SULT1C4 | |||||||||||||||||||||||||||||||||||||||||||||||||||
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Aliases | SULT1C4 , SULT1C, SULT1C2, sulfotransferase family 1C member 4 | ||||||||||||||||||||||||||||||||||||||||||||||||||
External IDs | OMIM: 608357 HomoloGene: 41383 GeneCards: SULT1C4 | ||||||||||||||||||||||||||||||||||||||||||||||||||
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Wikidata | |||||||||||||||||||||||||||||||||||||||||||||||||||
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Sulfotransferase 1C4 is an enzyme that in humans is encoded by the SULT1C4 gene. [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 protein that belongs to the SULT1 subfamily, responsible for transferring a sulfo moiety from PAPS to phenol-containing compounds. [5]
Alcohol sulfotransferase is an enzyme that catalyzes the sulfate conjugation of primary and secondary alcohols including many hormones, neurotransmitters, drugs, and xenobiotic compounds.
Estrone sulfotransferase (EST), also known as estrogen sulfotransferase, is an enzyme that catalyzes the transformation of an unconjugated estrogen like estrone into a sulfated estrogen like estrone sulfate. It is a steroid sulfotransferase and belongs to the family of transferases, to be specific, the sulfotransferases, which transfer sulfur-containing groups. This enzyme participates in androgen and estrogen metabolism and sulfur metabolism.
In enzymology, a steroid sulfotransferase is an enzyme that catalyzes the chemical reaction
Sulfotransferase 1A1 is an enzyme that in humans is encoded by the SULT1A1 gene.
Sulfotransferase 1A3/1A4 is an enzyme that in humans is encoded by the SULT1A3 gene.
Estrogen sulfotransferase is an enzyme that in humans is encoded by the SULT1E1 gene.
Sulfotransferase family cytosolic 2B member 1 is an enzyme that in humans is encoded by the SULT2B1 gene.
Sulfotransferase 1A2 is an enzyme that in humans is encoded by the SULT1A2 gene.
Sulfotransferase 1C2 is an enzyme that in humans is encoded by the SULT1C2 gene.
Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthetase 1 is an enzyme that in humans is encoded by the PAPSS1 gene.
Sulfotransferase 4A1 is an enzyme that in humans is encoded by the SULT4A1 gene.
Galactosylceramide sulfotransferase is an enzyme that in humans is encoded by the GAL3ST1 gene.
Sulfotransferase family cytosolic 1B member 1 is an enzyme that in humans is encoded by the SULT1B1 gene.
Carbohydrate sulfotransferase 15 is an enzyme that in humans is encoded by the CHST15 gene. It belongs to the N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase enzyme class.
Galactose-3-O-sulfotransferase 2 is an enzyme that in humans is encoded by the GAL3ST2 gene.
Galactose-3-O-sulfotransferase 4 is an enzyme that in humans is encoded by the GAL3ST4 gene.
Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 3 is an enzyme that in humans is encoded by the NDST3 gene. It catalyses the reaction:
3'-phosphoadenylyl sulfate + α-D-glucosaminyl-[heparan sulfate](n) = adenosine 3',5'-bisphosphate + 2 H+ + N-sulfo-α-D-glucosaminyl-[heparan sulfate](n)
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.
Sulfotransferase 1C3, also known as ST1C3, is an enzyme that in humans is encoded by the SULT1C3 gene.
Phenol sulfur transferase deficiency, in short PST deficiency, is the lack or the reduced activity of the functional enzyme phenol sulfur transferase, which is crucial in the detoxification of mainly phenolic compounds by catalysing the sulfate conjugation of the hydroxyl groups in the toxic phenolic compounds to result in more hydrophilic forms for more efficient excretion. This metabolic disorder was first discovered in the late 1990s by Dr. Rosemary Waring during her researches with autistic children, which also made this deficiency commonly associated to the topics of autism. Mutations in the PST genes account for the genetic causes of the deficiency, of which single nucleotide polymorphism and methylation of promoters are two examples of mutations that respectively cause conformational abnormalities and diminished expressions to the enzyme, resulting in the reduced detoxification of phenolic compounds and regulation of phenolic neurotransmitter. The deficiency may cause symptoms like flushing, tachycardia, and depression, and be a risk factor for disorders like autism, migraine, and cancer, while it also limits the use of phenolic drugs in PST deficient patients. There is currently no drug available for treating PST deficiency.