SULT1E1
| SULT1E1 | |||
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| Location (UCSC) | Chr 4: 69.84 – 69.86 Mb | Chr 5: 87.72 – 87.74 Mb | |||||||
| PubMed search | [3] | [4] | |||||||
| View/Edit Human | View/Edit Mouse |
Estrogen sulfotransferase is an enzyme that in humans is encoded by the SULT1E1 gene.[5][6]
Sulfotransferase enzymes catalyze the sulfate conjugation of many hormones, neurotransmitters, drugs, and xenobiotic compounds. These cytosolic enzymes are different in their tissue distributions and substrate specificities. The gene structure (number and length of exons) is similar among family members. This gene encodes a protein that transfers a sulfo moiety to and from estrone, which may control levels of estrogen receptors.[6]
See also
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000109193 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000029272 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- PMID 7961757.
- ^ a b "Entrez Gene: SULT1E1 sulfotransferase family 1E, estrogen-preferring, member 1".
Further reading
- Weinshilboum RM, Otterness DM, Aksoy IA, et al. (1997). "Sulfation and sulfotransferases 1: Sulfotransferase molecular biology: cDNAs and genes". FASEB J. 11 (1): 3–14. S2CID 12532583.
- Glatt H, Engelke CE, Pabel U, et al. (2000). "Sulfotransferases: genetics and role in toxicology". Toxicol. Lett. 112–113: 341–8. PMID 10720750.
- Glatt H (2001). "Sulfotransferases in the bioactivation of xenobiotics". Chem. Biol. Interact. 129 (1–2): 141–70. PMID 11154739.
- Glatt H, Boeing H, Engelke CE, et al. (2001). "Human cytosolic sulphotransferases: genetics, characteristics, toxicological aspects". Mutat. Res. 482 (1–2): 27–40. PMID 11535246.
- Falany CN, Krasnykh V, Falany JL (1995). "Bacterial expression and characterization of a cDNA for human liver estrogen sulfotransferase". J. Steroid Biochem. Mol. Biol. 52 (6): 529–39. S2CID 1341801.
- Aksoy IA, Wood TC, Weinshilboum R (1994). "Human liver estrogen sulfotransferase: identification by cDNA cloning and expression". Biochem. Biophys. Res. Commun. 200 (3): 1621–9. PMID 8185618.
- Her C, Aksoy IA, Kimura S, et al. (1996). "Human estrogen sulfotransferase gene (STE): cloning, structure, and chromosomal localization". Genomics. 29 (1): 16–23. PMID 8530066.
- Falany JL, Falany CN (1996). "Expression of cytosolic sulfotransferases in normal mammary epithelial cells and breast cancer cell lines". Cancer Res. 56 (7): 1551–5. PMID 8603401.
- Her C, Szumlanski C, Aksoy IA, Weinshilboum RM (1997). "Human jejunal estrogen sulfotransferase and dehydroepiandrosterone sulfotransferase: immunochemical characterization of individual variation". Drug Metab. Dispos. 24 (12): 1328–35. PMID 8971138.
- Song WC, Qian Y, Sun X, Negishi M (1997). "Cellular localization and regulation of expression of testicular estrogen sulfotransferase". Endocrinology. 138 (11): 5006–12. PMID 9348232.
- Rubin GL, Harrold AJ, Mills JA, et al. (1999). "Regulation of sulphotransferase expression in the endometrium during the menstrual cycle, by oral contraceptives and during early pregnancy". Mol. Hum. Reprod. 5 (11): 995–1002. PMID 10541560.
- Meinl W, Glatt H (2001). "Structure and localization of the human SULT1B1 gene: neighborhood to SULT1E1 and a SULT1D pseudogene". Biochem. Biophys. Res. Commun. 288 (4): 855–62. PMID 11688987.
- Pedersen LC, Petrotchenko E, Shevtsov S, Negishi M (2002). "Crystal structure of the human estrogen sulfotransferase-PAPS complex: evidence for catalytic role of Ser137 in the sulfuryl transfer reaction". J. Biol. Chem. 277 (20): 17928–32. PMID 11884392.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. PMID 12477932.
- Shevtsov S, Petrotchenko EV, Pedersen LC, Negishi M (2003). "Crystallographic analysis of a hydroxylated polychlorinated biphenyl (OH-PCB) bound to the catalytic estrogen binding site of human estrogen sulfotransferase". Environ. Health Perspect. 111 (7): 884–8. PMID 12782487.
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