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Literature summary extracted from

  • Zimmer, B.; Tenbusch, L.; Klymiuk, M.C.; Dezhkam, Y.; Schuler, G.
    Sulfation pathways Expression of SULT2A1, SULT2B1 and HSD3B1 in the porcine testis and epididymis (2018), J. Mol. Endocrinol., 61, M41-M55 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.8.2.2 gene SULT2A1, quantitative real-time RT-PCR enzyme expression analysis Sus scrofa
2.8.2.2 gene SULT2B1, quantitative real-time RT-PCR enzyme expression analysis Sus scrofa

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.8.2.2 cytosol
-
 Sus scrofa 5829
-
2.8.2.2 additional information different from the ileum epithelium where staining is exclusively cytosolic, in the epididymal duct epithelium in addition to cytoplasmic staining in part also nuclear signals are observed. But nuclear staining in the testis and epididymis is considered as an artifact Sus scrofa
-
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.8.2.2 3'-phosphoadenylyl sulfate + cholesterol Sus scrofa
-
 adenosine 3',5'-bisphosphate + cholesterol 3-sulfate
-
 ?
2.8.2.2 3'-phosphoadenylyl sulfate + dehydroepiandrosterone Sus scrofa
-
 adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
 ?
2.8.2.2 3'-phosphoadenylyl sulfate + pregnenolone Sus scrofa
-
 adenosine 3',5'-bisphosphate + pregnenolone 3-sulfate
-
 ?
2.8.2.2 additional information Sus scrofa for human SULT2B1, pregnenolone (P5, isoform 2B1a) and cholesterol (isoform 2B1b) are regarded as preferential steroidal substrates ?
-
-
2.8.2.2 additional information Sus scrofa SULT2A1 exhibits a broad substrate spectrum. In addition to its prototypical substrate dehydroepiandrosterone (DHEA) and other 3beta-hydroxysteroids, it is also capable of sulfonating 3alpha-hydroxysteroids, estrogens and xenobiotics ?
-
-

Organism

EC Number Organism UniProt Comment Textmining
2.8.2.2 Sus scrofa I3LRP8
-
-
2.8.2.2 Sus scrofa Q3S3F7
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.8.2.2 native enzyme from epididymis and testis cytosol by ultracentrifugation and ultrafiltration Sus scrofa

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.8.2.2 epididymis SULT2A1 expression is virtually confined to the body in the epididymis. The enzyme is secreted into the ductal lumen via an apocrine mechanism. In addition to the ductal epithelium, immunostaining is observed in spherical particles situated in the ductal lumen and in vascular endothelial cells of the epididymal connective tissue Sus scrofa
-
2.8.2.2 epididymis SULT2B1 expression is increased significantly along the epididymis, coexpression with HSD3B1. The enzyme is secreted into the ductal lumen via an apocrine mechanism. Immunolocalization study of SULT2B1. SULT2B1-mRNA expression is highest in the distal part of the epididymal tail in muscular cells Sus scrofa
-
2.8.2.2 epithelium
-
 Sus scrofa
-
2.8.2.2 ileum
-
 Sus scrofa
-
2.8.2.2 Leydig cell
-
 Sus scrofa
-
2.8.2.2 liver
-
 Sus scrofa
-
2.8.2.2 additional information SULT2B1 expression is absent or low in the testis. Tissue samples were collected from a total number of ten postpubertal crossbreed boars (nine German Landrace × Pietrain, one Large White) aged between 10 and 16 months. When measuring P5-ST activities in cytosols, conversion rates of the substrate is only marginal in testis, epididymal head and the initial segment of the epididymal body. They increased in the subsequent segments of the epididymal body and are maximal in the epididymal tail. When measuring the sulfonation of pregnenolone (P5) in homogenates prepared from the testis and selected segments (EH1, ET1) of the epididymis, as in cytosols sulfonation activities are high in epididymal tail and only marginal in epididymal head Sus scrofa
-
2.8.2.2 additional information tissue samples were collected from a total number of ten postpubertal crossbreed boars (nine German Landrace x Pietrain, one Large White) aged between 10 and 16 months. Immunolocalization study of SULT2A1. In epididymal samples, DHEA-ST activities are low in the head and in the proximal part of the body. In the distal body and tail, activities are in a similar range as observed in testicular samples, again with a considerable variability between individual animals and also between different segments of the organ Sus scrofa
-
2.8.2.2 testis
-
 Sus scrofa
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.8.2.2 3'-phosphoadenylyl sulfate + cholesterol
-
 Sus scrofa adenosine 3',5'-bisphosphate + cholesterol 3-sulfate
-
 ?
2.8.2.2 3'-phosphoadenylyl sulfate + dehydroepiandrosterone
-
 Sus scrofa adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
 ?
2.8.2.2 3'-phosphoadenylyl sulfate + pregnenolone
-
 Sus scrofa adenosine 3',5'-bisphosphate + pregnenolone 3-sulfate
-
 ?
2.8.2.2 additional information for human SULT2B1, pregnenolone (P5, isoform 2B1a) and cholesterol (isoform 2B1b) are regarded as preferential steroidal substrates Sus scrofa ?
-
-
2.8.2.2 additional information SULT2A1 exhibits a broad substrate spectrum. In addition to its prototypical substrate dehydroepiandrosterone (DHEA) and other 3beta-hydroxysteroids, it is also capable of sulfonating 3alpha-hydroxysteroids, estrogens and xenobiotics Sus scrofa ?
-
-

Subunits

EC Number Subunits Comment Organism
2.8.2.2 ? x * 34000, SDS-PAGE Sus scrofa

Synonyms

EC Number Synonyms Comment Organism
2.8.2.2 DHEA-ST
-
 Sus scrofa
2.8.2.2 hydroxysteroid sulfotransferase
-
 Sus scrofa
2.8.2.2 P5-ST
-
 Sus scrofa
2.8.2.2 SULT2A1
-
 Sus scrofa
2.8.2.2 SULT2B1
-
 Sus scrofa

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.8.2.2 37
-
 assay at Sus scrofa

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.8.2.2 7
-
 assay at Sus scrofa

General Information

EC Number General Information Comment Organism
2.8.2.2 physiological function enzyme SULT2A1 is the prevailing enzyme for the sulfonation of hydroxysteroids in the testis. In humans, SULTs 2A1 and 2B1 have been identified as the relevant sulfotransferases for neutral hydroxysteroids Sus scrofa
2.8.2.2 physiological function enzyme SULT2B1 may catalyze the formation of sterol sulfates in the epididymis. In humans, SULTs 2A1 and 2B1 have been identified as the relevant sulfotransferases for neutral hydroxysteroids Sus scrofa