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Literature summary extracted from

  • Eto, M.; Kitazawa, T.; Matsuzawa, F.; Aikawa, S.; Kirkbride, J.A.; Isozumi, N.; Nishimura, Y.; Brautigan, D.L.; Ohki, S.
    Phosphorylation-induced conformational switching of CPI-17 produces a potent myosin phosphatase inhibitor (2007), Structure, 15, 1591-1602.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
3.1.3.53 additional information phosphorylation of endogenous inhibitor proteins provides a mechanism for reciprocal coordination of kinase and phosphatase activities Sus scrofa

Protein Variants

EC Number Protein Variants Comment Organism
3.1.3.53 additional information construction of synthetic segments of MYPT1 (1-19) and (24-41) and MYPT1(1-19) and (24-41) peptides Sus scrofa

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.3.53 CPI-17 specific inhibitor predominantly expressed in smooth muscles and neurons, phosphorylation of CPI-17 at Thr38 is necessary and sufficient to convert the protein into a potent inhibitor of myosin phosphatase Sus scrofa

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.53 Sus scrofa
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.3.53 aortic smooth muscle
-
Sus scrofa
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.3.53 myosin light-chain phosphate + H2O muscle Sus scrofa myosin light-chain + phosphate
-
?

Subunits

EC Number Subunits Comment Organism
3.1.3.53 More MLCP is a heterotrimer composed of the catalytic subunit belonging to protein phosphatase 1c PPC1, the myosin phosphatase targeting subunit MYPT1, and M21 Sus scrofa

Synonyms

EC Number Synonyms Comment Organism
3.1.3.53 MLCP
-
Sus scrofa
3.1.3.53 myosin light chain phosphatase
-
Sus scrofa
3.1.3.53 myosin phosphatase
-
Sus scrofa
3.1.3.53 MYPT1
-
Sus scrofa