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Literature summary for 3.1.3.53 extracted from

  • Sobieszek, A.; Borkowski, J.; Babiychuk, V.S.
    Purification and characterization of a smooth muscle myosin light chain kinase-phosphatase complex (1997), J. Biol. Chem., 272, 7034-7041.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
additional information telokin facilitates the dissociation of the phosphatase or its catalytic subunit from myosin light chain kinase oligomers increasing the MLCPase activity of the multienzyme complex, but no effect on the activity of the purified MLCPase holoenzyme or its catalytic subunit Meleagris gallopavo

Localization

Localization Comment Organism GeneOntology No. Textmining
myofibril myofibrillar form of smooth muscle myosin light chain phosphatase forms a multienzyme complex with myosin light chain kinase Meleagris gallopavo 30016
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Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
37000
-
x * 37000 + x * 67000, 37 kDa catalytic subunit, 67 kDa targeting subunit binds to the catalytic subunit, to myosin light chain kinase and Ca2+-independently to calmodulin, ratio of subunits 1:2, MLCPase of the multienzyme complex with myosin light chain kinase is named KAMPPase, SDS-PAGE Meleagris gallopavo
65000
-
catalytic subunit of KAMPPase, gel filtration Meleagris gallopavo
67000
-
x * 37000 + x * 67000, 37 kDa catalytic subunit, 67 kDa targeting subunit binds to the catalytic subunit, to myosin light chain kinase and Ca2+-independently to calmodulin, ratio of subunits 1:2, MLCPase of the multienzyme complex with myosin light chain kinase is named KAMPPase, SDS-PAGE Meleagris gallopavo
150000
-
kinase- and myosin-associated protein phosphatase KAMPPase, gel filtration Meleagris gallopavo

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Meleagris gallopavo together with myosin light chain kinase key regulatory enzyme of smooth muscle ?
-
?

Organism

Organism UniProt Comment Textmining
Meleagris gallopavo
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KAMPPase: kinase- and myosin-associated protein phosphatase, a myofibrillar form of smooth muscle myosin light chain phosphatase forms a multienzyme complex with myosin light chain kinase
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Purification (Commentary)

Purification (Comment) Organism
KAMPPase, copurification of MLCPase and myosin light chain kinase activities, forming a multienzyme complex Meleagris gallopavo

Source Tissue

Source Tissue Comment Organism Textmining
gizzard smooth muscle myofibrillar form of MLCPase Meleagris gallopavo
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information KAMPPase: kinase- and myosin-associated protein phosphatase, functional multienzyme complex composed of a myofibrillar form of smooth muscle myosin light chain phosphatase and myosin light chain kinase with or without calmodulin, regulation of the phosphatase activity Meleagris gallopavo ?
-
?
additional information together with myosin light chain kinase key regulatory enzyme of smooth muscle Meleagris gallopavo ?
-
?
myosin light-chain phosphate + H2O
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Meleagris gallopavo myosin light-chain + phosphate
-
?
phosphorylated myosin + H2O
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Meleagris gallopavo myosin + phosphate
-
?
phosphorylated myosin-light chain kinase + H2O autophosphorylated myosin light chain kinase is a good substrate for the kinase- and myosin-associated protein phosphatase KAMPPase Meleagris gallopavo myosin light-chain kinase + phosphate
-
?

Subunits

Subunits Comment Organism
? x * 37000 + x * 67000, 37 kDa catalytic subunit, 67 kDa targeting subunit binds to the catalytic subunit, to myosin light chain kinase and Ca2+-independently to calmodulin, ratio of subunits 1:2, MLCPase of the multienzyme complex with myosin light chain kinase is named KAMPPase, SDS-PAGE Meleagris gallopavo

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Meleagris gallopavo