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Literature summary for 3.1.3.48 extracted from

  • Ku, B.; Keum, C.W.; Lee, H.S.; Yun, H.Y.; Shin, H.C.; Kim, B.Y.; Kim, S.J.
    Crystal structure of SP-PTP, a low molecular weight protein tyrosine phosphatase from Streptococcus pyogenes (2016), Biochem. Biophys. Res. Commun., 478, 1217-1222 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene SPy_0039, recombinant expression of His-tagged enzyme Sp-PTP in Escherichia coli strain BL21(DE3) Streptococcus pyogenes serotype M1

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant His-tagged enzyme, sitting drop vapor diffusion method, mixing of 0.001 ml of 20 mg/ml protein in 20 mM Tris-HCl, pH 7.5, 200 mM NaCl, 5 mM 2-mercaptoethanol, and 2 mM dithiothreitol, with 0.001 ml of precipitant solution containing 150 mM potassium thiocyanate, 100 mM Bis-Tris, pH 6.25, 8% PEG 3350, and 2% D-sorbitol, 18°C, X-ray diffraction structure determination and analysis at 1.9 A resolution, molecular replacement method using the structure of the YfkJ from Bacillus subtilis as a search model Streptococcus pyogenes serotype M1

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
[a protein]-tyrosine phosphate + H2O Streptococcus pyogenes serotype M1
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[a protein]-tyrosine + phosphate
-
?

Organism

Organism UniProt Comment Textmining
Streptococcus pyogenes serotype M1 Q9A1Y0 a Group A Streptococcus
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Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme Sp-PTP from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration Streptococcus pyogenes serotype M1

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl phosphate + H2O
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Streptococcus pyogenes serotype M1 4-nitrophenol + phosphate
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?
additional information enzyme SP-PTP shares high similarity with typical low molecular weight protein tyrosine phosphatases (LMWPTPs), which are specific for phosphotyrosine, but not with dual-specificity phosphatases, in overall folding and active site composition. In the dephosphorylation activity test, SP-PTP consistently acts on phosphotyrosine substrates, but not or only minimally on phosphoserine/phosphothreonine substrates. PTP as a canonical tyrosine-specific LMWPTP Streptococcus pyogenes serotype M1 ?
-
?
[a protein]-tyrosine phosphate + H2O
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Streptococcus pyogenes serotype M1 [a protein]-tyrosine + phosphate
-
?

Subunits

Subunits Comment Organism
More the SP-PTP molecule is composed of four parallel beta-strands [beta1(Lys3-Val7), beta2(Met32-Ala37), beta3(Tyr81-Gly84), and beta4(Ile105-Leu107)] sandwiched on both sides by five alpha-helices [a1(Cys13-Ile25), alpha2(Ser49-Tyr58), alpha3(Ile73-Thr78), alpha4(Ser87-Ser97), and alpha5(Phe122-Leu140)], which are arranged to form the Rossmann fold, which is typical of LMWPTPs Streptococcus pyogenes serotype M1

Synonyms

Synonyms Comment Organism
LMWPTP
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Streptococcus pyogenes serotype M1
low molecular weight protein tyrosine phosphatase
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Streptococcus pyogenes serotype M1
SP-PTP
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Streptococcus pyogenes serotype M1
SPy_0039
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Streptococcus pyogenes serotype M1

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
assay at Streptococcus pyogenes serotype M1

General Information

General Information Comment Organism
additional information enzyme structure analysis and comparisons, overview Streptococcus pyogenes serotype M1