to biosynthesize the hormonally active form of vitamin K is of relevance to work on human vitamin K requirements and bone health.
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页码:117 / 121
页数:4
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