Abstract：
: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 in 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 PAP, beta form of phenol sulfotransferase is produced.
journal_name
Chem Biol Interactjournal_title
Chemico-biological interactionsauthors
Yang YS,Tsai SW,Lin ESdoi
10.1016/s0009-2797(97)00127-0subject
Has Abstractpub_date
1998-02-20 00:00:00pages
129-35issue
1-3eissn
0009-2797issn
1872-7786pii
S0009-2797(97)00127-0journal_volume
109pub_type
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