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Literature summary for 3.1.3.48 extracted from

  • Srinivasan, B.; Marks, H.; Mitra, S.; Smalley, D.M.; Skolnick, J.
    Catalytic and substrate promiscuity distinct multiple chemistries catalysed by the phosphatase domain of receptor protein tyrosine phosphatase (2016), Biochem. J., 473, 2165-2177 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene PTPRD, sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha Homo sapiens
gene PTPRR, sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
4-nitrophenyl phosphate substrate inhibition at higher concentrations; substrate inhibition at higher concentrations Homo sapiens
additional information IPTG and lactose inhibit the sugar hydrolase activity of the enzyme PTPRdelta Homo sapiens
phosphate inhibits the phosphatase activity, but not the sugar hydrolase activity; inhibits the phosphatase activity, but not the sugar hydrolase activity Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Michaelis-Menten kinetics Homo sapiens
0.64
-
4-nitrophenyl phosphate pH 7.3, 22°C, recombinant enzyme Homo sapiens
1.04
-
4-nitrophenyl phosphate pH 7.3, 22°C, recombinant enzyme Homo sapiens
37
-
bis(4-nitrophenyl) phosphate pH 7.3, 22°C, recombinant enzyme Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
cell surface receptor protein tyrosine phosphatases (PTPRs) are a family of cell surface receptor proteins Homo sapiens 9986
-
membrane receptor protein tyrosine phosphatases (PTPRs) are a family of cell surface receptor proteins Homo sapiens 16020
-
additional information receptor protein tyrosine phosphatase subtype delta has a cell adhesion extracellular domain and two cytoplasmic protein tyrosine phosphatase (PTP) domains Homo sapiens
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ activates Homo sapiens
Mg2+ activates the sugar hydrolase activity, but not the phosphatase activity Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
[a protein]-tyrosine phosphate + H2O Homo sapiens
-
[a protein]-tyrosine + phosphate
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens P23468
-
-
Homo sapiens Q15256
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Homo sapiens

Reaction

Reaction Comment Organism Reaction ID
[a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate the phosphatase domain of PTPRs catalyze a two-step phosphate monoester hydrolysis reaction through a highly conserved sequence motif (H/V)CX5R(S/T) with a nucleophilic cysteine Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
brain PTPRdelta is predominantly expressed in the brain Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl phosphate + H2O
-
Homo sapiens 4-nitrophenol + phosphate
-
?
bis(4-nitrophenyl) phosphate + H2O
-
Homo sapiens ?
-
?
additional information receptor protein tyrosine phosphatase isoform delta (PTPRdelta) displays substrate promiscuity by hydrolyzing the diester bond while showing a high-level of discrimination in its primary monoesterase substrate preference. The phosphatase domain of receptor protein tyrosine phosphatases catalyzes the hydrolysis of glycosidic (COC) bonds apart from its primary activity of cleaving phosphomonoester (COP) bond. This is important because the hydrolysis of COC bond in beta-galactosides and COP bond in phosphomonoesters require different functional groups and different mechanism of cleavage. No activity with adenosine monophosphate, inosine monophosphate, guanosine monophosphate, nicotinamide adenine dinucleotide phosphate, and pyridoxal 5'-phosphate, also no activity with tris-(4-nitrophenyl) phosphate, tris-(4-nitrobenzyl) phosphate, tetrakis-(4-nitrophenyl) diphosphate, NADP+, and peptide H-Gly-PNA. The enzyme shows low activity with several nitrophenyl glycosides cleaving the glycosidic bond. Substrate specificity, overview. No phosphocysteinyl hydrolysis of isozyme PTPRdelta Homo sapiens ?
-
?
additional information receptor protein tyrosine phosphatase isoform delta (PTPRdelta) shows catalytic and substrate promiscuity. The phosphatase domain of receptor protein tyrosine phosphatases catalyzes the hydrolysis of glycosidic (COC) bonds apart from its primary activity of cleaving phosphomonoester (COP) bond. This is important because the hydrolysis of COC bond in beta-galactosides and COP bond in phosphomonoesters require different functional groups and different mechanism of cleavage. No activity with adenosine monophosphate, inosine monophosphate, guanosine monophosphate, nicotinamide adenine dinucleotide phosphate, and pyridoxal 5'-phosphate, also no activity with tris-(4-nitrophenyl) phosphate, tris-(4-nitrobenzyl) phosphate, tetrakis-(4-nitrophenyl) diphosphate, NADP+, and peptide H-Gly-PNA. The enzyme shows low activity with several nitrophenyl glycosides cleaving the glycosidic bond. Substrate specificity, overview. Isozyme PD-PTPRomega shows rate-limiting phosphocysteinyl hydrolysis leading to a biphasic time-dependence of substrate to product conversion Homo sapiens ?
-
?
O-phospho-L-tyrosine + H2O
-
Homo sapiens tyrosine + phosphate
-
?
[a protein]-tyrosine phosphate + H2O
-
Homo sapiens [a protein]-tyrosine + phosphate
-
?

Subunits

Subunits Comment Organism
? x * 34267, recombinant His-tagged enzyme, mass spectrometry Homo sapiens
More receptor protein tyrosine phosphatase subtype delta has a cell adhesion extracellular domain and two cytoplasmic protein tyrosine phosphatase (PTP) domains Homo sapiens

Synonyms

Synonyms Comment Organism
Ch-1PTPase UniProt Homo sapiens
NC-PTPCOM1 UniProt Homo sapiens
PCPTP1 UniProt Homo sapiens
protein tyrosine phosphatase
-
Homo sapiens
PTP
-
Homo sapiens
PTPRD
-
Homo sapiens
PTPRdelta
-
Homo sapiens
PTPRomega
-
Homo sapiens
PTPRQ
-
Homo sapiens
PTPRR
-
Homo sapiens
receptor protein tyrosine phosphatase isoform delta
-
Homo sapiens
receptor protein tyrosine phosphatase isoform omega
-
Homo sapiens
receptor-type tyrosine-protein phosphatase R UniProt Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
22
-
assay at room temperature Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.027
-
4-nitrophenyl phosphate pH 7.3, 22°C, recombinant enzyme Homo sapiens
0.033
-
bis(4-nitrophenyl) phosphate pH 7.3, 22°C, recombinant enzyme Homo sapiens
0.207
-
4-nitrophenyl phosphate pH 7.3, 22°C, recombinant enzyme Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.3
-
phosphatase activity Homo sapiens
7.3
-
assay at Homo sapiens
7.3
-
sugar hydrolase activity Homo sapiens

General Information

General Information Comment Organism
evolution receptor protein tyrosine phosphatases (PTPRs) are a family of cell surface receptor proteins that antagonize tyrosine kinase signaling Homo sapiens
physiological function the primary catalytic activity involves the hydrolysis of a phosphomonoester bond (C-O-P) with high catalytic efficiency, while the secondary activity is the hydrolysis of a glycosidic bond (C-O-C) with poorer catalytic efficiency. This enzyme also displays substrate promiscuity by hydrolyzing diester bonds while being highly discriminative for its monoester substrates. Additional distinct sugar hydrolase and diesterase activity for the phosphatase domain of PTPRdelta and its homologue PTPRomega Homo sapiens
physiological function the primary catalytic activity involves the hydrolysis of a phosphomonoester bond (C-O-P) with high catalytic efficiency, while the secondary activity is the hydrolysis of a glycosidic bond (C-O-C) with poorer catalytic efficiency. This enzyme also displays substrate promiscuity by hydrolyzing diester bonds while being highly discriminative for its monoester substrates. Additional distinct sugar hydrolase and diesterase activity for the phosphatase domain of PTPRdelta and its homologue PTPRomega. PTPRdelta is known to be involved in the guidance and termination of motor neurons during embryonic development, PTPRdelta is essential for the organization of neural circuits Homo sapiens

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.0009
-
bis(4-nitrophenyl) phosphate pH 7.3, 22°C, recombinant enzyme Homo sapiens
0.042
-
4-nitrophenyl phosphate pH 7.3, 22°C, recombinant enzyme Homo sapiens
0.199
-
4-nitrophenyl phosphate pH 7.3, 22°C, recombinant enzyme Homo sapiens