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Structure, function and polymorphism of human cytosolic sulfotransferases
Lindsay, Julian2; Wang, Lin-Lin1,3; Li, Yong1; Zhou, Shu-Feng3
关键词Sulfotransferase Sulfonation Polymorphism Toxicity
刊名CURRENT DRUG METABOLISM
2008-02-01
9期:2页:99-105
收录类别SCI
文章类型Review
WOS标题词Science & Technology
类目[WOS]Biochemistry & Molecular Biology ; Pharmacology & Pharmacy
研究领域[WOS]Biochemistry & Molecular Biology ; Pharmacology & Pharmacy
关键词[WOS]PHENOL SULFOTRANSFERASE ; HUMAN LIVER ; DEHYDROEPIANDROSTERONE SULFOTRANSFERASE ; GENETIC POLYMORPHISMS ; ALLELE FREQUENCIES ; LUNG-CANCER ; SULT1A1 ; PHARMACOGENETICS ; IDENTIFICATION ; SULFATION
英文摘要

The sulfotransferase (SULTs) catalyzes the sulfonation of a multitude of xenobiotics, hormones and neurotransmitters. This review has summarised the SULT family in detail, the structure of the twelve known enzymes, in their four known groups (SULT1, SULT2, SULT4, and SULT6) and the substrates for each respective SULT. Hepatic sulfonation is a common phase II metabolic mechanism for increasing molecular hydrophilicity in preparation for biliary excretion or efflux across the hepatic basolateral membrane for subsequent renal clearance. To date, a total of 13 human cytosolic SULT genes have been identified which spread across four families; SULT1, SULT2, SULT4, and SULT6. The established structures of SULTs provide evidence for both enzyme/substrate and enzyme/cofactor binary complexes, consistent with a random bi-bi mechanism and ruling out an ordered mechanism in which binding of substrate requires binding of cofactor (or vice versa). Members of the SULT1 family have demonstrated the ability to sulfonate simple (small planar) phenols including estradiol, thyroid hormones, environmental xenobiotics and drugs. The SULT2 family members catalyze sulfonation of hydroxyl groups of steroids, such as androsterone, allopregnanolone, and dehydroepiandrosterone. As yet, no known substrate or function has been identified for the SULT4 family, and the SULT6B1 gene, expressed in the testis of primates, has neither the protein nor its enzymatic activity characterized. The extent of nucleotide variation found in members of the SULT gene family is similar to that observed for other groups of human genes. Substrate inhibition was observed for most substrates with a trend in maximum velocity (V-max) of *1>*3>*2. There does appear to be an inter-ethnic/inter-racial difference in the incidence of the various SULT1A1 alleles also. There is mounting evidence to suggest that further research and understanding in the area of phase II metabolism and the SULT enzyme will have a great benefit in a clinical setting. Already research in the field is finding links with cancer and sulfonation-related disease, promising to deliver great advances in clinical practice in the future.

语种英语
WOS记录号WOS:000253936700001
引用统计
被引频次:79[WOS]   [WOS记录]     [WOS相关记录]
文献类型期刊论文
条目标识符http://ir.bjmu.edu.cn/handle/400002259/50293
专题北京大学公共卫生学院
作者单位1.Peking Univ, Sch Publ Hlth, Dept Nutr & Food Hyg, Beijing 100083, Peoples R China
2.Queensland Univ Technol, Div Pharma, Sch Life Sci, Brisbane, Qld, Australia
3.RMIT Univ, WHO Collaborating Ctr Tradit Med, Sch Hlth Sci, Div Chinese Med, Bundoora, Vic, Australia
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GB/T 7714
Lindsay, Julian,Wang, Lin-Lin,Li, Yong,et al. Structure, function and polymorphism of human cytosolic sulfotransferases[J]. CURRENT DRUG METABOLISM,2008,9(2):99-105.
APA Lindsay, Julian,Wang, Lin-Lin,Li, Yong,&Zhou, Shu-Feng.(2008).Structure, function and polymorphism of human cytosolic sulfotransferases.CURRENT DRUG METABOLISM,9(2),99-105.
MLA Lindsay, Julian,et al."Structure, function and polymorphism of human cytosolic sulfotransferases".CURRENT DRUG METABOLISM 9.2(2008):99-105.
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