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Literature summary for 3.1.3.53 extracted from

  • Gailly, P.; Wu, X.; Haystead, T.A.J.; Somlyo, A.P.; Cohen, P.T.W.; Cohen, P.; Somlyo, A.V.
    Regions of the 110-kDa regulatory subunit M110 required for regulation of myosin-light-chain-phosphatase activity in smooth muscle (1996), Eur. J. Biochem., 239, 326-332.
    View publication on PubMed
Search for more literature for 3.1.3.53

Cloned(Commentary)

Cloned (Comment) Organism
a 72.5 kDa N-terminal fragment of the 110 kDa subunit is cloned Rattus norvegicus

Inhibitors

Inhibitors Comment Organism Structure
arachidonic acid inhibits SMPP-1M, dissociates the catalytic subunit from the native holoenzyme, inhibits the regulatory action of the 110 kDa/21 kDa subunit complex on the catalytic subunit PP1C activity, the C-terminal half of the 110 kDa subunit is required for inhibition Sus scrofa

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
21000
-
 1 * 110000 + 1 * 37000 + 1 * 21000, enzyme SMPP-1M, 37 kDa catalytic subunit PP1C, 110 kDa regulatory subunit M110 Sus scrofa
37000
-
 1 * 110000 + 1 * 37000 + 1 * 21000, enzyme SMPP-1M, 37 kDa catalytic subunit PP1C, 110 kDa regulatory subunit M110 Sus scrofa
110000
-
 1 * 110000 + 1 * 37000 + 1 * 21000, enzyme SMPP-1M, 37 kDa catalytic subunit PP1C, 110 kDa regulatory subunit M110 Sus scrofa

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
 72.5 kDa N-terminal fragment of the 110 kDa subunit
-
Sus scrofa
-
 SMPP-1M
-
Sus scrofa SMPP-1M
-
 SMPP-1M
-

Purification (Commentary)

Purification (Comment) Organism
SMPP-1M, subunits M110, M21 and PP1C catalytic subunit Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
aorta fragments of the 110 kDa subunit Rattus norvegicus
-
bladder SMPP-1M Sus scrofa
-
kidney 72.5 kDa N-terminal fragment of the 110 kDa subunit Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information studies with fragments of the 110 kDa subunit on their ability to regulate relaxation and 20 kDa myosin light-chain dephosphorylation of rabbit permeabilized portal vein induced by the catalytic subunit PP1C Rattus norvegicus ?
-
 ?
additional information studies with fragments of the 110 kDa subunit on their ability to regulate relaxation and 20 kDa myosin light-chain dephosphorylation of rabbit permeabilized portal vein induced by the catalytic subunit PP1C Sus scrofa ?
-
 ?
additional information studies with fragments of the 110 kDa subunit on their ability to regulate relaxation and 20 kDa myosin light-chain dephosphorylation of rabbit permeabilized portal vein induced by the catalytic subunit PP1C Sus scrofa SMPP-1M ?
-
 ?
myosin light-chain phosphate + H2O 20 kDa myosin light chain Sus scrofa myosin light-chain + phosphate
-
 ?
myosin light-chain phosphate + H2O 110 kDa/21 kDa complex accelerates dephosphorylation induced by the catalytic subunit PP1C by 1.6fold, the N-terminal sequence 1-309 of the 110 kDa subunit is sufficient to enhance the PP1C activity in muscle Sus scrofa myosin light-chain + phosphate
-
 ?
myosin light-chain phosphate + H2O 20 kDa myosin light chain Sus scrofa SMPP-1M myosin light-chain + phosphate
-
 ?
myosin light-chain phosphate + H2O 110 kDa/21 kDa complex accelerates dephosphorylation induced by the catalytic subunit PP1C by 1.6fold, the N-terminal sequence 1-309 of the 110 kDa subunit is sufficient to enhance the PP1C activity in muscle Sus scrofa SMPP-1M myosin light-chain + phosphate
-
 ?
phosphorylated myosin + H2O
-
 Sus scrofa myosin + phosphate
-
 ?
phosphorylated myosin + H2O
-
 Sus scrofa SMPP-1M myosin + phosphate
-
 ?

Subunits

Subunits Comment Organism
heterotrimer 1 * 110000 + 1 * 37000 + 1 * 21000, enzyme SMPP-1M, 37 kDa catalytic subunit PP1C, 110 kDa regulatory subunit M110 Sus scrofa