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Literature summary 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

EC Number Activating Compound Comment Organism Structure
3.1.3.53 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

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.3.53 myofibril myofibrillar form of smooth muscle myosin light chain phosphatase forms a multienzyme complex with myosin light chain kinase Meleagris gallopavo 30016
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.3.53 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
3.1.3.53 65000
-
 catalytic subunit of KAMPPase, gel filtration Meleagris gallopavo
3.1.3.53 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
3.1.3.53 150000
-
 kinase- and myosin-associated protein phosphatase KAMPPase, gel filtration Meleagris gallopavo

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
2.7.11.18 Gallus gallus
-
-
-
3.1.3.53 Meleagris gallopavo
-
 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
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.11.18
-
 Gallus gallus
3.1.3.53 KAMPPase, copurification of MLCPase and myosin light chain kinase activities, forming a multienzyme complex Meleagris gallopavo

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.11.18 gizzard
-
 Gallus gallus
-
2.7.11.18 smooth muscle
-
 Gallus gallus
-
3.1.3.53 gizzard smooth muscle myofibrillar form of MLCPase Meleagris gallopavo
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.3.53 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 ?
-
 ?
3.1.3.53 additional information together with myosin light chain kinase key regulatory enzyme of smooth muscle Meleagris gallopavo ?
-
 ?
3.1.3.53 myosin light-chain phosphate + H2O
-
 Meleagris gallopavo myosin light-chain + phosphate
-
 ?
3.1.3.53 phosphorylated myosin + H2O
-
 Meleagris gallopavo myosin + phosphate
-
 ?
3.1.3.53 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

EC Number Subunits Comment Organism
2.7.11.18 More multienzyme complex with smooth muscle myosin light chain phosphatase Gallus gallus
3.1.3.53 ? 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]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.3.53 25
-
 assay at Meleagris gallopavo