(myosin-light-chain) phosphatase

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myosin-light-chain-phosphatase
Identifiers
EC number 3.1.3.53
CAS number 86417-96-1
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO

In enzymology, a myosin light-chain phosphatase (MLCP) (EC 3.1.3.53) is an enzyme that catalyzes the chemical reaction

[myosin light-chain] phosphate + H2O \rightleftharpoons [myosin light-chain] + phosphate

Thus, the two substrates of this enzyme are myosin light-chain phosphate and H2O, whereas its two products are myosin light-chain and phosphate.

This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name of this enzyme class is [myosin-light-chain]-phosphate phosphohydrolase. Other names in common use include myosin light chain kinase phosphatase, myosin phosphatase, myosin phosphatase, protein phosphatase 2A, and myosin-light-chain-phosphatase.

Structural studies[edit]

MLCP is composed of three subunits: a PP1c catalytic subunit, a myosin targeting subunit called MYPT1, and a small subunit of unknown function called M20.

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1S70.

Function[edit]

MLCP is important for regulating contraction in smooth muscle, which lacks the troponin binding system. It inhibits contraction by dephosphorylating myosin light-chain fibers. It counters the myosin light-chain kinase (MLCK), which promotes contraction by phosphorylating myosin light-chain proteins. MLCP is present in smaller amounts compared with MLCK, but compensates for this lack of mass by rapid movement along actin fibers. MLCP activity is inhibited by Rhoa and Rho kinase, components of the Ca2+ independent pathway for maintaining muscle contraction.[1] This can result in Ca2+ sensitization.

See also[edit]

References[edit]

Further reading[edit]

  • Pato MD, Adelstein RS (1983). "Purification and characterization of a multisubunit phosphatase from turkey gizzard smooth muscle. The effect of calmodulin binding to myosin light chain kinase on dephosphorylation". J. Biol. Chem. 258 (11): 7047–54. PMID 6304072. 
  • Kimura K et al. (1996). "Regulation of Myosin phosphatase by Rho and Rho-associated kinase (Rho-kinase)". Science 273 (5272): 245–248. doi:10.1126/science.273.5272.245. PMID 8662509.