Bile salt sulfotransferase

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Sulfotransferase family, cytosolic, 2A, dehydroepiandrosterone (DHEA)-preferring, member 1
Protein SULT2A1 PDB 1efh.png
PDB rendering based on 1efh.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols SULT2A1 ; DHEA-ST; DHEAS; HST; ST2; ST2A1; ST2A3; STD; hSTa
External IDs OMIM125263 MGI3690091 HomoloGene37741 ChEMBL: 2077 GeneCards: SULT2A1 Gene
EC number 2.8.2.14
RNA expression pattern
PBB GE SULT2A1 206292 s at tn.png
PBB GE SULT2A1 206293 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 6822 20859
Ensembl ENSG00000105398 ENSMUSG00000078798
UniProt Q06520 P52843
RefSeq (mRNA) NM_003167 NM_001111296
RefSeq (protein) NP_003158 NP_001104766
Location (UCSC) Chr 19:
48.37 – 48.39 Mb
Chr 7:
13.8 – 13.84 Mb
PubMed search [1] [2]

Bile salt sulfotransferase also known as hydroxysteroid sulfotransferase (HST) or sulfotransferase 2A1 (ST2A1) is an enzyme that in humans is encoded by the SULT2A1 gene.[1][2][3]

Function[edit]

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 is primarily expressed in liver and adrenal tissues where the encoded protein sulfates steroids and bile acids.[1]

See also[edit]

References[edit]

  1. ^ a b "Entrez Gene: SULT2A1 sulfotransferase family, cytosolic, 2A, dehydroepiandrosterone (DHEA)-preferring, member 1". 
  2. ^ Otterness DM, Wieben ED, Wood TC, Watson WG, Madden BJ, McCormick DJ, Weinshilboum RM (May 1992). "Human liver dehydroepiandrosterone sulfotransferase: molecular cloning and expression of cDNA". Mol. Pharmacol. 41 (5): 865–72. PMID 1588921. 
  3. ^ Otterness DM, Mohrenweiser HW, Brandriff BF, Weinshilboum RM (1995). "Dehydroepiandrosterone sulfotransferase gene (STD): localization to human chromosome band 19q13.3". Cytogenet. Cell Genet. 70 (1-2): 45–7. doi:10.1159/000133988. PMID 7736787. 

Further reading[edit]

  • 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. PMID 9034160. 
  • Glatt H, Engelke CE, Pabel U, et al. (2000). "Sulfotransferases: genetics and role in toxicology.". Toxicol. Lett. 112-113: 341–8. doi:10.1016/S0378-4274(99)00214-3. PMID 10720750. 
  • Glatt H, Boeing H, Engelke CE, et al. (2001). "Human cytosolic sulphotransferases: genetics, characteristics, toxicological aspects.". Mutat. Res. 482 (1-2): 27–40. doi:10.1016/S0027-5107(01)00207-X. PMID 11535246. 
  • Kong AN, Yang L, Ma M, et al. (1992). "Molecular cloning of the alcohol/hydroxysteroid form (hSTa) of sulfotransferase from human liver.". Biochem. Biophys. Res. Commun. 187 (1): 448–54. doi:10.1016/S0006-291X(05)81514-1. PMID 1520333. 
  • Comer KA, Falany CN (1992). "Immunological characterization of dehydroepiandrosterone sulfotransferase from human liver and adrenal.". Mol. Pharmacol. 41 (4): 645–51. PMID 1569919. 
  • Otterness DM, Wieben ED, Wood TC, et al. (1992). "Human liver dehydroepiandrosterone sulfotransferase: molecular cloning and expression of cDNA.". Mol. Pharmacol. 41 (5): 865–72. PMID 1588921. 
  • Radominska A, Comer KA, Zimniak P, et al. (1991). "Human liver steroid sulphotransferase sulphates bile acids.". Biochem. J. 272 (3): 597–604. PMC 1149750. PMID 2268288. 
  • Forbes KJ, Hagen M, Glatt H, et al. (1995). "Human fetal adrenal hydroxysteroid sulphotransferase: cDNA cloning, stable expression in V79 cells and functional characterisation of the expressed enzyme.". Mol. Cell. Endocrinol. 112 (1): 53–60. doi:10.1016/0303-7207(95)03585-U. PMID 7589785. 
  • Luu-The V, Dufort I, Paquet N, et al. (1995). "Structural characterization and expression of the human dehydroepiandrosterone sulfotransferase gene.". DNA Cell Biol. 14 (6): 511–8. doi:10.1089/dna.1995.14.511. PMID 7598806. 
  • Comer KA, Falany JL, Falany CN (1993). "Cloning and expression of human liver dehydroepiandrosterone sulphotransferase.". Biochem. J. 289 (1): 233–40. PMC 1132155. PMID 7678732. 
  • Otterness DM, Her C, Aksoy S, et al. (1995). "Human dehydroepiandrosterone sulfotransferase gene: molecular cloning and structural characterization.". DNA Cell Biol. 14 (4): 331–41. doi:10.1089/dna.1995.14.331. PMID 7710689. 
  • Otterness DM, Mohrenweiser HW, Brandriff BF, Weinshilboum RM (1995). "Dehydroepiandrosterone sulfotransferase gene (STD): localization to human chromosome band 19q13.3.". Cytogenet. Cell Genet. 70 (1-2): 45–7. doi:10.1159/000133988. PMID 7736787. 
  • Falany CN, Wheeler J, Oh TS, Falany JL (1994). "Steroid sulfation by expressed human cytosolic sulfotransferases.". J. Steroid Biochem. Mol. Biol. 48 (4): 369–75. doi:10.1016/0960-0760(94)90077-9. PMID 8142314. 
  • Barker EV, Hume R, Hallas A, Coughtrie WH (1994). "Dehydroepiandrosterone sulfotransferase in the developing human fetus: quantitative biochemical and immunological characterization of the hepatic, renal, and adrenal enzymes.". Endocrinology 134 (2): 982–9. doi:10.1210/en.134.2.982. PMID 8299591. 
  • Durocher F, Morissette J, Dufort I, et al. (1996). "Genetic linkage mapping of the dehydroepiandrosterone sulfotransferase (STD) gene on the chromosome 19q13.3 region.". Genomics 29 (3): 781–3. doi:10.1006/geno.1995.9935. PMID 8575776. 
  • 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. doi:10.1093/molehr/5.11.995. PMID 10541560. 
  • Tashiro A, Sasano H, Nishikawa T, et al. (2000). "Expression and activity of dehydroepiandrosterone sulfotransferase in human gastric mucosa.". J. Steroid Biochem. Mol. Biol. 72 (3-4): 149–54. doi:10.1016/S0960-0760(00)00020-0. PMID 10775806. 
  • Pedersen LC, Petrotchenko EV, Negishi M (2000). "Crystal structure of SULT2A3, human hydroxysteroid sulfotransferase.". FEBS Lett. 475 (1): 61–4. doi:10.1016/S0014-5793(00)01479-4. PMID 10854859. 

External links[edit]