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Literature summary extracted from

  • Pato, M.D.; Adelstein, R.S.
    Purification and characterization of a multisubunit phosphatase from turkey gizzard smooth muscle. The effect of calmodulin binding to myosin light chain kinase on dephosphorylation (1983), J. Biol. Chem., 258, 7047-7054.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.3.53 ADP SMP-I, catalytic subunit is more sensitive than holoenzyme Meleagris gallopavo
3.1.3.53 AMP SMP-I, catalytic subunit is more sensitive than holoenzyme Meleagris gallopavo
3.1.3.53 ATP SMP-I, catalytic subunit is more sensitive than holoenzyme Meleagris gallopavo
3.1.3.53 Ca2+ partial inhibition of SMP-I, only with myosin light chain as substrate Meleagris gallopavo
3.1.3.53 dephosphorylated myosin light chain SMP-I, product inhibition Meleagris gallopavo
3.1.3.53 diphosphate SMP-I, catalytic subunit is more sensitive than holoenzyme, most potent inhibitor among the phosphate analogs Meleagris gallopavo
3.1.3.53 KCl at high concentrations Meleagris gallopavo
3.1.3.53 Mg2+ partial inhibition of SMP-I, only with myosin light chain as substrate Meleagris gallopavo
3.1.3.53 NaF at high concentrations Meleagris gallopavo
3.1.3.53 phosphate SMP-I, holoenzyme and catalytic subunit, product inhibition Meleagris gallopavo

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.3.53 0.01
-
 myosin light-chain pH 7, 30°C, SMP-I holoenzyme Meleagris gallopavo
3.1.3.53 0.05
-
 myosin light-chain pH 7, 30°C, catalytic subunit of SMP-I Meleagris gallopavo

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.3.53 38000
-
 x * 60000 + x * 55000 + x * 38000, 38 kDa catalytic subunit, ratio 1:1:1, enzyme SMP-I, SDS-PAGE Meleagris gallopavo
3.1.3.53 55000
-
 x * 60000 + x * 55000 + x * 38000, 38 kDa catalytic subunit, ratio 1:1:1, enzyme SMP-I, SDS-PAGE Meleagris gallopavo
3.1.3.53 60000
-
 x * 60000 + x * 55000 + x * 38000, 38 kDa catalytic subunit, ratio 1:1:1, enzyme SMP-I, SDS-PAGE Meleagris gallopavo
3.1.3.53 165000
-
 sedimentation equilibrium centrifugation Meleagris gallopavo
3.1.3.53 230000
-
 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 two forms of SMP-I, the intact form and the catalytic subunit, may act in an opposite manner to regulate smooth muscle contraction in vivo ?
-
 ?
3.1.3.53 phosphorylated myosin-light chain kinase + H2O Meleagris gallopavo SMP-I modulates the activity of myosin-light chain kinase myosin light-chain kinase + phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.53 Meleagris gallopavo
-
 smooth muscle phosphatase I, i.e. SMP-I
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.3.53 SMP-I, holoenzyme and 38 kDa catalytic subunit Meleagris gallopavo

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.3.53 gizzard smooth muscle
-
 Meleagris gallopavo
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.1.3.53 additional information
-
-
 Meleagris gallopavo
3.1.3.53 4 7.7 pH 7, 30°C, myosin light-chain, enzyme SMP-I Meleagris gallopavo

Storage Stability

EC Number Storage Stability Organism
3.1.3.53 -20°C, enzyme SMP-I, 20 mM KCl, 20 mM Tris-HCl, pH 7.4, 50% glycerol, 0.5 mM EGTA, 0.5 mM EDTA, 1 mM dithiothreitol, at least 1 year, stable Meleagris gallopavo
3.1.3.53 -70°C, enzyme SMP-I, 1 M KCl, 20 mM Tris-HCl, pH 7.4, 0.5 mM EGTA, 0.5 mM EDTA, 1 mM dithiothreitol, at least 1 year, stable Meleagris gallopavo

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.3.53 additional information two forms of SMP-I, the intact form and the catalytic subunit, may act in an opposite manner to regulate smooth muscle contraction in vivo Meleagris gallopavo ?
-
 ?
3.1.3.53 myosin light-chain phosphate + H2O holoenzyme and isolated catalytic subunit are active Meleagris gallopavo myosin light-chain + phosphate
-
 ?
3.1.3.53 myosin light-chain phosphate + H2O 20 kDa myosin light chain Meleagris gallopavo myosin light-chain + phosphate
-
 ?
3.1.3.53 phosphorylated myosin + H2O catalytic subunit is active, holoenzyme not Meleagris gallopavo myosin + phosphate
-
 ?
3.1.3.53 phosphorylated myosin-light chain kinase + H2O holoenzyme and isolated catalytic subunit are active, phosphorylated at 2 sites, in absence of bound calmodulin rapid dephosphorylation at both sites, in presence of bound calmodulin dephosphorylation of only one site Meleagris gallopavo myosin light-chain kinase + phosphate
-
 ?
3.1.3.53 phosphorylated myosin-light chain kinase + H2O SMP-I modulates the activity of myosin-light chain kinase Meleagris gallopavo myosin light-chain kinase + phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.3.53 ? x * 60000 + x * 55000 + x * 38000, 38 kDa catalytic subunit, ratio 1:1:1, enzyme SMP-I, 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, dephosphorylation of myosin light chain kinase in presence or absence of calmodulin bound to the kinase Meleagris gallopavo
3.1.3.53 30
-
 assay at Meleagris gallopavo

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.3.53 7
-
 dephosphorylation of intact myosin or isolated myosin light-chain by the catalytic subunit Meleagris gallopavo
3.1.3.53 7.5
-
 dephosphorylation of myosin light-chain by the holoenzyme Meleagris gallopavo

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.1.3.53 0.0115
-
 dephosphorylated myosin light chain pH 7, 30°C, SMP-I Meleagris gallopavo
3.1.3.53 1.5
-
 phosphate pH 7, 30°C, SMP-I Meleagris gallopavo