SULT1A3

From Wikipedia, the free encyclopedia


Sulfotransferase family, cytosolic, 1A, phenol-preferring, member 3
PDB rendering based on 1cjm.
Available structures: 1cjm, 1ls6, 1z28, 1z29, 2a3r, 2d06
Identifiers
Symbol(s) SULT1A3; HAST; HAST3; M-PST; MGC117469; ST1A5; STM; SULT1A4; TL-PST
External IDs OMIM: 600641 HomoloGene: 81075
Orthologs
Human Mouse
Entrez 6818 n/a


Refseq XM_001126153 (mRNA)
XP_001126153 (protein)		 n/a (mRNA)
n/a (protein)
Pubmed search [1] n/a

Sulfotransferase family, cytosolic, 1A, phenol-preferring, member 3, also known as SULT1A3, is a human gene.[1]

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 phenol sulfotransferase with thermolabile enzyme activity. Four sulfotransferase genes are located on the p arm of chromosome 16; this gene and SULT1A4 arose from a segmental duplication. This gene is the most centromeric of the four sulfotransferase genes. Exons of this gene overlap with exons of a gene that encodes a protein containing GIY-YIG domains (GIYD1). Three alternatively spliced variants that encode the same protein have been described.[1]

[edit] References

  1. ^ a b Entrez Gene: SULT1A3 sulfotransferase family, cytosolic, 1A, phenol-preferring, member 3.

[edit] 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. PMID 9034160. 
  • 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. 
  • Aksoy IA, Weinshilboum RM (1995). "Human thermolabile phenol sulfotransferase gene (STM): molecular cloning and structural characterization.". Biochem. Biophys. Res. Commun. 208 (2): 786–95. doi:10.1006/bbrc.1995.1406. PMID 7695637. 
  • Jones AL, Hagen M, Coughtrie MW, et al. (1995). "Human platelet phenolsulfotransferases: cDNA cloning, stable expression in V79 cells and identification of a novel allelic variant of the phenol-sulfating form.". Biochem. Biophys. Res. Commun. 208 (2): 855–62. doi:10.1006/bbrc.1995.1414. PMID 7695643. 
  • Dooley TP, Probst P, Munroe PB, et al. (1995). "Genomic organization and DNA sequence of the human catecholamine-sulfating phenol sulfotransferase gene (STM).". Biochem. Biophys. Res. Commun. 205 (2): 1325–32. doi:10.1006/bbrc.1994.2810. PMID 7802665. 
  • Aksoy IA, Callen DF, Apostolou S, et al. (1995). "Thermolabile phenol sulfotransferase gene (STM): localization to human chromosome 16p11.2.". Genomics 23 (1): 275–7. doi:10.1006/geno.1994.1494. PMID 7829089. 
  • Bernier F, Leblanc G, Labrie F, Luu-The V (1994). "Structure of human estrogen and aryl sulfotransferase gene. Two mRNA species issued from a single gene.". J. Biol. Chem. 269 (45): 28200–5. PMID 7961757. 
  • Veronese ME, Burgess W, Zhu X, McManus ME (1994). "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 ( Pt 2): 497–502. PMID 8093002. 
  • Wood TC, Aksoy IA, Aksoy S, Weinshilboum RM (1994). "Human liver thermolabile phenol sulfotransferase: cDNA cloning, expression and characterization.". Biochem. Biophys. Res. Commun. 198 (3): 1119–27. doi:10.1006/bbrc.1994.1159. PMID 8117269. 
  • Bernier F, Lopez Solache I, Labrie F, Luu-The V (1994). "Cloning and expression of cDNA encoding human placental estrogen sulfotransferase.". Mol. Cell. Endocrinol. 99 (1): R11–5. PMID 8187949. 
  • Zhu X, Veronese ME, Bernard CC, et al. (1993). "Identification of two human brain aryl sulfotransferase cDNAs.". Biochem. Biophys. Res. Commun. 195 (1): 120–7. PMID 8363592. 
  • Her C, Raftogianis R, Weinshilboum RM (1996). "Human phenol sulfotransferase STP2 gene: molecular cloning, structural characterization, and chromosomal localization.". Genomics 33 (3): 409–20. doi:10.1006/geno.1996.0216. PMID 8661000. 
  • Dooley TP, Huang Z (1996). "Genomic organization and DNA sequences of two human phenol sulfotransferase genes (STP1 and STP2) on the short arm of chromosome 16.". Biochem. Biophys. Res. Commun. 228 (1): 134–40. doi:10.1006/bbrc.1996.1628. PMID 8912648. 
  • Dajani R, Sharp S, Graham S, et al. (1999). "Kinetic properties of human dopamine sulfotransferase (SULT1A3) expressed in prokaryotic and eukaryotic systems: comparison with the recombinant enzyme purified from Escherichia coli.". Protein Expr. Purif. 16 (1): 11–8. doi:10.1006/prep.1999.1030. PMID 10336855. 
  • Bidwell LM, McManus ME, Gaedigk A, et al. (1999). "Crystal structure of human catecholamine sulfotransferase.". J. Mol. Biol. 293 (3): 521–30. doi:10.1006/jmbi.1999.3153. PMID 10543947. 
  • Dajani R, Cleasby A, Neu M, et al. (2000). "X-ray crystal structure of human dopamine sulfotransferase, SULT1A3. Molecular modeling and quantitative structure-activity relationship analysis demonstrate a molecular basis for sulfotransferase substrate specificity.". J. Biol. Chem. 274 (53): 37862–8. PMID 10608851. 
  • Harris RM, Waring RH, Kirk CJ, Hughes PJ (2000). "Sulfation of "estrogenic" alkylphenols and 17beta-estradiol by human platelet phenol sulfotransferases.". J. Biol. Chem. 275 (1): 159–66. PMID 10617600. 
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