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Literature summary for 3.1.3.53 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
Search for more literature for 3.1.3.53

Application

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

Protein Variants

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

Inhibitors

Inhibitors Comment Organism Structure
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

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
aortic smooth muscle
-
 Sus scrofa
-

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
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

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