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Literature summary for 3.1.3.53 extracted from

  • Pato, M.D.; Kerc, E.
    Purification of smooth muscle myosin phosphatase from turkey gizzard (1988), Methods Enzymol., 159, 446-453.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
ATP enzyme SMP-IV is less sensitive than the other enzymes Meleagris gallopavo
diphosphate enzyme SMP-IV is less sensitive than the other enzymes Meleagris gallopavo
NaF enzyme SMP-IV is less sensitive than the other enzymes Meleagris gallopavo

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0015
-
myosin light-chain pH 7, 30°C, enzyme SMP-IV Meleagris gallopavo
0.0059
-
heavy meromyosin pH 7, 30°C, enzyme SMP-IV Meleagris gallopavo

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required by enzyme SMP-II 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
40000
-
x * 58000 + x * 40000, enzyme SMP-IV Meleagris gallopavo
43000
-
1 * 43000, enzyme SMP-II Meleagris gallopavo
55000
-
x * 60000 + x * 55000 + x * 38000, 38 kDa catalytic subunit, ratio 1:1:1, enzyme SMP-I, SDS-PAGE Meleagris gallopavo
58000
-
x * 58000 + x * 40000, enzyme SMP-IV Meleagris gallopavo
60000
-
x * 60000 + x * 55000 + x * 38000, 38 kDa catalytic subunit, ratio 1:1:1, enzyme SMP-I, SDS-PAGE Meleagris gallopavo

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
myosin light-chain phosphate + H2O Meleagris gallopavo reaction is a prerequisite for the actin activation of the myosin Mg2+-ATPase myosin light-chain + phosphate
-
?

Organism

Organism UniProt Comment Textmining
Meleagris gallopavo
-
4 different protein phosphatases are active towards isolated myosin light-chains: SMP-I, SMP-II, SMP-III, SMP-IV
-

Purification (Commentary)

Purification (Comment) Organism
SMP-IV, 2000-6133fold 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
1.6
-
pH 7, 30°C, myosin light-chain, enzyme SMP-IV Meleagris gallopavo
1.84
-
pH 7, 30°C, heavy meromyosin, enzyme SMP-IV Meleagris gallopavo

Storage Stability

Storage Stability Organism
-20°C, enzyme SMP-IV, 20 mM KCl, 20 mM Tris-HCl, pH 7.4, 50% glycerol, 0.1 mM EGTA, 0.1 mM EDTA, 1 mM dithiothreitol, 0.1 mM phenylmethylsulfonyl fluoride, several months, stable Meleagris gallopavo

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
myosin light-chain phosphate + H2O SMP-I, -II, -III and -IV are active Meleagris gallopavo myosin light-chain + phosphate
-
?
myosin light-chain phosphate + H2O reaction is a prerequisite for the actin activation of the myosin Mg2+-ATPase Meleagris gallopavo myosin light-chain + phosphate
-
?
phosphorylated heavy meromyosin + H2O a chymotryptic fragment of myosin, only SMP-III and SMP-IV are active, SMP-I and SMP-II not Meleagris gallopavo heavy meromyosin + phosphate
-
?
phosphorylated myosin + H2O only SMP-III and SMP-IV are active, SMP-I and SMP-II not Meleagris gallopavo myosin + 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
? x * 58000 + x * 40000, enzyme SMP-IV Meleagris gallopavo
monomer 1 * 43000, enzyme SMP-II Meleagris gallopavo

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Meleagris gallopavo

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
assay at Meleagris gallopavo