Literature summary for 3.1.3.53 extracted from

Koga, Y.; Ikebe, M.
A novel regulatory mechanism of myosin light chain phosphorylation via binding of 14-3-3 to myosin phosphatase (2007), Mol. Biol. Cell, 19, 1062-1071.

Search for more literature for 3.1.3.53

Cloned(Commentary)

Cloned (Comment)	Organism
of MYPT1 in yeast AH109 strain for yeast two hybrid screening, MLCP holoenzyme in Sf9 cells by coinfection of rat His MYPT1, Flag MYPT1, rat PP1delta, and rat M21 expressing viruses, transfection of COS7 or NIH3T3 cells	Rattus norvegicus

Protein Variants

Protein Variants	Comment	Organism
additional information	deletion of the C-terminal residues of MYPT1 at codon 39, 172, 297 and 517 by site directed mutagenesis	Rattus norvegicus

Inhibitors

Inhibitors	Comment	Organism	Structure
14-3-3beta protein	70% inhibition in the presence of 0.5 mM 14-3-3beta, dissociates MLCP from myosin II	Rattus norvegicus
additional information	MLCP holoenzyme is inhibited by binding of 14-3-3beta protein to MYPT1, 14-3-3beta protein diminishes the binding between MYPT1 and myosin II, and abolishes MYPT1 localization at stress fibers	Rattus norvegicus

Organism

Organism	UniProt	Comment	Textmining
Rattus norvegicus	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
Flag MYPT1 using anti-Flag affinity chromatography, His tagged proteins by Ni-NTA chromatography	Rattus norvegicus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
myosin light-chain phosphate + H2O	muscle	Rattus norvegicus	myosin light-chain + phosphate	-	?

Subunits

Subunits	Comment	Organism
More	MLCP is a heterotrimer composed of the catalytic subunit belonging to protein phosphatase 1c PPC1, the myosin phosphatase targeting subunit MYPT1, and M21	Rattus norvegicus

Synonyms

Synonyms	Comment	Organism
mLC phosphatase	-	Rattus norvegicus
MLCP	-	Rattus norvegicus
myosin light chain phosphatase	-	Rattus norvegicus
MYPT1	-	Rattus norvegicus

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)