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Information on EC 3.1.3.48 - protein-tyrosine-phosphatase and Organism(s) Yersinia enterocolitica and UniProt Accession P15273

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.3 Phosphoric-monoester hydrolases
                3.1.3.48 protein-tyrosine-phosphatase
IUBMB Comments
Dephosphorylates O-phosphotyrosine groups in phosphoproteins, such as the products of EC 2.7.10.2, non-specific protein-tyrosine kinase.
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This record set is specific for:
Yersinia enterocolitica
UNIPROT: P15273
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The taxonomic range for the selected organisms is: Yersinia enterocolitica
The enzyme appears in selected viruses and cellular organisms
Synonyms
ptp1b, protein tyrosine phosphatase, shp-1, shp-2, tyrosine phosphatase, protein phosphatase 2a, acid phosphatase activity, mkp-1, cdc25a, ptpn22, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70Z-SHP
-
-
-
-
Brain-derived phosphatase
-
-
-
-
BVP
-
-
-
-
CD148 antigen
-
-
-
-
CD45
-
-
-
-
CD45 antigen
-
-
-
-
Cdc25-like protein
-
-
-
-
CDK2-associated dual specificity phosphatase
-
-
-
-
Ch-1PTPase
-
-
-
-
CPTP1
-
-
-
-
DLAR
-
-
-
-
Dual specificity phosphatase Cdc25A
-
-
-
-
Dual specificity phosphatase Cdc25B
-
-
-
-
Dual specificity phosphatase Cdc25C
-
-
-
-
Dual specificity protein phosphatase hVH1
-
-
-
-
Dual specificity protein phosphatase hVH2
-
-
-
-
Dual specificity protein phosphatase hVH3
-
-
-
-
Dual specificity protein phosphatase PYST1
-
-
-
-
Dual specificity protein phosphatase PYST2
-
-
-
-
Dual specificity protein phosphatase VHR
-
-
-
-
Dual-specificity tyrosine phosphatase TS-DSP6
-
-
-
-
Dual-specificity tyrosine phosphatase YVH1
-
-
-
-
ES cell phosphatase
-
-
-
-
HCP
-
-
-
-
Hematopoietic cell protein-tyrosine phosphatase
-
-
-
-
Hematopoietic cell protein-tyrosine phosphatase 70Z-PEP
-
-
-
-
Hematopoietic protein-tyrosine phosphatase
-
-
-
-
HEPTP
-
-
-
-
HPTP beta-like tyrosine phosphatase
-
-
-
-
HPTP eta
-
-
-
-
hPTPE1
-
-
-
-
ICAAR
-
-
-
-
Islet cell autoantigen related protein
-
-
-
-
kinase associated phosphatase
-
-
-
-
L-CA
-
-
-
-
Late protein H1
-
-
-
-
LCA
-
-
-
-
LCA-related phosphatase
-
-
-
-
Leukocyte antigen related
-
-
-
-
Low molecular weight cytosolic acid phosphatase
-
-
-
-
LRP
-
-
-
-
Lymphoid phosphatase
-
-
-
-
LyP
-
-
-
-
M1851
-
-
-
-
MAP-kinase phosphatase CPG21
-
-
-
-
MEG
-
-
-
-
Mitosis initiation protein
-
-
-
-
Mitosis initiation protein MIH1
-
-
-
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Mitotic inducer homolog
-
-
-
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MKP-1 like protein tyrosine phosphatase
-
-
-
-
MPTP
-
-
-
-
MPTP-PEST
-
-
-
-
NC-PTPCOM1
-
-
-
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Neural-specific protein-tyrosine phosphatase
-
-
-
-
ORF5
-
-
-
-
OST-PTP
-
-
-
-
P19-PTP
-
-
-
-
P80
-
-
-
-
PC12-PTP1
-
-
-
-
Phogrin
-
-
-
-
Phosphacan
-
-
-
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phosphatase, phosphoprotein (phosphotyrosine)
-
-
-
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phosphatase, phosphotyrosine
-
-
-
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phosphoprotein phosphatase (phosphotyrosine)
-
-
-
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phosphotyrosine histone phosphatase
-
-
-
-
phosphotyrosine phosphatase
-
-
-
-
Phosphotyrosine phosphatase 13
-
-
-
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phosphotyrosine protein phosphatase
-
-
-
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phosphotyrosylprotein phosphatase
-
-
-
-
protein phosphotyrosine phosphatase
-
-
-
-
protein tyrosine phosphatase
-
-
Protein tyrosine phosphatase-NP
-
-
-
-
Protein-protein-tyrosine phosphatase HA2
-
-
-
-
Protein-tyrosine phosphatase 1B
-
-
-
-
Protein-tyrosine phosphatase 1C
-
-
-
-
Protein-tyrosine phosphatase 1E
-
-
-
-
Protein-tyrosine phosphatase 2C
-
-
-
-
Protein-tyrosine phosphatase 2E
-
-
-
-
Protein-tyrosine phosphatase 3CH134
-
-
-
-
Protein-tyrosine phosphatase CL100
-
-
-
-
Protein-tyrosine phosphatase D1
-
-
-
-
Protein-tyrosine phosphatase ERP
-
-
-
-
Protein-tyrosine phosphatase G1
-
-
-
-
Protein-tyrosine phosphatase H1
-
-
-
-
Protein-tyrosine phosphatase LC-PTP
-
-
-
-
Protein-tyrosine phosphatase MEG1
-
-
-
-
Protein-tyrosine phosphatase MEG2
-
-
-
-
Protein-tyrosine phosphatase P19
-
-
-
-
Protein-tyrosine phosphatase PCPTP1
-
-
-
-
Protein-tyrosine phosphatase pez
-
-
-
-
Protein-tyrosine phosphatase PTP-RL10
-
-
-
-
Protein-tyrosine phosphatase PTP36
-
-
-
-
Protein-tyrosine phosphatase PTPL1
-
-
-
-
Protein-tyrosine phosphatase striatum-enriched
-
-
-
-
Protein-tyrosine phosphatase SYP
-
-
-
-
Protein-tyrosine-phosphatase SL
-
-
-
-
Protein-tyrosine-phosphate phosphohydrolase
-
-
-
-
PTP IA-2beta
-
-
-
-
PTP-1B
-
-
-
-
PTP-1C
-
-
-
-
PTP-1D
-
-
-
-
PTP-2C
-
-
-
-
PTP-BAS
-
-
-
-
PTP-E1
-
-
-
-
PTP-H1
-
-
-
-
PTP-HA2
-
-
-
-
PTP-NP
-
-
-
-
PTP-SH2beta
-
-
-
-
PTP1C
-
-
-
-
PTP1D
-
-
-
-
PTP2C
-
-
-
-
PTPase YVH1
-
-
-
-
PTPase-MEG1
-
-
-
-
PTPase-MEG2
-
-
-
-
PTPG1
-
-
-
-
PTPN6
-
-
-
-
PTPNE6
-
-
-
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PY protein phosphatase
-
-
-
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R-PTP-alpha
-
-
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R-PTP-beta
-
-
-
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R-PTP-delta
-
-
-
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R-PTP-epsilon
-
-
-
-
R-PTP-eta
-
-
-
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R-PTP-gamma
-
-
-
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R-PTP-kappa
-
-
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R-PTP-mu
-
-
-
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R-PTP-zeta
-
-
-
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Receptor-linked protein-tyrosine phosphatase 10D
-
-
-
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Receptor-linked protein-tyrosine phosphatase 99A
-
-
-
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RNA/RNP complex-intereracting phosphatase
-
-
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ROL B protein
-
-
-
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RPTPalpha
-
-
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SH-PTP1
-
-
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SH-PTP2
-
-
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SH-PTP3
-
-
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SHP
-
-
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Small tyrosine phosphatase
-
-
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Small, acidic phosphotyrosine protein phosphatase
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-
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STEP
-
-
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String protein
-
-
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Syp
-
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T-cell protein-tyrosine phosphatase
-
-
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T-DSP11
-
-
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T200
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-
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TCPTP
-
-
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Testis-and skeletal-muscle-specific DSP
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-
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tyrosine O-phosphate phosphatase
-
-
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Tyrosine phosphatase CBPTP
-
-
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tyrosylprotein phosphatase
-
-
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[phosphotyrosine]protein phosphatase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
[a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate
show the reaction diagram
mechanism
[a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
-
-
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-
SYSTEMATIC NAME
IUBMB Comments
protein-tyrosine-phosphate phosphohydrolase
Dephosphorylates O-phosphotyrosine groups in phosphoproteins, such as the products of EC 2.7.10.2, non-specific protein-tyrosine kinase.
CAS REGISTRY NUMBER
COMMENTARY hide
79747-53-8
-
97162-86-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
essential for virulence of the bacteria responsible for the plague
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pervanadate
-
pervanadate inhibits PTP by irreversibly oxidizing the catalytic cysteine of PTP
vanadate
-
enzyme inhibition by vanadate takes place through an oxidant-independent pathway, the inhibition is reversible with EDTA
[RuIII(EDTA)(OH2/OH)]1-/2-
-
RuIII-EDTA inhibits PTP, like vanadate, through an oxidant-independent pathway. It inhibits PTP at physiological pH values by a mechanism that involves binding of the Cys residue of the catalytic domain of the enzyme, overview. At pH 7.4, the Ru-EDTA complex exists as a mixture of aqua and hydroxo-species. The inhibition is reversible or inhibited by glutathione
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.89 - 57.7
4-nitrophenyl phosphate
-
value strongly dependent on ionic strength and pH
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6.2 - 1440
4-nitrophenyl phosphate
-
value strongly dependent on ionic strength and pH
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
Ru(III) complexes with thiolato groups, stopped-flow kinetic studies with both RuIII-EDTA and RuIII-hEDTRA with the thiol-containing biomolecules, GSH or Cys, in the buffer
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1233
-
enzyme Yop51 DELTA162, catalytic domain
799
-
enzyme Yop51
806
-
enzyme Yop51*, point mutation C235R
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
encoded on a virulence plasmid
Uniprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
YOPH_YEREN
468
0
50939
Swiss-Prot
-
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35000
-
enzyme Yop51*Delta162, catalytic domain, gel filtration
49800
-
enzymes Yop51, Yop51*, sedimentation equilibrium centrifugation
51000
-
1 * 51000, enzymes Yop51 and Yop51*, SDS-PAGE
74000
-
enzymes Yop51, Yop51*, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
-
overview on structural properties
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A33D
-
interferes with substrate binding
C235R
D356N
-
dramatically reduced activity, D356 acts as general acid/base
N34D
-
interferes with substrate binding
Q11R
-
interferes with substrate binding
R409A
-
dramatical decrease in kcat, 26-fold increase in Km-value
R409K
-
dramatical decrease in kcat, 1.9-fold increase in Km-value
V31G
-
interferes with substrate binding
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
DTT stabilizes the enzyme
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, 2-3 months, loss of activity, DTT stabilizes
-
4°C, 100 mM acetate, pH 5.7, 1 mM EDTA, ionic strength 0.15, several months, no loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of Yop51 and Yop51*, a C235R point mutation and expression of the catalytic domain, residues 163-468 in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fauman, E.B.; Yuvaniyama, C.; Schubert, H.L.; Suckey, J.A.; Saper, m.A.
The x-ray crystal structures of Yersinia tyrosine phosphatase with bound tungstate and nitrate. Mechanistic implications
J. Biol. Chem.
271
18780-18788
1996
Yersinia enterocolitica (P15273)
Manually annotated by BRENDA team
Zhang, Z.Y.; Clemens, J.C.; Schubert, H.L.; Stuckey, J.A.; Fischer, M.W.F.; Hume, D.M.; Saper, M.A.; Dixon, J.E.
Expression, purification, and physicochemical characterization of a recombinant Yersinia protein tyrosine phosphatase
J. Biol. Chem.
267
23759-23766
1992
Yersinia enterocolitica
Manually annotated by BRENDA team
Zhang, Z.Y.
Chemical and mechanistic approaches to the study of protein tyrosine phosphatases
Acc. Chem. Res.
36
385-392
2003
Yersinia enterocolitica
Manually annotated by BRENDA team
Czyryca, P.G.; Hengge, A.C.
The mechanism of the phosphoryl transfer catalyzed by Yersinia protein-tyrosine phosphatase: a computational and isotope effect study
Biochim. Biophys. Acta
1547
245-253
2001
Yersinia enterocolitica
Manually annotated by BRENDA team
Kolmodin, K.; Aqvist, J.
The catalytic mechanism of protein tyrosine phosphatases revisited
FEBS Lett.
498
208-213
2001
Saccharomyces cerevisiae, Homo sapiens, Yersinia enterocolitica
Manually annotated by BRENDA team
Montagna, L.G.; Ivanov, M.I.; Bliska, J.B.
Identification of residues in the N-terminal domain of the Yersinia tyrosine phosphatase that are critical for substrate recognition
J. Biol. Chem.
276
5005-5011
2001
Yersinia enterocolitica
Manually annotated by BRENDA team
Chatterjee, D.; Mitra, A.; Levina, A.; Lay, P.A.
A potential role for protein tyrosine phosphatase inhibition by a RuIII-edta complex (edta = ethylenediaminetetraacetate) in its biological activity
Chem. Commun. (Camb. )
2008
2864-2866
2008
Yersinia enterocolitica
Manually annotated by BRENDA team