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Literature summary for 3.1.3.53 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
Search for more literature for 3.1.3.53

Inhibitors

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

KM Value [mM]

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

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
38000
-
 x * 60000 + x * 55000 + x * 38000, 38 kDa catalytic subunit, ratio 1:1:1, enzyme SMP-I, SDS-PAGE Meleagris gallopavo
55000
-
 x * 60000 + x * 55000 + x * 38000, 38 kDa catalytic subunit, ratio 1:1:1, enzyme SMP-I, SDS-PAGE Meleagris gallopavo
60000
-
 x * 60000 + x * 55000 + x * 38000, 38 kDa catalytic subunit, ratio 1:1:1, enzyme SMP-I, SDS-PAGE Meleagris gallopavo
165000
-
 sedimentation equilibrium centrifugation Meleagris gallopavo
230000
-
 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 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 ?
-
 ?
phosphorylated myosin-light chain kinase + H2O Meleagris gallopavo SMP-I modulates the activity of myosin-light chain kinase myosin light-chain kinase + phosphate
-
 ?

Organism

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

Purification (Commentary)

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

Source Tissue

Source Tissue Comment Organism Textmining
gizzard smooth muscle
-
 Meleagris gallopavo
-

Specific Activity [micromol/min/mg]

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

Storage Stability

Storage Stability Organism
-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
-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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
-
 ?
myosin light-chain phosphate + H2O holoenzyme and isolated catalytic subunit are active Meleagris gallopavo myosin light-chain + phosphate
-
 ?
myosin light-chain phosphate + H2O 20 kDa myosin light chain Meleagris gallopavo myosin light-chain + phosphate
-
 ?
phosphorylated myosin + H2O catalytic subunit is active, holoenzyme not Meleagris gallopavo myosin + phosphate
-
 ?
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
-
 ?
phosphorylated myosin-light chain kinase + H2O SMP-I modulates the activity of myosin-light chain kinase Meleagris gallopavo myosin light-chain kinase + phosphate
-
 ?

Subunits

Subunits Comment Organism
? x * 60000 + x * 55000 + x * 38000, 38 kDa catalytic subunit, ratio 1:1:1, enzyme SMP-I, SDS-PAGE Meleagris gallopavo

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at, dephosphorylation of myosin light chain kinase in presence or absence of calmodulin bound to the kinase Meleagris gallopavo
30
-
 assay at Meleagris gallopavo

pH Optimum

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

Ki Value [mM]

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