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, protein phosphatase 2A, and myosin-light-chain-phosphatase.
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. This can result in Ca2+ sensitization.
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. PMID6304072.