Sulfotransferase 1A3/1A4 is an
enzyme that in humans is encoded by the SULT1A3gene.[3][4][5]
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.[5]
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.
PMID10720750.
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.
PMID7695643.
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.
PMID7802665.
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.
PMID8912648.
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.
PMID10336855.
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.
PMID10543947.
Sulfotransferase 1A3/1A4 is an
enzyme that in humans is encoded by the SULT1A3gene.[3][4][5]
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.[5]
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.
PMID10720750.
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.
PMID7695643.
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.
PMID7802665.
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.
PMID8912648.
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.
PMID10336855.
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.
PMID10543947.