From sequence and structure of sulfotransferases and dihydropyrimidinases to an understanding of their mechanisms of action and function

Bibliography

• Mulder GJ, Jakoby WB. Conjugation reactions in drug metabolism. Taylor and Francis, Ltd.; 1990
   Google Scholar
• Zimniak P. Detoxification reactions: relevance to aging. Ageing Res Rev 2008;7:281-300
   PubMed Web of Science ®Google Scholar
• Guengerich FP. Cytochrome P450 and chemical toxicology. Chem Res Toxicol 2008;21:70-83
   PubMed Web of Science ®Google Scholar
• Iyanagi T. Molecular mechanism of phase I and phase II drug-metabolizing enzymes: implications for detoxification. Int Rev Cytol 2007;260:35-112
   PubMed Web of Science ®Google Scholar
• International Human Genome Sequencing Consortium. Finishing the euchromatic sequence of the human genome. Nature 2004;431:931-45
   PubMed Web of Science ®Google Scholar
• Waterston RH, Lander ES, Sulston JE. More on the sequencing of the human genome. Proc Natl Acad Sci USA 2003;100:3022-4
   PubMed Web of Science ®Google Scholar
• Chandonia JM, Brenner SE. The impact of structural genomics: expectations and outcomes. Science 2006;311:347-51
   PubMed Web of Science ®Google Scholar
• Marsden RL, Lewis TA, Orengo CA. Towards a comprehensive structural coverage of completed genomes: a structural genomics viewpoint. BMC Bioinformatics 2007;8:86
   PubMedGoogle Scholar
• Nowell S, Falany CN. Pharmacogenetics of human cytosolic sulfotransferases. Oncogene 2006;5:1673-8
   Google Scholar
• Rath VL, Verdugo D, Hemmerich S. Sulfotransferase structural biology and inhibitor discovery. Drug Discov Today 2004;9:1003-11
   PubMed Web of Science ®Google Scholar
• Hemmerich S, Verdugo D, Rath VL. Strategies for drug discovery by targeting sulfation pathways. Drug Discov Today 2004;9:967-75
   PubMed Web of Science ®Google Scholar
• Kauffman FC. Sulfonation in pharmacology and toxicology. Drug Metab Rev 2004;36:823-43
   PubMed Web of Science ®Google Scholar
• Pasqualini JR. The selective estrogen enzyme modulators in breast cancer: a review. Biochim Biophys Acta 2004;1654:123-43
   PubMed Web of Science ®Google Scholar
• Falany C, Roth JA. In: Human drug metabolism: from molecular biology to man. CRC Press, Inc. Boca Raton, FL; 1993
   Google Scholar
• Weinshilboum R, Otterness D. In: Conjugation-deconjugation reactions in drug metabolism and toxicity. Springer-Verlag, Berlin, 1994
   Google Scholar
• DeBaun JR, Miller EC, Miller JA. N-hydroxy-2-acetylaminofluorene sulfotransferase: its probable role in carcinogenesis and in protein-(methion-S-yl) binding in rat liver. Cancer Res 1970;30:577-95
   PubMed Web of Science ®Google Scholar
• Glatt H. Sulfation and sulfotransferases 4: bioactivation of mutagens via sulfation. FASEB J 1997;11:314-21
   PubMed Web of Science ®Google Scholar
• Falany CN. Sulfation and sulfotransferases. Introduction: changing view of sulfation and the cytosolic sulfotransferases. FASEB J 1997;11:1-2
   PubMed Web of Science ®Google Scholar
• Falany CN. Enzymology of human cytosolic sulfotransferases. FASEB J 1997;11:206-16
   PubMed Web of Science ®Google Scholar
• Sharma V, Duffel MW. A comparative molecular field analysis-based approach to prediction of sulfotransferase catalytic specificity. Methods Enzymol 2005;400:249-63
   PubMed Web of Science ®Google Scholar
• Gamage NU, Tsvetanov S, Duggleby RG, The structure of human SULT1A1 crystallized with estradiol. An insight into active site plasticity and substrate inhibition with multi-ring substrates. J Biol Chem 2005;280:41482-6
   PubMed Web of Science ®Google Scholar
• Gamage NU, Tsvetanov S, Duggleby RG, Structure of a human carcinogen-converting enzyme, SULT1A1. Structural and kinetic implications of substrate inhibition. J Biol Chem 2003;278:7655-62
   PubMed Web of Science ®Google Scholar
• Rehse PH, Zhou M, Lin SX. Crystal structure of human dehydroepiandrosterone sulphotransferase in complex with substrate. Biochem J 2002;364:165-71
   PubMed Web of Science ®Google Scholar
• Wallach DP, Grisolia S. The purification and properties of hydropyrimidine hydrase. J Biol Chem 1957;226:277-88
   PubMed Web of Science ®Google Scholar
• Cai Y, Trodler P, Jiang S, Isolation and molecular characterization of a novel D-hydantoinase from Jannaschia sp. CCS1. FEBS J 2009;276:3575-88
   PubMed Web of Science ®Google Scholar
• Yang YS, Ramaswamy S, Jakoby WB. Rat liver imidase. J Biol Chem 1993;268:10870-5
   PubMed Web of Science ®Google Scholar
• Abendroth J, Niefind K, Schomburg D. X-ray Structure of a Dihydropyrimidinase from Thermus sp. at 1.3Å Resolution. J Mol Biol 2002;320:143-56
   PubMed Web of Science ®Google Scholar
• Lohkamp B, Anderson B, Piskur J, Dobritzsch D. The crystal structures of dihydropyrimidinases reaffirm the close relationship between cyclic amidohydrolases and explain their substrate specificity. J Biol Chem 2006;281:13762-76
   PubMed Web of Science ®Google Scholar
• Welin M, Karlberg T, Andersson J, The crystal structure of human dihydropyrimidinase. Published on PDB 2008
   Google Scholar
• Martínez-Rodríguez S, Martínez-Gómez AI, Clemente-Jiménez JM, Structure of dihydropyrimidinase from Sinorhizobium meliloti CECT4114: new features in an amidohydrolase family member. J Struct Biol 2009; doi: 10.1016/j.jsb.2009.10.013
   Google Scholar
• Soong CL, Ogawa J, Honda M, Shimizu S. Cyclic-imide-hydrolyzing activity of D-hydantoinase from Blastobacter sp. strain A17p-4. Appl Environ Microbiol 1999;65:1459-62
   PubMed Web of Science ®Google Scholar
• Seibert CM, Raushel FM. Structural and catalytic diversity within the amidohydrolase superfamily. Biochemistry 2005;44:6383-91
   PubMed Web of Science ®Google Scholar
• Gojkovic Z, Jahnke K, Schnackerz KD, Piskur J. PYD2 encodes 5,6-dihydropyrimidine aminohydrolase which participates in a novel fungal catabolic pathway. J Mol Biol 2000;295:1073-87
   PubMed Web of Science ®Google Scholar
• Holm L, Sander C. An evolutionary treasure: unification of a broad set of amidohydrolases related to urease. Proteins 1997;28:72-82
   PubMed Web of Science ®Google Scholar
• May O, Habenicht A, Mattes R, Molecular evolution of hydantoinases. Biol Chem 1998;379:743-7
   PubMed Web of Science ®Google Scholar
• Goshima Y, Nakamura F, Strittmatter P, Strittmatter SM. Collapsin-induced growth cone collapse mediated by an intracellular protein related to unc-33. Nature 1995;376:509-14
   PubMed Web of Science ®Google Scholar
• Thoden JB, Phillips GN Jr, Tamiko MN, Molecular structure of dihydroorotase: a paradigm for catalysis through the use of a binuclear metal center. Biochemistry 2001;40:6989-99
   PubMed Web of Science ®Google Scholar
• Jabri E, Carr MB, Hausinger RP, Karplus PA. The crystal structure of urease from Klebsiella aerogenes. Science 1995;268:998-1004
   PubMed Web of Science ®Google Scholar
• Deo RC, Schmidt EF, Elhabazi A, Structural bases for CRMP function in plexin-dependent semaphorin3A signaling. EMBO J 2004;23:9-22
   PubMed Web of Science ®Google Scholar
• Benning MM, Kuo JM, Raushel FM, Holden HM. Three-dimensional structure of phosphotriesterase: an enzyme capable of detoxifying organophosphate nerve agents. Biochemistry 1994;33:15001-7
   PubMed Web of Science ®Google Scholar
• Huang CY, Yang YS. The role of metal on imide hydrolysis: metal content and pH profiles of metal ion-replaced mammalian imidase. Biochem Biophys Res Commun 2002;297:1027-32
   PubMed Web of Science ®Google Scholar
• Huang CY, Hsu CC, Chen MC, Yang YS. Effect of metal binding and posttranslational lysine carboxylation on the activity of recombinant hydantoinase. J Biol Inorg Chem 2009;14:111-21
   PubMed Web of Science ®Google Scholar
• Duffel MW, Jakoby WB. On the mechanism of aryl sulfotransferase. J Biol Chem 1981;256:11123-7
   PubMed Web of Science ®Google Scholar
• Zhang H, Varlamova O, Vargas FM, Sulfuryl transfer: the catalytic mechanism of human estrogen sulfotransferase. J Biol Chem 1998;273:10888-92
   PubMed Web of Science ®Google Scholar
• Chang HJ, Shi R, Rehse P, Lin SX. Identifying androsterone (ADT) as a cognate substrate for human dehydroepiandrosterone sulfotransferase (DHEA-ST) important for steroid homeostasis: structure of the enzyme-ADT complex. J Biol Chem 2004;279:2689-96
   PubMed Web of Science ®Google Scholar
• Barnett AC, Tsvetanov S, Gamage N, Active site mutations and substrate inhibition in human sulfotransferase 1A1 and 1A3. J Biol Chem 2004;279:18799-805
   PubMed Web of Science ®Google Scholar
• Lu LY, Hsieh YC, Liu MY, Identification and characterization of two amino acids critical for the substrate inhibition of human dehydroepiandrosterone sulfotransferase (SULT2A1). Mol Pharmacol 2008;73:660-8
   PubMed Web of Science ®Google Scholar
• Pedersen LC, Petrotchenko EV, Negishi M. Crystal structure of SULT2A3, human hydroxysteroid sulfotransferase. FEBS Lett 2000;475:61-4
   PubMed Web of Science ®Google Scholar
• Kuchel OG, Kuchel GA. Peripheral dopamine in pathophysiology of hypertension. Interaction with aging and lifestyle. Hypertension 1991;18:709-21
   PubMed Web of Science ®Google Scholar
• Goldstein DS, Swoboda KJ, Miles JM, Sources and physiological significance of plasma dopamine sulfate. J Clin Endocrinol Metab 1999;84:2523-31
   PubMed Web of Science ®Google Scholar
• Sakakibara Y, Katafuchi J, Takami Y, Manganese-dependent Dopa/tyrosine sulfation in HepG2 human hepatoma cells: novel dopa/tyrosine sulfotransferase activities associated with the human monoamine-form phenol sulfotransferase. Biochim Biophys Acta 1997;1355:102-6
   PubMed Web of Science ®Google Scholar
• Pai TG, Ohkimoto K, Sakakibara Y, Manganese stimulation and stereospecificity of the Dopa (3,4-dihydroxyphenylalanine)/tyrosine-sulfating activity of human monoamine-form phenol sulfotransferase. Kinetic studies of the mechanism using wild-type and mutant enzymes. J Biol Chem 2002;277:43813-20
   PubMed Web of Science ®Google Scholar
• Lu JH, Li HT, Liu MC, Crystal structure of human sulfotransferase SULT1A3 in complex with dopamine and 3′-phosphoadenosine 5′-phosphate. Biochem Biophys Res Commun 2005;335:417-23
   PubMed Web of Science ®Google Scholar
• Lindsay J, Wang LL, Li Y, Zhou SF. Structure, function and polymorphism of human cytosolic sulfotransferases. Curr Drug Metab 2008;9:99-105
   PubMed Web of Science ®Google Scholar
• Hebbring SJ, Moyer AM, Weinshilboum RM. Sulfotransferase gene copy number variation: pharmacogenetics and function. Cytogenet Genome Res 2008;123:205-10
   PubMed Web of Science ®Google Scholar
• Hempel N, Gamage N, Martin JL, McManus ME. Human cytosolic sulfotransferase SULT1A1. Int J Biochem Cell Biol 2007;39:685-9
   PubMed Web of Science ®Google Scholar
• Hempel N, Barnett A, Gamage N, Human SULT1A sulfotransferases, in Human cytosolic sulfotransferases. CRC Press, London; 2005
   Google Scholar
• Hildebrandt MA, Salavaggione OE, Martin YN, Human SULT1A3 pharmacogenetics: gene duplication and functional genomic studies. Biochem Biophys Res Commun 2004;321:870-8
   PubMed Web of Science ®Google Scholar
• Blanchard RL, Freimuth RR, Buck J, A proposed nomenclature system for the cytosolic sulfotransferase (SULT) superfamily. Pharmacogenetics 2004;14:199-211
   PubMedGoogle Scholar
• Hirata H, Hinoda Y, Okayama N, CYP1A1, SULT1A1, and SULT1E1 polymorphisms are risk factors for endometrial cancer susceptibility. Cancer 2008;112:1964-73
   PubMed Web of Science ®Google Scholar
• Nagar S, Walther S, Blanchard RL. Sulfotransferase (SULT) 1A1 polymorphic variants *1, *2, and *3 are associated with altered enzymatic activity, cellular phenotype, and protein degradation. Mol Pharmacol 2006;69:2084-92
   PubMed Web of Science ®Google Scholar
• van Kuilenburg ABP, Meinsma JR, Zonnenberg BA, Dihydropyrimidinase deficiency and severe 5-fluorouracil toxicity. Clin Cancer Res 2003;9:4363-7
   PubMed Web of Science ®Google Scholar
• van Kuilenburg ABP, Meijer J, Dobritzsch D, Clinical, biochemical and genetic findings in two siblings with a dihydropyrimidinase deficiency. Mol Genet Metab 2007;91:157-64
   PubMed Web of Science ®Google Scholar
• van Kuilenburg ABP. Dihydropyrimidine dehydrogenase and the efficacy and toxicity of 5-fluorouracil. Eur J Cancer 2004;40:939-50
   PubMed Web of Science ®Google Scholar
• Chapman E, Best MD, Hanson SR, Wong CH. Sulfotransferases: structure, mechanism, biological activity, inhibition, and synthetic utility. Angew Chem Int Ed Engl 2004;43:3526-48
   PubMed Web of Science ®Google Scholar
• Strott CA. Sulfonation and molecular action. Endocr Rev 2002;23:703-32
   PubMed Web of Science ®Google Scholar
• Sakakibara Y, Takami Y, Nakayama T, Localization and functional analysis of the substrate specificity/catalytic domains of human M-form and P-form phenol sulfotransferases. J Biol Chem 1998;273:6242-7
   PubMed Web of Science ®Google Scholar
• Liu MC, Suiko M, Sakakibara Y. Mutational analysis of the substrate binding/catalytic domains of human M form and P form phenol sulfotransferases. J Biol Chem 2000;275:13460-4
   PubMed Web of Science ®Google Scholar
• Brooks SC, Rozhin J, Pack BA, Role of sulfate conjugation in estrogen metabolism and activity. J Toxicol Environ Health 1978;4:283-300
   PubMed Web of Science ®Google Scholar
• Chatterjee B, Song CS, Kim JM, Roy AK. Androgen and estrogen sulfotransferases of the rat liver: physiological function, molecular cloning, and in vitro expression. Chem Biol Interact 1994;92:273-9
   PubMed Web of Science ®Google Scholar
• Petrotchenko EV, Doerflein ME, Kakuta Y, Substrate gating confers steroid specificity to estrogen sulfotransferase. J Biol Chem 1999;274:30019-22
   PubMed Web of Science ®Google Scholar
• Petrotchenko EV, Pedersen LC, Borchers CH, The dimerization motif of cytosolic sulfotransferases. FEBS Lett 2001;490:39-43
   PubMed Web of Science ®Google Scholar
• Kiehlbauch CC, Lam YF, Ringer DP. Homodimeric and heterodimeric aryl sulfotransferases catalyze the sulfuric acid esterification of N-hydroxy-2-acetylaminofluorene. J Biol Chem 1995;270:18941-7
   PubMed Web of Science ®Google Scholar
• Lu LY, Chiang HP, Chen WT, Yang YS. Dimerization is responsible for the structural stability of human sulfotransferase 1A1. Drug Metab Dispos 2009;37:1083-8
   PubMed Web of Science ®Google Scholar
• Cheon YH, Kim HS, Han KH, Crystal structure of D-hydantoinase from Bacillus stearothermophilus: insight into the stereochemistry of enantioselectivity. Biochemistry 2002;41:9410-7
   PubMed Web of Science ®Google Scholar
• Xu Z, Liu YQ, Yang YL, Crystal structure of D-hydantoinase from Burkholderia pickettii at a resolution of 2.7 Angstroms: insights into the molecular basis of enzyme thermostability. J Bacteriol 2003;185:4038-49
   PubMed Web of Science ®Google Scholar
• Kim GJ, Kim HS. C-terminal regions of D-hydantoinases are non-essential for catalysis, but affect the oligomeric structure. Biochem Biophys Res Commun 1998;243:96-100
   PubMed Web of Science ®Google Scholar
• Niu L, Zhang X, Shi Y, Yuan J. Subunit dissociation and stability alteration of D-hydantoinase deleted at the terminal amino acid residue. Biotechnol Lett 2007;29:303-8
   PubMed Web of Science ®Google Scholar
• Vakiani E, Luz JG, Buck J. Substrate specificity and kinetic mechanism of the insect sulfotransferase, retinol dehydratase. J Biol Chem 1998;273:35381-7
   PubMed Web of Science ®Google Scholar
• Pakhomova S, Kobayashi M, Buck J, Newcomer ME. A helical lid converts a sulfotransferase to a dehydratase. Nat Struct Biol 2001;8:447-51
   PubMedGoogle Scholar
• Hsiao YS, Yang YS. A single mutation converts the nucleotide specificity of phenol sulfotransferase from PAP to AMP. Biochemistry 2002;41:12959-66
   PubMed Web of Science ®Google Scholar
• Cheon YH, Park HS, Kim JH, Manipulation of the active site loops of D-Hydantoinase, a (alpha/beta)8-barrel protein for modulation of the substrate specificity. Biochemistry 2004;43:7413-20
   PubMed Web of Science ®Google Scholar