標題: Effects of 3 '-phosphoadenosine 5 '-phosphate on the activity and folding of phenol sulfotransferase
作者: Yang, YS
Tsai, SW
Lin, ES
生物科技學系
Department of Biological Science and Technology
關鍵字: phenol sulfotransferase IV;3 '-phosphoadenosine 5 '-phosphosulfate;3 '-phosphoadenosine 5 '-phosphate;protein folding;physiological reaction;transfer reaction
公開日期: 20-Feb-1998
摘要: Known spectroscopic and kinetic data are used to formulate pathways of the physiological and transfer reactions and the substrate inhibition of phenol sulfotransferase. Kinetic mechanisms indicate that release of PAP from enzyme complex is required for the physiological reaction but not for the transfer reaction. The pathways explain rate difference between the physiological and transfer reactions since the release of PAP is the rate-limiting step of the former reaction. Two enzyme species of phenol sulfotransferase which distinguish the physiological and transfer reaction were found to involve the binding of PAP. Differences between two forms of phenol sulfotransferase, alpha and beta, indicate that they assemble through different folding process. It is demonstrated that only alpha enzyme renatures in the presence of PAP and beta enzyme renatures only ir. the absence of PAP in vitro. In the over-expressed system, formation of alpha and beta phenol sulfotransferase is also dependent on the availability of PAP in Escherichia coli. It is concluded that folding of phenol sulfotransferase is assisted by PAP to form alpha enzyme. In the absence of PAT, beta form of phenol sulfotransferase is produced. (C) 1998 Elsevier Science Ireland Ltd. All rights reserved.
URI: http://dx.doi.org/10.1016/S0009-2797(97)00127-0
http://hdl.handle.net/11536/32788
ISSN: 0009-2797
DOI: 10.1016/S0009-2797(97)00127-0
期刊: CHEMICO-BIOLOGICAL INTERACTIONS
Volume: 109
Issue: 1-3
起始頁: 129
結束頁: 135
Appears in Collections:Conferences Paper


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