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Substrate specificities of cytochrome P-450, C-P-450(16)alpha and P-450(15)alpha, and contribution to steroid hydroxylase activities in mouse liver microsomes.

作者信息

Harada N, Negishi M

机构信息

Pharmacogenetics Section, National Institute of Environmental Health Sciences, Research Triangle Park, NC 27709.

出版信息

Biochem Pharmacol. 1988 Dec 15;37(24):4778-80. doi: 10.1016/0006-2952(88)90352-8.

DOI:10.1016/0006-2952(88)90352-8
PMID:3202910
Abstract
摘要

相似文献

1
Substrate specificities of cytochrome P-450, C-P-450(16)alpha and P-450(15)alpha, and contribution to steroid hydroxylase activities in mouse liver microsomes.细胞色素P-450、C-P-450(16)α和P-450(15)α的底物特异性及其对小鼠肝脏微粒体中类固醇羟化酶活性的贡献。
Biochem Pharmacol. 1988 Dec 15;37(24):4778-80. doi: 10.1016/0006-2952(88)90352-8.
2
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Evidence for a specific cytochrome P-450 with short half-life catalyzing 7 alpha-hydroxylation of cholesterol.具有短半衰期的特定细胞色素P-450催化胆固醇7α-羟化作用的证据。
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Purification and characterization of constituent testosterone 2 alpha-hydroxylase (cytochrome P450(2)alpha) from mouse liver.从小鼠肝脏中纯化并鉴定组成型睾酮2α-羟化酶（细胞色素P450(2)α）
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Maturation of various testosterone hydroxylase activities in hepatic microsomes from AKR/J mice.AKR/J小鼠肝脏微粒体中各种睾酮羟化酶活性的成熟。
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Steroid hydroxylations catalyzed by cytochrome P-450.细胞色素P-450催化的类固醇羟基化反应。
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Point mutations at threonine-301 modify substrate specificity of rabbit liver microsomal cytochromes P-450 (laurate (omega-1)-hydroxylase and testosterone 16 alpha-hydroxylase).
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Properties of reconstituted cholesterol 7 alpha-hydroxylase system from rat and rabbit liver microsomes.大鼠和兔肝脏微粒体中重组胆固醇7α-羟化酶系统的特性
Eur J Biochem. 1979 Jan 15;93(2):419-26. doi: 10.1111/j.1432-1033.1979.tb12838.x.

引用本文的文献

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Determinants of the substrate specificity of human cytochrome P-450 CYP2D6: design and construction of a mutant with testosterone hydroxylase activity.人细胞色素P-450 CYP2D6底物特异性的决定因素：具有睾酮羟化酶活性突变体的设计与构建
Biochem J. 1998 May 1;331 ( Pt 3)(Pt 3):783-92. doi: 10.1042/bj3310783.
2
Site-directed mutagenesis of mouse steroid 7 alpha-hydroxylase (cytochrome P-450(7) alpha): role of residue-209 in determining steroid-cytochrome P-450 interaction.小鼠类固醇7α-羟化酶（细胞色素P-450(7)α）的定点诱变：209位残基在确定类固醇-细胞色素P-450相互作用中的作用。
Biochem J. 1993 Apr 15;291 ( Pt 2)(Pt 2):569-73. doi: 10.1042/bj2910569.
3
Multiple steroid-binding orientations: alteration of regiospecificity of dehydroepiandrosterone 2- and 7-hydroxylase activities of cytochrome P-450 2a-5 by mutation of residue 209.
多种类固醇结合方向：通过209位残基突变改变细胞色素P-450 2a-5的脱氢表雄酮2-羟化酶和7-羟化酶活性的区域特异性
Biochem J. 1995 Feb 15;306 ( Pt 1)(Pt 1):29-33. doi: 10.1042/bj3060029.