BRENDA - Enzyme Database

Interaction of smooth muscle myosin phosphatase with phospholipids

Ito, M.; Feng, J.; Tsujino, S.; Inagaki, N.; Inagaki, M.; Tanaka, J.; Ichikawa, K.; Hartshorne, D.J.; Nakano, T.; Biochemistry 36, 7607-7614 (1997)

Data extracted from this reference:

Cloned(Commentary)
EC Number
Commentary
Organism
3.1.3.53
cDNAs encoding the 133 kDa myosin-binding subunit and the 20 kDa regulatory subunit are cloned and expressed in Escherichia coli BL21(DE3)
Gallus gallus
Engineering
EC Number
Amino acid exchange
Commentary
Organism
3.1.3.53
additional information
mutants of the 133 kDa myosin-binding subunit
Gallus gallus
Inhibitors
EC Number
Inhibitors
Commentary
Organism
Structure
3.1.3.53
acidic phospholipid
interaction of enzyme with acidic phospholipids inhibits activity toward phosphorylated myosin
Gallus gallus
3.1.3.53
okadaic acid
potent inhibitor of PP-1 and PP-2A
Gallus gallus
3.1.3.53
phosphatidic acid
most effective inhibitor among acidic phospholipids, followed by phosphatidylserine and phosphatidylinositol, phosphorylated myosin as substrate
Gallus gallus
3.1.3.53
phosphatidylinositol
phosphatidic acid is the most effective inhibitor among acidic phospholipids, followed by phosphatidylserine and phosphatidylinositol, phosphorylated myosin as substrate
Gallus gallus
3.1.3.53
phosphatidylserine
phosphatidic acid is the most effective inhibitor among acidic phospholipids, followed by phosphatidylserine and phosphatidylinositol, phosphorylated myosin as substrate
Gallus gallus
Localization
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
3.1.3.53
cytosol
133 kDa myosin-binding subunit
Rattus norvegicus
5829
-
3.1.3.53
membrane
enzyme may interact with membranes, phosphorylation by protein kinase A may modify interaction, distribution of the 130/133 kDa myosin-binding subunit at the membrane
Gallus gallus
16020
-
3.1.3.53
plasma membrane
133 kDa myosin-binding subunit
Rattus norvegicus
5886
-
Molecular Weight [Da]
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
3.1.3.53
20000
-
x * 130000 + x * 38000 + x * 20000, 130 kDa regulatory myosin-binding subunit, 38 kDa catalytic subunit, 20 kDa regulatory subunit, SDS-PAGE
Gallus gallus
3.1.3.53
38000
-
x * 130000 + x * 38000 + x * 20000, 130 kDa regulatory myosin-binding subunit, 38 kDa catalytic subunit, 20 kDa regulatory subunit, SDS-PAGE
Gallus gallus
3.1.3.53
130000
-
x * 130000 + x * 38000 + x * 20000, 130 kDa regulatory myosin-binding subunit, 38 kDa catalytic subunit, 20 kDa regulatory subunit, SDS-PAGE
Gallus gallus
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
3.1.3.53
Gallus gallus
-
-
-
3.1.3.53
Rattus norvegicus
-
-
-
Posttranslational Modification
EC Number
Posttranslational Modification
Commentary
Organism
3.1.3.53
phosphoprotein
130/133 kDa myosin-binding subunits M130/M133 and 20 kDa regulatory subunit M20 are phosphorylated by protein kinase A to 3 and 1 mol phosphate/mol of subunit, phosphorylation of holoenzyme decreases phospholipid binding, M130/133: C-terminal phosphorylation site involved in regulation of phospholipid binding, no phosphorylation of the catalytic subunit PP-1cdelta, protein kinase C also phosphorylates M130/M133 and M20, but no effect on binding of phospholipids
Gallus gallus
3.1.3.53
phosphoprotein
-
Rattus norvegicus
Purification (Commentary)
EC Number
Commentary
Organism
3.1.3.53
native holoenzyme; recombinant 133 kDa myosin-binding subunit and 20 kDa regulatory subunit, expressed in Escherichia coli
Gallus gallus
Source Tissue
EC Number
Source Tissue
Commentary
Organism
Textmining
3.1.3.53
gizzard
-
Gallus gallus
-
3.1.3.53
REF-52 cell
rat embryonic fibroblast cells, mitotic, 133 kDa myosin-binding subunit
Rattus norvegicus
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3.1.3.53
additional information
-
646357
Rattus norvegicus
?
-
-
-
-
3.1.3.53
additional information
enzyme binds to vesicles of acidic phospholipids, i.e. phosphatidylserine, phosphatidylinositol and phosphatidic acid, but not to neutral phospholipids, phosphatidylserine binding decreases by increasing ionic strength and Mg2+ concentration, phospholipid binding is associated with the C-terminal part of the 130/133 kDa myosin-binding subunit and the 20 kDa regulatory subunit
646357
Gallus gallus
?
-
-
-
-
3.1.3.53
myosin light-chain phosphate + H2O
-
646357
Gallus gallus
myosin light-chain + phosphate
-
646357
Gallus gallus
?
3.1.3.53
phosphorylated myosin + H2O
-
646357
Gallus gallus
myosin + phosphate
-
646357
Gallus gallus
?
Subunits
EC Number
Subunits
Commentary
Organism
3.1.3.53
?
x * 130000 + x * 38000 + x * 20000, 130 kDa regulatory myosin-binding subunit, 38 kDa catalytic subunit, 20 kDa regulatory subunit, SDS-PAGE
Gallus gallus
Temperature Optimum [C]
EC Number
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
3.1.3.53
30
-
assay at
Gallus gallus
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
3.1.3.53
cDNAs encoding the 133 kDa myosin-binding subunit and the 20 kDa regulatory subunit are cloned and expressed in Escherichia coli BL21(DE3)
Gallus gallus
Engineering (protein specific)
EC Number
Amino acid exchange
Commentary
Organism
3.1.3.53
additional information
mutants of the 133 kDa myosin-binding subunit
Gallus gallus
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
3.1.3.53
acidic phospholipid
interaction of enzyme with acidic phospholipids inhibits activity toward phosphorylated myosin
Gallus gallus
3.1.3.53
okadaic acid
potent inhibitor of PP-1 and PP-2A
Gallus gallus
3.1.3.53
phosphatidic acid
most effective inhibitor among acidic phospholipids, followed by phosphatidylserine and phosphatidylinositol, phosphorylated myosin as substrate
Gallus gallus
3.1.3.53
phosphatidylinositol
phosphatidic acid is the most effective inhibitor among acidic phospholipids, followed by phosphatidylserine and phosphatidylinositol, phosphorylated myosin as substrate
Gallus gallus
3.1.3.53
phosphatidylserine
phosphatidic acid is the most effective inhibitor among acidic phospholipids, followed by phosphatidylserine and phosphatidylinositol, phosphorylated myosin as substrate
Gallus gallus
Localization (protein specific)
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
3.1.3.53
cytosol
133 kDa myosin-binding subunit
Rattus norvegicus
5829
-
3.1.3.53
membrane
enzyme may interact with membranes, phosphorylation by protein kinase A may modify interaction, distribution of the 130/133 kDa myosin-binding subunit at the membrane
Gallus gallus
16020
-
3.1.3.53
plasma membrane
133 kDa myosin-binding subunit
Rattus norvegicus
5886
-
Molecular Weight [Da] (protein specific)
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
3.1.3.53
20000
-
x * 130000 + x * 38000 + x * 20000, 130 kDa regulatory myosin-binding subunit, 38 kDa catalytic subunit, 20 kDa regulatory subunit, SDS-PAGE
Gallus gallus
3.1.3.53
38000
-
x * 130000 + x * 38000 + x * 20000, 130 kDa regulatory myosin-binding subunit, 38 kDa catalytic subunit, 20 kDa regulatory subunit, SDS-PAGE
Gallus gallus
3.1.3.53
130000
-
x * 130000 + x * 38000 + x * 20000, 130 kDa regulatory myosin-binding subunit, 38 kDa catalytic subunit, 20 kDa regulatory subunit, SDS-PAGE
Gallus gallus
Posttranslational Modification (protein specific)
EC Number
Posttranslational Modification
Commentary
Organism
3.1.3.53
phosphoprotein
130/133 kDa myosin-binding subunits M130/M133 and 20 kDa regulatory subunit M20 are phosphorylated by protein kinase A to 3 and 1 mol phosphate/mol of subunit, phosphorylation of holoenzyme decreases phospholipid binding, M130/133: C-terminal phosphorylation site involved in regulation of phospholipid binding, no phosphorylation of the catalytic subunit PP-1cdelta, protein kinase C also phosphorylates M130/M133 and M20, but no effect on binding of phospholipids
Gallus gallus
3.1.3.53
phosphoprotein
-
Rattus norvegicus
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
3.1.3.53
native holoenzyme; recombinant 133 kDa myosin-binding subunit and 20 kDa regulatory subunit, expressed in Escherichia coli
Gallus gallus
Source Tissue (protein specific)
EC Number
Source Tissue
Commentary
Organism
Textmining
3.1.3.53
gizzard
-
Gallus gallus
-
3.1.3.53
REF-52 cell
rat embryonic fibroblast cells, mitotic, 133 kDa myosin-binding subunit
Rattus norvegicus
-
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3.1.3.53
additional information
-
646357
Rattus norvegicus
?
-
-
-
-
3.1.3.53
additional information
enzyme binds to vesicles of acidic phospholipids, i.e. phosphatidylserine, phosphatidylinositol and phosphatidic acid, but not to neutral phospholipids, phosphatidylserine binding decreases by increasing ionic strength and Mg2+ concentration, phospholipid binding is associated with the C-terminal part of the 130/133 kDa myosin-binding subunit and the 20 kDa regulatory subunit
646357
Gallus gallus
?
-
-
-
-
3.1.3.53
myosin light-chain phosphate + H2O
-
646357
Gallus gallus
myosin light-chain + phosphate
-
646357
Gallus gallus
?
3.1.3.53
phosphorylated myosin + H2O
-
646357
Gallus gallus
myosin + phosphate
-
646357
Gallus gallus
?
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
3.1.3.53
?
x * 130000 + x * 38000 + x * 20000, 130 kDa regulatory myosin-binding subunit, 38 kDa catalytic subunit, 20 kDa regulatory subunit, SDS-PAGE
Gallus gallus
Temperature Optimum [C] (protein specific)
EC Number
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
3.1.3.53
30
-
assay at
Gallus gallus