Structural basis for the broad range substrate specificity of a novel mouse cytosolic sulfotransferase-mSULT1D1

Biochemical and Biophysical Research Communications

Volumn 379, Issue 1, 2009, Pages 76-80

  Teramoto, Takamasa ^a   Sakakibara, Yoichi ^b   Liu, Ming Cheh ^c   Suiko, Masahito ^b   Kimura, Makoto ^a   Kakuta, Yoshimitsu ^a  

^a KYUSHU UNIVERSITY   (Japan)

^b UNIVERSITY OF MIYAZAKI   (Japan)

^c MEDICAL COLLEGE OF OHIO   (United States)

Author keywords

Broad range substrate specificity; Crystal structure; Cytosolic sulfotransferase; Sulfonation; SULT

Indexed keywords

1 NAPHTHOL; 4 NITROPHENOL; ADENOSINE 3',5' DIPHOSPHATE; ADENOSINE DERIVATIVE; AMINO ACID; CELL ENZYME; DOPAMINE; ENZYME BINDING SITE; GLUTAMIC ACID; ISOLEUCINE; SEROTONIN; SULFOTRANSFERASE; UNCLASSIFIED DRUG; WATER;

ARTICLE; BINDING AFFINITY; BINDING SITE; CATALYSIS; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; CRYSTALLIZATION; CYTOSOL; ENZYME ANALYSIS; ENZYME BINDING; ENZYME PURIFICATION; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; METABOLITE; MOLECULAR CLONING; MOUSE; NONHUMAN; PRIORITY JOURNAL; SULFONATION;

ANIMALS; CRYSTALLOGRAPHY, X-RAY; CYTOSOL; MICE; PROTEIN CONFORMATION; SUBSTRATE SPECIFICITY; SULFOTRANSFERASES;

EID: 58149468347     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2008.12.013     Document Type: Article

References (19)

1. Coughtrie M.W., Sharp S., Maxwell K., and Innes N.P. Biology, function of the reversible sulfation pathway catalysed by human sulfotransferases, sulfatases. Chem. Biol. Interact. 109 (1998) 3-27
2. Falany C.N. Enzymology of human cytosolic sulfotransferases. FASEB J. 11 (1997) 206-216
3. Blanchard R.L., Freimuth R.R., Buck J., Weinshilboum R.M., and Coughtrie M.W. A proposed nomenclature system for the cytosolic sulfotransferase (SULT) superfamily. Pharmacogenetics 14 (2004) 199-211
4. Sakakibara Y., Yanagisawa K., Takami Y., Nakayama T., Suiko M., and Liu M.C. Molecular cloning, expression, and functional characterization of novel mouse sulfotransferases. Biochem. Biophys. Res. Commun. 247 (1998) 681-686
5. Tsoi C., Falany C.N., Morgenstern R., and Swedmark S. Identification of a new subfamily of sulphotransferases: Cloning and characterization of canine SULT1D1. Biochem. J. 356 (2001) 891-897
6. Meinl W., and Glatt H. Structure, localization of the human SULT1B1 gene: neighborhood to SULT1E1 and a SULT1D pseudogene. Biochem. Biophys. Res. Commun. 288 (2001) 855-862
7. Alnouti Y., and Klaassen C.D. Tissue distribution, ontogeny of sulfotransferase enzymes in mice. Toxicol. Sci. 93 (2006) 242-255
8. Shimada M., Terazawa R., Kamiyama Y., Honma W., Nagata K., and Yamazoe Y. Unique properties of a renal sulfotransferase, St1d1, in dopamine metabolism. J. Pharmacol. Exp. Ther. 310 (2004) 808-814
9. van den Bosch H.M., Bunger M., de Groot P.J., van der Meijde J., Hooiveld G.J., and Muller M. Gene expression of transporters and phase I/II metabolic enzymes in murine small intestine during fasting. BMC Genomics 8 (2007) 267
10. Liu M.C., Sakakibara Y., and Liu C.C. Bacterial expression, purification, and characterization of a novel mouse sulfotransferase that catalyzes the sulfation of eicosanoids. Biochem. Biophys. Res. Commun. 254 (1999) 65-69
11. Teramoto T., Sakakibara Y., Inada K., Kurogi K., Liu M.C., Suiko M., Kimura M., and Kakuta Y. Crystal structure of mSULT1D1, a mouse catecholamine sulfotransferase. FEBS Lett. 582 (2008) 3909-3914
12. Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
13. Vagin A., and Teplyakov A. An approach to multi-copy search in molecular replacement. Acta Crystallogr. D Biol. Crystallogr. 56 (2000) 1622-1624
14. Murshudov G.N., Vagin A.A., and Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D Biol. Crystallogr. 53 (1997) 240-255
15. Emsley P., and Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D Biol. Crystallogr. 60 (2004) 2126-2132
16. Vaguine A.A., Richelle J., and Wodak S.J. SFCHECK: a unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model. Acta Crystallogr. D Biol. Crystallogr. 55 (1999) 191-205
17. Kakuta Y., Pedersen L.G., Carter C.W., Negishi M., and Pedersen L.C. Crystal structure of estrogen sulphotransferase. Nat. Struct. Biol. 4 (1997) 904-908
18. Gamage N.U., Duggleby R.G., Barnett A.C., Tresillian M., Latham C.F., Liyou N.E., McManus M.E., and Martin J.L. Structure of a human carcinogen-converting enzyme, SULT1A1. structural and kinetic implications of substrate inhibition. J. Biol. Chem. 278 (2003) 7655-7662
19. Gamage N.U., Tsvetanov S., Duggleby R.G., McManus M.E., and Martin J.L. The structure of human, SULT1A1 crystallized with estradiol: an insight into active site plasticity and substrate inhibition with multi-ring substrates. J. Biol. Chem. 280 (2005) 41482-41486