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Human 3-alpha hydroxysteroid dehydrogenase type 3 (3 alpha-HSD3): The V54L mutation restricting the steroid alternative binding and enhancing the 20 alpha-HSD activity
文献类型:期刊
作者:Zhang, Bo[1]  Zhu, Dao-Wei[2]  Hu, Xiao-Jian[3]  Zhou, Ming[4]  Shang, Peng[5]  Lin, Sheng-Xiang[6]  
机构:[1]Ctr Hosp Univ CHU Quebec, Res Ctr CHUL, Lab Mol Endocrinol & Oncol, Quebec City, PQ G1V 4G2, Canada.,Univ Laval, Quebec City, PQ G1V 4G2, Canada.;Northwestern Polytech Univ, Sch Life Sci, Inst Special Environm Biophys, Key Lab Space Biosci & Biotechnol, Xian 710072, Peoples R China.;
[2]Ctr Hosp Univ CHU Quebec, Res Ctr CHUL, Lab Mol Endocrinol & Oncol, Quebec City, PQ G1V 4G2, Canada.,Univ Laval, Quebec City, PQ G1V 4G2, Canada.;
[3]Fudan Univ, Sch Life Sci, Shanghai 200433, Peoples R China.;
[4]Ctr Hosp Univ CHU Quebec, Res Ctr CHUL, Lab Mol Endocrinol & Oncol, Quebec City, PQ G1V 4G2, Canada.,Univ Laval, Quebec City, PQ G1V 4G2, Canada.;
[5]Northwestern Polytech Univ, Sch Life Sci, Inst Special Environm Biophys, Key Lab Space Biosci & Biotechnol, Xian 710072, Peoples R China.;
[6]Ctr Hosp Univ CHU Quebec, Res Ctr CHUL, Lab Mol Endocrinol & Oncol, Quebec City, PQ G1V 4G2, Canada.,Univ Laval, Quebec City, PQ G1V 4G2, Canada.;WHO Collaborating Ctr Res Human Reprod Hlth, Shanghai 200031, Peoples R China.;
通讯作者:Lin, SX (reprint author), CHUL Res Ctr, 2705 Boul Laurier, Quebec City, PQ G1V 4G2, Canada.
年:2014
期刊名称:JOURNAL OF STEROID BIOCHEMISTRY AND MOLECULAR BIOLOGY影响因子和分区
卷:141
页码范围:135-143
增刊:增刊
学科:生物学和生物化学
收录情况:SCI(E)(WOS:000335114500016)  (24434280)  
所属部门:生命学院
被引频次:7
人气指数:2965
浏览次数:2934
基金:Canadian Institutes of Health Research (CIHR) [MOP 97917]; U.S. DOE [DE-AC02-06CH11357]
关键词:3-Alpha hydroxysteroid dehydrogenase; AKR1C2; 20 alpha-HSD; Mutation; Kinetics; Crystal structure
摘要:
Human 3-alpha hydroxysteroid dehydrogenase type 3 (3 alpha-HSD3) has an essential role in the inactivation of 5 alpha-dihydrotestosterone (DHT). Notably, human 3 alpha-HSD3 shares 97.8% sequence identity with human 20-alpha hydroxysteroid dehydrogenase (20 alpha-HSD) and there is only one amino acid difference (residue 54) that is located in their steroid binding pockets. However, 20 alpha-HSD displays a distinctive ability in transforming progesterone to 20 alpha-hydroxy-progesterone (20 alpha- ...More
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