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Information on EC 2.8.2.20 - protein-tyrosine sulfotransferase and Organism(s) Drosophila melanogaster and UniProt Accession Q9VYB7
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2.8.2.20 protein-tyrosine sulfotransferaseIUBMB Comments
The tyrosine residues of some specific proteins of rat pheochromocytoma cells act as acceptors.
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Word Map
- 2.8.2.20
-
tpsts
- 5'-phosphosulfate
-
o-sulfation
-
tyrosine-sulfated
- 3'-phosphoadenosine
- eay
-
sulfotyrosine
- psgl-1
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phytosulfokine
- 3'-phosphoadenosine-5'-phosphosulfate
-
sulfurylation
- disulfated
- synthesis
- molecular biology
- medicine
The taxonomic range for the selected organisms is: Drosophila melanogaster
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
tyrosylprotein sulfotransferase, tpst2, tpst-1, tpst1, tpst-2, tyrosylprotein sulfotransferase 2, tpst-a, tyrosylprotein sulfotransferase-1, tyrosylprotein sulfotransferase 1, tyrosylprotein sulfotransferase-2, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
sulfotransferase, protein (tyrosine)
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TPST
tyrosylprotein sulfotransferase
TPST
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-
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tyrosylprotein sulfotransferase
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
sulfate group transfer
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SYSTEMATIC NAME
IUBMB Comments
3'-phosphoadenylyl-sulfate:protein-tyrosine O-sulfotransferase
The tyrosine residues of some specific proteins of rat pheochromocytoma cells act as acceptors.
CAS REGISTRY NUMBER
COMMENTARY
87588-33-8
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3'-phosphoadenylyl sulfate + P-selectin glycoprotein ligand-1
?
recombinantly expressed substrate PSGL-1, glycoprotein found on the plasma membrane of neutrophils or monocytes. TPST activity on GST-tagged PSGL-1 is not affected by the GST fusion tag
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-
?
3'-phosphoadenylyl sulfate + protein tyrosine
adenosine 3',5'-bisphosphate + protein tyrosine-O-sulfate
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-
-
?
3'-phosphoadenylylsulfate + acidic polypeptide tyrosine
adenosine 3',5'-bisphosphate + acidic polypeptide tyrosine-O-sulfate
dominant characteristic is that there are generally between 3 and 4 acidic amino acids within the +/-5 residues of the sulfotyrosine
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-
?
3'-phosphoadenylyl sulfate + glutathione S-transferase-tagged P-selectin glycoprotein ligand-1
adenosine 3',5'-bisphosphate + glutathione S-transferase-tagged P-selectin glycoprotein ligand-1 tyrosine O-sulfate
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-
-
-
?
3'-phosphoadenylyl sulfate + P-selectin glycoprotein ligand-1
adenosine 3',5'-bisphosphate + P-selectin glycoprotein ligand-1 tyrosine O-sulfate
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i.e. ATEYEYLDYDFL
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-
?
3'-phosphoadenylyl sulfate + protein tyrosine
adenosine 3',5'-bisphosphate + protein tyrosine O-sulfate
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-
-
-
?
additional information
?
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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
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3'-phosphoadenylyl sulfate + protein tyrosine
adenosine 3',5'-bisphosphate + protein tyrosine-O-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + glutathione S-transferase-tagged P-selectin glycoprotein ligand-1
adenosine 3',5'-bisphosphate + glutathione S-transferase-tagged P-selectin glycoprotein ligand-1 tyrosine O-sulfate
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-
-
-
?
3'-phosphoadenylyl sulfate + P-selectin glycoprotein ligand-1
adenosine 3',5'-bisphosphate + P-selectin glycoprotein ligand-1 tyrosine O-sulfate
-
i.e. ATEYEYLDYDFL
-
-
?
3'-phosphoadenylyl sulfate + protein tyrosine
adenosine 3',5'-bisphosphate + protein tyrosine O-sulfate
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-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0021
3'-phosphoadenylyl sulfate
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using glutathione S-transferase-tagged P-selectin glycoprotein ligand-1 as cosubstrate, in 50 mM MES buffer (pH 6.5), 5 mM 2-mercaptoethanol, at 37°C
0.016
3'-phosphoadenylyl sulfate
-
using P-selectin glycoprotein ligand-1 as cosubstrate, in 50 mM MES buffer (pH 6.5), 5 mM 2-mercaptoethanol, at 37°C
0.011
P-selectin glycoprotein ligand-1
-
using glutathione S-transferase-tagged P-selectin glycoprotein ligand-1 as cosubstrate, in 50 mM MES buffer (pH 6.5), 5 mM 2-mercaptoethanol, at 37°C
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0.053
P-selectin glycoprotein ligand-1
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using P-selectin glycoprotein ligand-1 as cosubstrate, in 50 mM MES buffer (pH 6.5), 5 mM 2-mercaptoethanol, at 37°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.058
3'-phosphoadenylyl sulfate
-
using glutathione S-transferase-tagged P-selectin glycoprotein ligand-1 as cosubstrate, in 50 mM MES buffer (pH 6.5), 5 mM 2-mercaptoethanol, at 37°C
0.11
3'-phosphoadenylyl sulfate
-
using P-selectin glycoprotein ligand-1 as cosubstrate, in 50 mM MES buffer (pH 6.5), 5 mM 2-mercaptoethanol, at 37°C
0.045
P-selectin glycoprotein ligand-1
-
using glutathione S-transferase-tagged P-selectin glycoprotein ligand-1 as cosubstrate, in 50 mM MES buffer (pH 6.5), 5 mM 2-mercaptoethanol, at 37°C
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0.1
P-selectin glycoprotein ligand-1
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using P-selectin glycoprotein ligand-1 as cosubstrate, in 50 mM MES buffer (pH 6.5), 5 mM 2-mercaptoethanol, at 37°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6.7
3'-phosphoadenylyl sulfate
-
using P-selectin glycoprotein ligand-1 as cosubstrate, in 50 mM MES buffer (pH 6.5), 5 mM 2-mercaptoethanol, at 37°C
18.2
3'-phosphoadenylyl sulfate
-
using glutathione S-transferase-tagged P-selectin glycoprotein ligand-1 as cosubstrate, in 50 mM MES buffer (pH 6.5), 5 mM 2-mercaptoethanol, at 37°C
2
P-selectin glycoprotein ligand-1
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using P-selectin glycoprotein ligand-1 as cosubstrate, in 50 mM MES buffer (pH 6.5), 5 mM 2-mercaptoethanol, at 37°C
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4.2
P-selectin glycoprotein ligand-1
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using glutathione S-transferase-tagged P-selectin glycoprotein ligand-1 as cosubstrate, in 50 mM MES buffer (pH 6.5), 5 mM 2-mercaptoethanol, at 37°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.031
3'-phosphoadenylyl sulfate
-
using glutathione S-transferase-tagged P-selectin glycoprotein ligand-1 as substrate,in 50 mM MES buffer (pH 6.5), 5 mM 2-mercaptoethanol, at 37°C
0.061
3'-phosphoadenylyl sulfate
-
using P-selectin glycoprotein ligand-1 as substrate,in 50 mM MES buffer (pH 6.5), 5 mM 2-mercaptoethanol, at 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
assay at, recombinant hPAPSS-1 and DmTPST in a coupled assay using Escherchia coli proteins as substrates
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
assay at, recombinant hPAPSS-1 and DmTPST in a coupled assay using Escherchia coli proteins as substrates
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
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post-translational sulfation of tyrosine residues occurs in numerous secreted and integral membrane proteins and, in many cases, plays a crucial role in controlling the interactions of these proteins with physiological binding partners as well as invading pathogens
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
physiological function
protein tyrosine sulfation (PTS), catalyzed by membrane-anchored tyrosylprotein sulfotransferase (TPST), is one of the most common posttranslational modifications of secretory and transmembrane proteins. PTS, a key modulation of extracellular protein-protein interactions, accounts for various important biological activities, namely, virus entry, inflammation, coagulation, and sterility. PTS occurs in the trans-Golgi network, and the sulfated proteins and peptides are typically transmembrane or secretory proteins
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). TPST_DROME
499
1
58050
Swiss-Prot
Secretory Pathway (Reliability: 1)
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
preparation of TPST from Golgi-enriched membrane fractions, recombinant His-tagged GST- or NusA-fused enzyme from Escherichia coli strain BL21(DE3) to homogeneity by nickel affinity chromatography, low solubility or contamination with tag material
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene Tpst, recombinant expression of His-tagged enzyme fused to GST or NusA in Escherichia coli strain BL21(DE3), method optimization, overview
substance protein A-fused tyrosylprotein sulfotransferase is expressed in Escherichia coli BL21(DE3) cells
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TPST DNA and amino acid sequence determinationand analysis, sequence comparison
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
usage of tyrosylprotein sulfotransferases for in vitro one-pot enzymatic synthesis of sulfated proteins/peptides
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Moore, K.L.
The biology and enzymology of protein tyrosine O-sulfation
J. Biol. Chem.
278
24243-24246
2003
Homo sapiens, Mammalia, no activity in yeast, no activity in prokaryotes, Drosophila melanogaster (Q9VYB7)
Stone, M.J.; Chuang, S.; Hou, X.; Shoham, M.; Zhu, J.Z.
Tyrosine sulfation: an increasingly recognised post-translational modification of secreted proteins
N. Biotechnol.
25
299-317
2009
Bos taurus, Drosophila melanogaster, Homo sapiens, Mus musculus, Rattus norvegicus
Chen, B.H.; Wang, C.C.; Lu, L.Y.; Hung, K.S.; Yang, Y.S.
Fluorescence assay for protein post-translational tyrosine sulfation
Anal. Bioanal. Chem.
405
1425-1429
2013
Drosophila melanogaster
Wang, C.C.; Chen, B.H.; Lu, L.Y.; Hung, K.S.; Yang, Y.S.
Preparation of tyrosylprotein sulfotransferases for in vitro one-pot enzymatic synthesis of sulfated proteins/peptides
ACS Omega
3
11633-11642
2018
Drosophila melanogaster (Q9VYB7), Drosophila melanogaster, Homo sapiens (O60507), Homo sapiens (O60704), Homo sapiens
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
Anal. Chem.
89
3278-3284
2017
Drosophila melanogaster (Q9VYB7)
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