Evolution of 17β-HSD type 4, a multifunctional protein of β-oxidation

被引：52

作者：

Breitling, R ^{[1
]}

Marijanovic, Z ^{[1
]}

Perovic, D ^{[1
]}

Adamski, J ^{[1
]}

机构：

[1] GSF, Natl Res Ctr Environm & Hlth, Inst Expt Genet, D-85764 Neuherberg, Germany

来源：

MOLECULAR AND CELLULAR ENDOCRINOLOGY | 2001年 / 171卷 / 1-2期

关键词：

beta-oxidation; steroids; evolution; 17 beta-hydroxysteroid dehydrogenases; peroxisomes; HSD17B4; multifunctional protein;

D O I：

10.1016/S0303-7207(00)00415-9

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

17 beta -Hydroxysteroid dehydrogenase type 1 (17 beta -HSD4) is the most unusual among human 17 beta -HSDs. It is characterized by a multidomain structure, in which the dehydrogenase domain is fused to a hydratase and a lipid transfer domain. 17 beta -HSD4 not only inactivates estradiol by conversion to estrone but its three protein domains also participate in successive steps of peroxisomal beta -oxidation of long- and branched-chain fatty acids. We have compared the genomic structure of human 17 beta -HSD4 and several homologous genes from lower animals and fungi. Our data suggest an evolutionary scenario for the three protein domains and indicate a highly dynamic history of the enzyme but also a very high conservation of multifunctionality. This suggests that the main function of human 17 beta -HSD4 is still its involvement in fatty-acid metabolism while steroid conversion is only a secondary and possibly minor activity in vivo. (C) 2001 Elsevier Science Ireland Ltd. All rights reserved.

引用

页码：205 / 210

页数：6

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