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Overview for MACiE Entry M0047

Version history

General Information

EC Number: 3.1.3.48 (A member of the Hydrolases, Acting on ester bonds, Phosphoric-monoester hydrolases)

Enzyme Name: protein-tyrosine-phosphatase

Biological Species: Yersinia enterocolitica (Bacteria)

Catalytic Chain UniprotKB Accession Codes:

  • P15273 - Tyrosine-protein phosphatase yopH

Representative PDB Code: 1ytw - YERSINIA PTPASE COMPLEXED WITH TUNGSTATE (Resolution = 2.40 Å).

Catalytic CATH Codes:

Display structure information

Overall Reaction:

Image of protein tyrosine phosphate

Image of water

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Image of protein tyrosine

Image of phosphate

protein tyrosine phosphate
C01167
CHEBI:61972
water
C00001
CHEBI:15377
protein tyrosine
C00585
CHEBI:32789
phosphate
C00009
CHEBI:18367

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Stepwise Description of the Reaction

Step 1Cys403 initiates a nucleophilic attack upon the phosphate of the substrate in a substitution reaction, which eliminates the tyrosine with concomitant deprotonation of Asp356.
Step 2Glu290 deprotonates water, which initiates a nucleophilic attack upon the phosphate of the covalently bound intermediate in a substitution reaction, which eliminates Cys403.
Step 3Asp356 deprotonates Glu290 in an inferred return step.

View similar reactions (composite manual annotation)


Catalytic Residues Involved

Type Number Chain Location of Function
Glu 290 A Side Chain
Asp 356 A Side Chain
His 402 A Side Chain
Cys 403 A Side Chain
Arg 409 A Side Chain
Thr 410 A Side Chain

References

  1. E. B. Fauman et al. (1996), J. Biol. Chem., 271, 18780-18788. The X-ray crystal structures of Yersinia tyrosine phosphatase with bound tungstate and nitrate. Mechanistic implications.
    Medline: 8702535
  2. R. H. Hoff et al. (1999), J. Am. Chem. Soc., 121, 9514-9521. Does Positive Charge at the Active Sites of Phosphatases Cause a Change in Mechanism? The Effect of the Conserved Arginine on the Transition State for Phosphoryl Transfer in the Protein-Tyrosine Phosphatase from Yersinia.
  3. F. Wang et al. (1998), Biochemistry, 37, 15289-15299. Conformational and dynamic changes of Yersinia protein tyrosine phosphatase induced by ligand binding and active site mutation and revealed by H/D exchange and electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry.
    Medline: 9799489

Homologue information for M0047 (1ytw)

CSA Homologues

MACiE Homologues (within the PDB)

MACiE Homologues (within UniprotKB/SwissProt)


Links to this entry in other databases

Link to EC-PDB-SUM Link to PDB-SUM Link to RCSB PDB Link to PDBe Link to CSA
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GOA logo
phosphoprotein phosphatase activity (molecular function)
protein tyrosine phosphatase activity (molecular function)
extracellular region (cellular component)
protein dephosphorylation (biological process)
pathogenesis (biological process)
dephosphorylation (biological process)
hydrolase activity (molecular function)
phosphatase activity (molecular function)
peptidyl-tyrosine dephosphorylation (biological process)
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