Structural and functional characterisation of human sulfotransferases

Chemico-Biological Interactions

Volumn 109, Issue 1-3, 1998, Pages 123-127

  Brix, Lulu A ^a   Nicoll, Raelene ^a   Zhu, Xiaoyi ^a   McManus, Michael E ^a  

^a UNIVERSITY OF QUEENSLAND   (Australia)

Author keywords

Active site; Function; Human; Structure; Sulfotransferase

Indexed keywords

4 NITROPHENOL; ADENOSINE 3' PHOSPHATE 5' PHOSPHOSULFATE; ARYL SULFOTRANSFERASE; ASPARAGINE; CHIMERIC PROTEIN; DOPAMINE; THREONINE;

CARBOXY TERMINAL SEQUENCE; CONFERENCE PAPER; CONTROLLED STUDY; ENZYME BINDING; ENZYME KINETICS; HUMAN; STRUCTURE ACTIVITY RELATION;

ARYLSULFOTRANSFERASE; HUMANS; ISOENZYMES; KINETICS; PHOSPHOADENOSINE PHOSPHOSULFATE; RECOMBINANT FUSION PROTEINS; SUBSTRATE SPECIFICITY;

EID: 0032548877     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0009-2797(97)00126-9     Document Type: Conference Paper

References (14)

1. Coughtrie M.W.H. Sulphation catalysed by the human cytosolic sulphotransferases - chemical defence or molecular terrorism? Hum. Exp. Toxicol. 15:1996;547-555.
2. Weinshilboum R., Otterness D. Sulfotransferase enzymes. Kauffman F.C. Handbook of Experimental Pharmacology. 1994;45-78 Springer, Berlin.
3. Zhu X., Veronese M.E., Sansom L.N., McManus M.E. Molecular characterisation of a human aryl sulfotransferase cDNA. Biochem. Biophys. Res. Commun. 192:1993;671-676.
4. Zhu X., Veronese M.E., Bernard C.C.A., Sansom L.N., McManus M.E. Identification of two human brain aryl sulfotransferase cDNAs. Biochem. Biophys. Res. Commun. 195:1993;120-127.
5. Zhu X., Veronese M.E., Iocco P., McManus M.E. cDNA cloning and expression of a new form of human aryl sulfotransferase. Int. J. Biochem. Cell. Biol. 28:1996;565-571.
6. Veronese M.E., Burgess W., Zhu X., McManus M.E. Functional characterization of two human sulphotransferase cDNAs that encode monoamine- and phenol-sulphating forms of phenol sulphotransferase: substrate kinetics, thermal-stability and inhibitor-sensitivity studies. Biochem. J. 302:1994;497-502.
7. Marsolais F., Varin L. Identification of amino acid residues critical for catalysis and cosubstrate binding in the flavonol 3-sulfotransferase. J. Biol. Chem. 270:1995;30458-30463.
8. Komatsu K., Driscoll W.J., Koh Y., Strott C.A. A P-loop related motif (GxxGxxK) highly conserved in sulfotransferases is required for binding the activated sulfate donor. Biochem. Biophys. Res. Commun. 204:1994;1178-1185.
9. Driscoll W.J., Komatsu K., Strott C.A. Proposed active site domain in estrogen sulfotransferase as determined by mutational analysis. Proc. Natl. Acad. Sci. USA. 92:1995;12328-12332.
10. Zheng Y., Bergold A., Duffel M.W. Affinity labelling of aryl sulfotransferase IV. J. Biol. Chem. 269:1994;30313-30319.
11. Varin L., Marsolais F., Brisson N. Chimeric flavonol sulfotransferases define a domain responsible for substrate and position specificities. J. Biol. Chem. 270:1995;12498-12502.
12. Borchardt R.T., Schasteen C.S. Phenol-sulfotransferase inactivation by 2,3-butanedione and phenylglyoxal: evidence for an active site arginyl residue. Biochem. Biophys. Res. Commun. 78:1977;1067-1073.
13. Borchardt R.T., Schasteen C.S., Wu S.-E. Phenol sulfotransferase II. Inactivation by phenylglyoxal, N-ethylmaleimide and ribonucleotide 2′,3′-dialdehydes. Biochim. Biophys. Acta. 708:1982;280-293.
14. Foldes A., Meek J.L. Rat brain phenol sulfotransferase - partial purification and some properties. Biochim. Biophys. Acta. 327:1973;365-373.