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Information on EC 3.1.3.53 - [myosin-light-chain] phosphatase

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.3 Phosphoric-monoester hydrolases
                3.1.3.53 [myosin-light-chain] phosphatase
IUBMB Comments
The enzyme is composed of three subunits. The holoenzyme dephosphorylates myosin light chains and EC 2.7.11.18, myosin-light-chain kinase, but not myosin; the catalytic subunit acts on all three substrates.
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This record set is specific for:
UNIPROT: O14974
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Word Map
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
mypt1, myosin phosphatase, mlcp, hek-293 cell, mlc phosphatase, myosin phosphatase target subunit 1, ppp1r12a, myosin phosphatase targeting subunit 1, smpp-1m, smooth muscle myosin phosphatase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
myosin phosphatase
-
myosin phosphatase targeting subunit 1
-
MLCP
-
-
-
-
MLCPase
-
-
-
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MLCPPase
-
-
-
-
MP
-
-
-
-
myosin light chain kinase phosphatase
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-
-
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myosin light chain phosphatase
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-
-
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myosin phosphatase
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-
-
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phosphatase, myosin
-
-
-
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phosphatase, myosin light-chain kinase
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-
-
-
PP-1G
-
-
-
-
PP-1M
-
-
-
-
PP-2A
-
-
-
-
protein phosphatase 2A
-
-
-
-
SMMP
-
-
-
-
smooth muscle myosin phosphatase
-
-
-
-
smooth muscle phosphatase I-IV
-
-
-
-
SMP-I
-
-
-
-
SMP-II
-
-
-
-
SMP-III
-
-
-
-
SMP-IV
-
-
-
-
SMPP
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
[myosin-light-chain]-phosphate phosphohydrolase
The enzyme is composed of three subunits. The holoenzyme dephosphorylates myosin light chains and EC 2.7.11.18, myosin-light-chain kinase, but not myosin; the catalytic subunit acts on all three substrates.
CAS REGISTRY NUMBER
COMMENTARY hide
108658-39-5
-
86417-96-1
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
P-MLC20 + H2O
MLC20 + phosphate
show the reaction diagram
P-MLC20: phospho-peptide mimicking MLC20(3-26:P-Ser19)
-
-
?
phosphorylated myosin + H2O
myosin + phosphate
show the reaction diagram
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Mn2+
at 1 mM inhibitory effect
okadaic acid
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
dephosphorylation activity of myosin phosphatase immunoprecipitated from the apoptotic cells is lower than that from nonapoptotic control cells
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
assay at
25
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
knockdown of MYPT1 does not cause apoptosis in normal HeLa cells but the percentage of TNF/CHX-induced apoptotic cells is increased in MYPT1-depleted cells
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MYPT1_HUMAN
1030
0
115281
Swiss-Prot
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
proteolytic modification
in apoptotic cells, the myosin-binding domain of myosin phosphatase targeting subunit 1 (MYPT1) is cleaved by caspase-3 at Asp-884
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
determination of three-dimensional structure of the 57-residue peptide corresponding to residue 658-714 of myosin phosphatase targeting subunit 1 using multi-dimensional NMR techniques
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DELTA495-1030
using a deletion mutant it is shown that the C-terminal domain of human MYPT1(495-1030) is responsible for the binding to the N-terminal portion of myosin light meromyosin
T696A
substitution of Thr696 with Ala eliminates the phosphorylation-dependent inhibition
T853A
the extent of inhibition of mutant T853A MLCP is indistinguishable from that of wild-type
additional information
expression of the caspase-3 cleaved form of MYPT1 that lacks the C-terminal end in HeLa cells causes the dissociation of MYPT1 from actin stress fibers
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
immobilized metal ion affinity chromatography (Ni2+)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
His-tagged 57-residue peptide corresponding to residue 658-714 of myosin phosphatase targeting subunit 1 expressed in Escherichia coli
MLCP complex (MYPT1-PP1 dimer) is transiently expressed in COS1 cells
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the expression of isovariants PPP1R12A, PPP1R12BLZ+, PPP1R16A and PPP1R16B mRNA is reduced in late pregnancy (not-in-labor) relative to non-pregnancy. PPP1R12ALZ+ and PPP1R12ALZ- mRNA levels are similar in the non-pregnant and pregnant not-in-labor groups. There is a further reduction in the uterine expression of PPP1R12ALZ+, PPP1R12CLZ+ and PPP1R12ALZ- mRNA with labor relative to the pregnant not-in-labor group. PPP1R12A, PPP1R12BLZ+, PPP1R16A and PPP1R16B mRNA levels are invariant between the not in labor and in-labor groups
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
the expression of isovariants PPP1R12A, PPP1R12BLZ+, PPP1R16A and PPP1R16B mRNA is reduced in late pregnancy (not-in-labor) relative to non-pregnancy. PPP1R12ALZ+ and PPP1R12ALZ- mRNA levels are similar in the non-pregnant and pregnant not-in-labor groups. There is a further reduction in the uterine expression of PPP1R12ALZ+, PPP1R12CLZ+ and PPP1R12ALZ- mRNA with labor relative to the pregnant not-in-labor group. PPP1R12A, PPP1R12BLZ+, PPP1R16A and PPP1R16B mRNA levels are invariant between the not in labor and in-labor groups
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mori, S.; Iwaoka, R.; Eto, M.; Ohki, S.
Solution structure of the inhibitory phosphorylation domain of myosin phosphatase targeting subunit 1
Proteins
77
732-735
2009
Homo sapiens (O14974)
Manually annotated by BRENDA team
Khasnis, M.; Nakatomi, A.; Gumpper, K.; Eto, M.
Reconstituted human myosin light chain phosphatase reveals distinct roles of two inhibitory phosphorylation sites of the regulatory subunit, MYPT1
Biochemistry
53
2701-2709
2014
Homo sapiens (O14974), Homo sapiens
Manually annotated by BRENDA team
Iwasaki, T.; Katayama, T.; Kohama, K.; Endo, Y.; Sawasaki, T.
Myosin phosphatase is inactivated by caspase-3 cleavage and phosphorylation of myosin phosphatase targeting subunit 1 during apoptosis
Mol. Biol. Cell
24
748-756
2013
Homo sapiens (O14974), Mus musculus (Q9DBR7)
Manually annotated by BRENDA team
Horvath, D.; Sipos, A.; Major, E.; Konya, Z.; Batori, R.; Dedinszki, D.; Szoell Si, A.; Tamas, I.; Ivan, J.; Kiss, A.; Erd di, F.; Lontay, B.
Myosin phosphatase accelerates cutaneous wound healing by regulating migration and differentiation of epidermal keratinocytes via Akt signaling pathway in human and murine skin
Biochim. Biophys. Acta
1864
3268-3280
2018
Homo sapiens (O14974), Homo sapiens, Mus musculus (Q9DBR7), Mus musculus
Manually annotated by BRENDA team
Lee, E.; Stafford, W.3.
Interaction of myosin phosphatase target subunit (MYPT1) with myosin phosphatase-RhoA interacting protein (MRIP) a role of glutamic acids in the interaction
PLoS One
10
e0139875
2015
Homo sapiens (O14974)
Manually annotated by BRENDA team
Lartey, J.; Taggart, J.; Robson, S.; Taggart, M.
Altered expression of human smooth muscle myosin phosphatase targeting (MYPT) isovariants with pregnancy and labor
PLoS ONE
11
e0164352
2016
Homo sapiens (O14974), Homo sapiens
Manually annotated by BRENDA team