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Chem Biol Interact. 1998 Feb 20;109(1-3):123-7.

Structural and functional characterisation of human sulfotransferases.

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Department of Physiology and Pharmacology, The University of Queensland, Brisbane, Australia.


The human aryl sulfotransferases HAST4 and HAST4v vary by only two amino acids but exhibit markedly different affinity towards the sulfonate acceptor p-nitrophenol and the sulfonate donor 3'-phosphoadenosine-5'-phosphosulfate (PAPS). To determine the importance of each of these amino acid differences, chimeric constructs were made of HAST4 and HAST4v. By attaching the last 120 amino acids of HAST4v to HAST4 (changing Thr235 to Asn235) we have been able to produce a protein that has a Km for PAPS similar to HAST4v. The reverse construct, HAST4v/4 produces a protein with a Km for PAPS similar to HAST4. These data suggests that the COOH-terminal of sulfotransferases is involved in co-factor binding.

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