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Literature summary extracted from

  • Huang, B.Y.; Chen, P.C.; Chen, B.H.; Wang, C.C.; Liu, H.F.; Chen, Y.Z.; Chen, C.S.; Yang, Y.S.
    High-throughput screening of sulfated proteins by using a genome-wide proteome microarray and protein tyrosine sulfation system (2017), Anal. Chem., 89, 3278-3284 .
    View publication on PubMed

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.8.2.20 Golgi apparatus
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 Drosophila melanogaster 5794
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2.8.2.20 Golgi membrane
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 Drosophila melanogaster 139
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2.8.2.20 membrane a type II membrane enzyme Drosophila melanogaster 16020
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Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.8.2.20 3'-phosphoadenylyl sulfate + protein tyrosine Drosophila melanogaster
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 adenosine 3',5'-bisphosphate + protein tyrosine-O-sulfate
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 ?

Organism

EC Number Organism UniProt Comment Textmining
2.8.2.20 Drosophila melanogaster Q9VYB7
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.8.2.20 3'-phosphoadenylyl sulfate + protein tyrosine
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 Drosophila melanogaster adenosine 3',5'-bisphosphate + protein tyrosine-O-sulfate
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 ?
2.8.2.20 additional information localization of the potential sulfation sites of Escherichia coli proteins on a proteome microarray by using a 3'-phosphoadenosine 5'-phosphosulfate (PAPS) synthase (recombinant hPAPSS-1, UniProt ID O43252)-coupled tyrosylprotein sulfotransferase (TPST) catalysis system that involves in situ PAPS generation and TPST catalysis. Among the 4256 Escherichia coli strain K12 proteins, 875 sulfated proteins are identified via antisulfotyrosine primary and Cy3-labeled antimouse secondary antibodies and are potential proteins subjected to tyrosine sulfation by the recombinant Drosophila melanogaster TPST (DmTPST) with human PAPSS-1. Method overview Drosophila melanogaster ?
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Synonyms

EC Number Synonyms Comment Organism
2.8.2.20 DmTPST
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 Drosophila melanogaster
2.8.2.20 TPST
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 Drosophila melanogaster
2.8.2.20 tyrosylprotein sulfotransferase
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 Drosophila melanogaster

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.8.2.20 6.5
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 assay at, recombinant hPAPSS-1 and DmTPST in a coupled assay using Escherchia coli proteins as substrates Drosophila melanogaster

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.8.2.20 6.5
-
 assay at, recombinant hPAPSS-1 and DmTPST in a coupled assay using Escherchia coli proteins as substrates Drosophila melanogaster

General Information

EC Number General Information Comment Organism
2.8.2.20 physiological function protein tyrosine sulfation (PTS) is a posttranslational modification commonly detected in secreted proteins and cell-surface receptors. PTS facilitates protein-protein interactions and critically affects enzymatic activity and protein lifespan, and PTS is catalyzed by the enzyme tyrosylprotein sulfotransferase (TPST), a Golgi-localized type II transmembrane protein. In contrast to phosphorylation, which is central to intracellular signal transduction, sulfation modulates cell-cell and cell-matrix communication, and TPST functions at critical steps in generating the sulfation that forms a part of the recognition motifs for adhesion molecules, chemokines, growth factors and their receptors, and pathogens. PTS plays a crucial role in physiology and pathology, including in the immune responses and viral infection involved in numerous diseases Drosophila melanogaster