Information on EC 3.6.4.1 - myosin ATPase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.6.4.1
-
RECOMMENDED NAME
GeneOntology No.
myosin ATPase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + H2O = ADP + phosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphonic ester
-
-
-
-
hydrolysis of phosphoric ester
SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (actin-translocating)
Proteins of the contractile apparatus of muscle and nonmuscle cells; myosin molecule consists of two heavy chains (about 200 kDa) and two pairs of light chains (15-27 kDa). The head region of the heavy chain contains actin- and ATP-binding sites. ATP hydrolysis provides energy for actomyosin contraction.
CAS REGISTRY NUMBER
COMMENTARY hide
9000-83-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
nematode
-
-
Manually annotated by BRENDA team
guinea pig
-
-
Manually annotated by BRENDA team
Lethocerus griseus
giant waterbug
-
-
Manually annotated by BRENDA team
giant waterbug
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
turkey
-
-
Manually annotated by BRENDA team
mouse
-
-
Manually annotated by BRENDA team
pig
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + H2O
ADP + phosphate
show the reaction diagram
ATP + H2O + actin
ADP + phosphate + actin
show the reaction diagram
-
-
-
-
?
CTP + H2O
CDP + phosphate
show the reaction diagram
CTP + H2O + actin
CDP + phosphate + actin
show the reaction diagram
-
-
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
?
gTP + H2O + actin
GDP + phosphate + actin
show the reaction diagram
-
-
-
-
?
ITP + H2O
IDP + phosphate
show the reaction diagram
-
-
-
?
ITP + H2O + actin
IDP + phosphate + actin
show the reaction diagram
-
-
-
-
?
TTP + H2O + actin
TDP + phosphate + actin
show the reaction diagram
-
-
-
-
?
UTP + H2O
UDP + phosphate
show the reaction diagram
-
-
-
?
UTP + H2O + actin
UDP + phosphate + actin
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + H2O
ADP + phosphate
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
-
activates
Ni2+
-
activates
Sr2+
-
activates
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(S)-(-)-blebbistatin
-
-
-
(S)-(2)-blebbistatin
-
-
-
1-(4-methoxyphenyl)-2-phenyl-1H-pyrrole
-
-
2,3,4-tribromo-5-(2-methoxyphenyl)-1-methyl-1H-pyrrole
-
-
2,3,4-tribromo-5-(3,5-dibromo-2-hydroxyphenyl)-1-methyl-1H-pyrrole
-
-
2,3,4-tribromo-5-(3,5-dibromo-2-methoxyphenyl)-1H-pyrrole
2,3,4-tribromo-5-(3,5-dichloro-2-hydroxyphenyl)-1H-pyrrole
-
-
2,3,4-tribromo-5-(3,5-dichloro-2-methoxyphenyl)pyrrole
-
-
2,3,4-tribromo-5-(3,5-difluoro-2-hydroxyphenyl)-1H-pyrrole
-
-
2,3,4-tribromo-5-(3,5-difluoro-2-methoxyphenyl)-1H-pyrrole
-
-
2,3,4-trichloro-5-(2-methoxyphenyl)-1H-pyrrole
-
-
2,3,4-trichloro-5-(3,5-dichloro-2-methoxyphenyl)-1H-pyrrole
2,3,4-triiodo-5-(3,5-dichloro-2-methoxyphenyl)pyrrole
-
-
2,3,4-triiodo-5-(3,5-difluoro-2-methoxyphenyl)-1H-pyrrole
-
-
2,3-butanedione monoxime
-
reversible
2,4,6-Trinitrobenzene sulfonate
2,4-dibromo-6-(3,4,5-tribromo-1-methyl-1H-pyrrol-2-yl)phenol
-
2,4-dibromo-6-(3,4,5-tribromo-1H-pyrrol-2-yl)phenol
-
2,4-dichloro-6-(3,4,5-tribromo-1H-pyrrol-2-yl)phenol
-
2,4-dichloro-6-(3,4,5-trichloro-1H-pyrrol-2-yl)phenol
-
2,4-dichloro-6-(3,4,5-triiodo-1H-pyrrol-2-yl)phenol
-
-
2,4-difluoro-6-(3,4,5-triiodo-1H-pyrrol-2-yl)phenol
-
-
2-(2-hydroxyphenyl)-1-methyl-1H-pyrrole
-
-
2-(2-hydroxyphenyl)-1H-pyrrole
-
-
2-(2-methoxyphenyl)-1-(p-tolylsulfonyl)-2,3-dihydro-1H-pyrrole
-
-
2-(2-methoxyphenyl)-1-(p-tolylsulfonyl)-2,5-dihydro-1H-pyrrole
-
-
2-(2-methoxyphenyl)-1-methyl-1H-pyrrole
-
-
2-(2-methoxyphenyl)-1H-pyrrole
-
-
2-(3,4,5-tribromo-1-methyl-1H-pyrrol-2-yl)phenol
-
2-(3,5-dibromo-2-methoxyphenyl)-1-(p-tolylsulfonyl)-2,3-dihydro-1H-pyrrole
-
-
2-(3,5-dibromo-2-methoxyphenyl)-1-(p-tolylsulfonyl)-2,5-dihydro-1H-pyrrole
-
-
2-(3,5-dibromo-2-methoxyphenyl)-1H-pyrrole
-
-
2-(3,5-dichloro-2-methoxyphenyl)-1-(p-tolylsulfonyl)-2,3-dihydro-1H-pyrrole
-
-
2-(3,5-dichloro-2-methoxyphenyl)-1-(p-tolylsulfonyl)-2,5-dihydro-1H-pyrrole
-
-
2-(3,5-dichloro-2-methoxyphenyl)-1H-pyrrole
-
-
2-(3,5-difluoro-2-methoxyphenyl)-1-(4-methylbenzene-1-sulfonyl)-2,5-dihydro-1H-pyrrole
-
-
2-(3,5-difluoro-2-methoxyphenyl)-1-(p-tolylsulfonyl)-2,3-dihydro-1H-pyrrole
-
-
2-(3,5-difluoro-2-methoxyphenyl)-1H-pyrrole
-
-
2-Methoxybenzaldehyde
-
-
3,5-dibromo-2-methoxybenzaldehyde
-
-
3,5-dichloro-2-methoxybenzaldehyde
-
-
3,5-difluoro-2-methoxybenzaldehyde
-
-
3-morpholinosydnonimine
-
-
4-methoxy-N-[1-phenyl-4-(trimethylsilyl)but-3-yn-1-yl]aniline
-
-
acetone
ADP
-
competitive inhibition
AlF4-
-
phosphate analogue
BeFx
-
phosphate analogue
-
blebbistatin
-
100 micromol reduces appearance of new graded polarity (actomyosin) bundles within the lamella 10-fold
caldesmon
calponin
-
25% inhibition in the presence of actin, calmodulin abolishes inhibitory effect
-
cardiac myosin binding protein-C
-
reduces actin filament velocity in concentration-dependent manner: 200 nM cMYBP-C to around 25%, 400 nM cMYBP-C to almost 0%
-
D2O
-
about 50% inhibition of enzyme, increase in maximum isometric force P0 by about 20%
decavanadate
-
-
Fluorescein 5'-isothiocyanate
-
90% of enzyme activity is lost with the incorporation of 2.6 mol of reagent /mol of myosin, fluorescent label is mainly incorporated into the myosin heavy chain
heparin
-
heparins of molecular weights from 1.75 kDa to 11.6 kDa are competitive inhibitors
HgCl2
-
uncompetitive, 50 nM, 15% inhibition, 400 nM, 80% inhibition, DTT or glutathione protect, full activity is restored by 500 nM DTT or glutathione
KF
-
in the presence of fluoride Mg2+ and MgADP- form a stable S1-MgADP-MgFx complex, that traps the active site of S 1, Mg2+ may occupy the gamma-phosphate position in the ATP binding site of S 1
myosin
-
aging results in chemical changes in myosin (probably oxidation of cysteines) that have inhibitory effects on the actin-activated myosin ATPase
-
N-(2-methoxybenzylidene)-4-methylbenzenesulfonamide
-
-
N-(3,5-dibromo-2-methoxybenzylidene)-4-methylbenzenesulfonamide
-
-
N-(3,5-dichloro-2-methoxybenzylidene)-4-methylbenzenesulfonamide
-
-
N-(3,5-difluoro-2-methoxybenzylidene)-4-methylbenzenesulfonamide
-
-
N-benzyl-p-toluenesulfonamide
N-ethylmaleimide
-
in the absence of divalent cations and in the presence of K+ ions
N-[1-(2-methoxyphenyl)-4-(trimethylsilyl)but-3-ynyl]-4-methylbenzenesulfonamide
-
-
N-[1-(2-methoxyphenyl)-but-3-ynyl]-4-methylbenzenesulfonamide
-
-
N-[1-(2-methoxyphenyl)buta-2,3-dienyl]-4-methylbenzenesulfonamide
-
-
N-[1-(3,5-dibromo-2-methoxyphenyl)-2-(trimethylsilyl)buta-2,3-dienyl]-4-methylbenzenesulfonamide
-
-
N-[1-(3,5-dibromo-2-methoxyphenyl)-4-(trimethylsilyl)but-3-ynyl]-4-methylbenzenesulfonamide
-
-
N-[1-(3,5-dibromo-2-methoxyphenyl)-but-3-ynyl]-4-methylbenzenesulfonamide
-
-
N-[1-(3,5-dibromo-2-methoxyphenyl)buta-2,3-dienyl]-4-methylbenzenesulfonamide
-
-
N-[1-(3,5-dichloro-2-methoxyphenyl)-2-(trimethylsilyl)buta-2,3-dienyl]-4-methylbenzenesulfonamide
-
-
N-[1-(3,5-dichloro-2-methoxyphenyl)-4-(trimethylsilyl)but-3-ynyl]-4-methylbenzenesulfonamide
-
-
N-[1-(3,5-dichloro-2-methoxyphenyl)-but-3-ynyl]-4-methylbenzenesulfonamide
-
-
N-[1-(3,5-dichloro-2-methoxyphenyl)buta-2,3-dienyl]-4-methylbenzenesulfonamide
-
-
N-[1-(3,5-difluoro-2-methoxyphenyl)-2-(trimethylsilyl)buta-2,3-dienyl]-4-methylbenzenesulfonamide
-
-
N-[1-(3,5-difluoro-2-methoxyphenyl)-4-(trimethylsilyl)but-3-ynyl]-4-methylbenzenesulfonamide
-
-
N-[1-(3,5-difluoro-2-methoxyphenyl)-but-3-ynyl]-4-methylbenzenesulfonamide
-
-
N-[1-(3,5-difluoro-2-methoxyphenyl)buta-2,3-dien-1-yl]-4-methylbenzene-1-sulfonamide
-
-
N-[1-(methoxyphenyl)-2-(trimethylsilyl)-buta-2,3-dienyl]-4-methylbenzenesulfonamide
-
-
p-mercuribenzoate
-
enzyme activity increases until 40% of SH-groups are titrated, complete inhibition when all SH-groups are titrated
p-Mercuriphenyl sulfonate
-
enzyme activity increases until 40% of SH-groups are titrated, complete inhibition when all SH-groups are titrated
Pb(CH3COO)2
-
100 micromol lead acetate reduces myosin Ca2+ ATPase activity by 25%
pentabromopseudilin
-
-
pentachloropseudilin
-
-
peroxynitrite
-
-
phenylmercuric acetate
-
enzyme activity increases until 40% of SH-groups are titrated, complete inhibition when all SH-groups are titrated
ScFx
-
phosphate analogue
-
succinic acid
-
-
tropomyosin
Troponin
-
troponin together with tropomyosin inhibits the actomyosin ATPase activity in vitro
-
vanadate
VO43-
-
phosphate analog, binds in solution to myosin and inhibits its ATPase, forming a stable inactive myosin-ADP-VO43- complex (rate constant of ADP and orthovanadate dissociation about 0.00001 s-1)
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetic acid
-
0.030 mM
arachidonic acid
-
0.0503 mM half-maximal effective concentration, 0.0263 mM half-maximal effective concentration in the presence of actin
Caffeine
-
increase in enzyme activity by 4% for non-failing, 11% for idiopathic and 10% ischemic cardiomyopathic hearts
caldesmon
-
in the absence of actin
calponin
-
1.2fold increase in myosin ATPase activity in the absence of actin
-
cystein ethyl ester
-
-
D-malic acid
-
0.025 - 0.050 mM
dioxane
DPI201-206
-
increase in enzyme activity by less than 5% for all preparations
F-actin
-
glycolic acid
-
0.030 mM
L-lactic acid
-
L-lactic acid is more effective than D-lactic acid
L-Malic acid
-
0.025 - 0.050 mM
malonic acid
-
0.030 mM
MCI-154
-
increase in enzyme activity by 11% for non-failing, 19% for idiopathic and 24% ischemic cardiomyopathic hearts
myorod
-
N-ethylmaleimide
-
Ca2+-activated ATPase
oxalic acid
-
0.030 mM
oxaloacetic acid
-
0.030 mM
phalloidin F-actin
-
up to 6.8fold, fast muscle myosin, up to 2.27fold, slow muscle myosin
-
polylysine
-
activation may be related to transition from 10 S to 6 S form of myosin ATPase conformation
Pyruvic acid
-
0.030 mM
S-beta-aminoethylisothiuronium
-
-
additional information
-
myosin II seems to be activated by a rapid actin-linked mechanism rather than slow myosin light chain phosphorylation
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00000027 - 0.00028
actin
0.0001 - 0.428
ATP
0.11
CTP
-
pH 7.6, 25°C
0.5
GTP
-
pH 7.6, 25°C
1
ITP
-
pH 7.6, 25°C
0.25
TTP
-
pH 7.6, 25°C
0.2
UTP
-
pH 7.6, 25°C
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00892 - 20
ATP
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00027
decavanadate
-
ATPase activity of the actomyosin complex
0.0002
HgCl2
-
pH 7.0, 30°C
0.00027
vanadate
-
25°C, pH 7.0
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0919
2,3,4-tribromo-5-(3,5-dibromo-2-methoxyphenyl)-1H-pyrrole
Dictyostelium discoideum
P08799
pH not specified in the publication, 25°C
0.2745
2,3,4-trichloro-5-(3,5-dichloro-2-methoxyphenyl)-1H-pyrrole
Dictyostelium discoideum
P08799
pH not specified in the publication, 25°C
0.1254
2,4-dibromo-6-(3,4,5-tribromo-1-methyl-1H-pyrrol-2-yl)phenol
Dictyostelium discoideum
P08799
pH not specified in the publication, 25°C
0.0244
2,4-dibromo-6-(3,4,5-tribromo-1H-pyrrol-2-yl)phenol
Dictyostelium discoideum
P08799
pH not specified in the publication, 25°C
0.0472
2,4-dichloro-6-(3,4,5-tribromo-1H-pyrrol-2-yl)phenol
Dictyostelium discoideum
P08799
pH not specified in the publication, 25°C
0.1263
2,4-dichloro-6-(3,4,5-trichloro-1H-pyrrol-2-yl)phenol
Dictyostelium discoideum
P08799
pH not specified in the publication, 25°C
0.1822
2-(3,4,5-tribromo-1-methyl-1H-pyrrol-2-yl)phenol
Dictyostelium discoideum
P08799
pH not specified in the publication, 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0003
-
substrate UTP, basal myosin ATPase, 0.6 M KCl, 2 mM MgCl2, pH 7
0.001
-
in the absence of actin
0.003
-
substrate ATP, basal myosin ATPase, 0.6 M KCl, 2 mM MgCl2, pH 7
0.004
-
substrate CTP, basal myosin ATPase, 0.6 M KCl, 2 mM MgCl2, pH 7
0.007
-
substrate GTP, basal myosin ATPase, 0.6 M KCl, 2 mM MgCl2, pH 7
0.027
-
actin and light chain kinase activated, phosphorylation of myosin is Ca2+ and Calmodulin-dependent
0.03
-
conduction system, in the absence of actin
0.05
-
myosin B, Ca2+-ATPase, 0.5 M KCl
0.06
-
myosin B, EDTA-ATPase, 0.5 M KCl
0.07
-
activation with polylysine
0.11
-
activity value of the semimembranous muscles from rats that are hindlimb unloaded for 2 wk, resting; activity value of the semimembranous muscles from rats that are hindlimb unloaded for 3 wk, resting; semimembranous muscles, resting
0.13
-
soleus muscles, resting
0.15
-
ventricular tissue, in the absence of actin
0.18
-
K+(EDTA)-ATPase, isoenzyme V1
0.28
-
Ca-ATPase activity, isoenzyme V3
0.3
-
soleus muscles, Ca2+-activated
0.34
-
80 weeks old rats, activity decreases with age, Ca2+activated ATPase
0.35
-
30 weeks old rats, Ca2+activated ATPase
0.4
-
diaphragm, increasing enzyme activity in cold stressed rats
0.5
-
control; rats treated with ouabain for 3 days
0.517
-
rats treated with ouabain for 7 days
0.638
-
rats treated with ouabain for 30 days
0.65
-
semimembranous muscles, Ca2+-activated
0.66
-
activity value of the semimembranous muscles from rats that are cage control, Ca2+-activated
0.67
-
activity value of the semimembranous muscles from rats that are hindlimb unloaded for 2 wk, Ca2+-activated; activity value of the semimembranous muscles from rats that are hindlimb unloaded for 3 wk, Ca2+-activated
0.707
-
rats treated with ouabain for 15 days
0.78
-
activity value of the semimembranous muscles from rats that are hindlimb unloaded for 4 wk, Ca2+-activated
0.8
-
Ca-ATPase activity, myosin II
0.82
-
Ca-ATPase activity, isoenzyme V1
3
-
K+(EDTA)-ATPase activity, myosin IA
4
-
K+(EDTA)-ATPase activity, myosin IB
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
-
platelet myosin, Mg-ATPase at 25°C, high ionic strength, 0.6 M KCl
5.8
-
cardiac myosin at 25°C
9.5
-
platelet myosin, Ca-ATPase at 25°C, high ionic strength, 0.6 M KCl; platelet myosin, Mg-ATPase at 25°C, high ionic strength, 0.6 M KCl
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 10
-
Ca-ATPase, acidic maximum at pH 5.0, alkaline maximum (higher) at pH 9.5, high ionic strength, 0.6 M KCl; Mg-ATPase, acidic maximum at pH 5.0, alkaline maximum at pH 9.5, high ionic strength, 0.6 M KCl
6 - 9
-
myosin B Ca2+-ATPase, U-shaped curve, minimum at pH 7, second maximum (lower) at pH 6; myosin B, EDTA-activated-ATPase, activity increases with rising pH, strong decrease above pH 9; myosin B, Mg2+-ATPase, little activity increase until pH 7, decrease above pH 9
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0 - 37
-
cardiac myosin activity increases steadily at acidic pH, at alkaline pH activity increases between 0 and 10°C and declines between 20 and 37°C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
2 mol of ATP and 2 mol of actin monomer bind to 1 mol of arterial myosin
Manually annotated by BRENDA team
-
myosin-VIIa, exclusively expressed by sensory hair cells
Manually annotated by BRENDA team
-
myosin ATPase isoenzymes show different temperature sensivities
Manually annotated by BRENDA team
-
polymorphonuclear neutrophils
Manually annotated by BRENDA team
-
myosin-VIIa, exclusively expressed by pigmented epithelial cells
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
cell edge
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
14000
-
alpha,beta,gamma, 1 * 125000 + 1 * 27000 + 1 * 14000, myosin IB, one heavy chain and two light chains, ATP catalytic-, actin binding- and phosphorylation site are located on heavy chain, SDS-PAGE; alpha,beta,gamma, 1 * 130000 + 1 * 17000 + 1 * 14000, myosin IA, one heavy chain and two light chains, SDS-PAGE
16500
-
alpha,beta 1,beta 2, 1 * 20000 + 2 * 16500, at least three species of light chains, SDS-PAGE
17000
-
alpha2,beta2,gamma2, 2 * 170000 + 2 * 17500 + 2 * 17000, two heavy chains and four light chains, SDS-PAGE; alpha,beta,gamma, 1 * 130000 + 1 * 17000 + 1 * 14000, myosin IA, one heavy chain and two light chains, SDS-PAGE
17500
-
alpha2,beta2,gamma2, 2 * 170000 + 2 * 17500 + 2 * 17000, two heavy chains and four light chains, SDS-PAGE
20000
-
alpha,beta 1,beta 2, 1 * 20000 + 2 * 16500, at least three species of light chains, SDS-PAGE
27000
-
alpha,beta,gamma, 1 * 125000 + 1 * 27000 + 1 * 14000, myosin IB, one heavy chain and two light chains, ATP catalytic-, actin binding- and phosphorylation site are located on heavy chain, SDS-PAGE
125000
-
alpha,beta,gamma, 1 * 125000 + 1 * 27000 + 1 * 14000, myosin IB, one heavy chain and two light chains, ATP catalytic-, actin binding- and phosphorylation site are located on heavy chain, SDS-PAGE
130000
-
alpha,beta,gamma, 1 * 130000 + 1 * 17000 + 1 * 14000, myosin IA, one heavy chain and two light chains, SDS-PAGE
150000
-
myosin IA and IB, sucrose density gradient and eqilibrium centrifugation
170000
-
alpha2,beta2,gamma2, 2 * 170000 + 2 * 17500 + 2 * 17000, two heavy chains and four light chains, SDS-PAGE
400000
-
myosin II, sucrose density gradient and eqilibrium centrifugation
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heteromer
-
alpha,beta 1,beta 2, 1 * 20000 + 2 * 16500, at least three species of light chains, SDS-PAGE
hexamer
-
alpha2,beta2,gamma2, 2 * 170000 + 2 * 17500 + 2 * 17000, two heavy chains and four light chains, SDS-PAGE
trimer
-
alpha,beta,gamma, 1 * 125000 + 1 * 27000 + 1 * 14000, myosin IB, one heavy chain and two light chains, ATP catalytic-, actin binding- and phosphorylation site are located on heavy chain, SDS-PAGE; alpha,beta,gamma, 1 * 130000 + 1 * 17000 + 1 * 14000, myosin IA, one heavy chain and two light chains, SDS-PAGE
additional information
P13538 and P02609 and P02604
domain structure of myosin head or myosin subfragment 1, S1
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
phosphorylation of Ser-639 in loop-2 of myosin-2 affects the processive behavior of myosin-2 filaments
side-chain modification
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure analysis, in which myosin II from Dictyostelium discoideum is complexed with Mg2-ADP-vanadate, a transition state analogue, PDB ID 1VOM
hanging drop vapor diffusion method
analysis of structures of nucleotide-free chicken skeletal S1 (PDB entry 2MYS) and chicken gizzard S1 in the S1-ADP-BeFx complex (PDB entry 1BR4)
P13538 and P02609 and P02604
X-ray crystallographic analysis of the Dictyostelium discoideum myosin-2 motor domain complexes with magnesium(II)-ADP-metavanadate and the three pseudilin inhibitors pentabromopseudilin, pentachloropseudilin, and tribromodichloropseudilin, PDB IDs 2JJ9, 1VOM, and 2XO8
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9
-
after 1 h at pH 9.0 isoenzyme V1 shows 2-12% loss of activity compared with 45% for isoenzyme V3
247002
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 30
-
activity of skeletal myosin decreases about 50% after preincubation for 20 min at 30°C and pH 5.7, very slow decrease at pH 8.6, activity of cardiac myosin decreases about 90% after preincubation at 25°C and pH 8.6, very slow decrease at pH 5.7
25 - 37
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100% inhibition after incubation at pH 9.0 and 37°C for 2 min, 10% at 25°C
25 - 30
additional information
P13538 and P02609 and P02604
thermal unfolding of myosin head or myosin subfragment 1, S1, thermally induced dissociation of leight chain 1 from the S1 heavy chain, overview
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, ADP-agarose, hydroxyapatite, BioGel adsorption, myosin Ia and IB; myosin-enriched actomyosin, BioGel, DEAE, myosin II
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immobilized metal ion affinity chromatography (Ni2+)
myofibrils are isolated from heart tissue
myosin with unphosphorylated regulatory light chain (20000 Da) from smooth muscle of gizzard; recombinant His-tagged myosin head: immobilized metal ion affinity chromatography (Ni2+)
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native myosin and myorod from posterior adductor by ammonium sulfate fractionation, dialysis, and gel filtration
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native myosin from smooth adductor muscle
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prepared from heart tissue samples
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
for expression in insect amd mammalian cells
-
His-tagged motor domain construct comprising amino acids 1-761
His-tagged myosin head (Met1-Gln729) expressed in a baculovirus system
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
phosphorylation of Ser639 in loop-2 of the catalytic motor domain of the heavy chain of Acanthamoeba castellanii myosin-2 and the phosphomimetic mutation S639D downregulate the actin-activated ATPase activity of both the full-length myosin and single-headed subfragment-1
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S639D
site-directed mutagenesis, a phosphomimetic mutation that affects the processive behavior of myosin-2 filaments
I499C
-
plus cysteine-light mutations C49S, C312Y, C470I, C599L, C678Y, rescues growth of cells in suspension similarly to wild type, minimal implications on actin binding, ATP-induced actin release, actin-activated ATPase activity
I499C/R738C
-
plus cysteine-light mutations C49S, C312Y, C470I, C599L, C678Y, rescues growth of cells in suspension similarly to wild type, even after disulfide-induced crosslinking of mutated residues just minimal implications on actin binding, ATP-induced actin release, actin-activated ATPase activity
R738C
-
plus cysteine-light mutations C49S, C312Y, C470I, C599L, C678Y, rescues growth of cells in suspension similarly to wild type, minimal implications on actin binding, ATP-induced actin release, actin-activated ATPase activity
D412A
-
mutation in loop3, cardiomyopathy loop, involved in actin binding
F547A
-
mutation in loop 1, a hydrophobic triplet of residues, involved in actin binding
I407A
-
mutation in loop3, cardiomyopathy loop, involved in actin binding
K652A
-
mutation in loop 2, involved in actin binding
K652A/K653A
-
double mutation in loop 2, involved in actin binding
K653A
-
mutation in loop 2, involved in actin binding
P548A
-
mutation in loop 1, a hydrophobic triplet of residues, involved in actin binding
V409A
-
mutation in loop3, cardiomyopathy loop, involved in actin binding
V413A
-
mutation in loop3, cardiomyopathy loop, involved in actin binding
V414A
-
mutation in loop3, cardiomyopathy loop, involved in actin binding
W546A
-
mutation in loop 1, a hydrophobic triplet of residues, involved in actin binding
Myo1b-GAGEGA
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Myo1b in which wild-type loop 4 is replaced with loop 4 of Dictyostelium myosin II, GAGEGA
Myo1b-NGLD
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Myo1b in which wild-type loop 4 is truncated to NGLD
Myo1b1IQ-GAGEGA
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Myo1b1IQ in which wild-type loop 4 is replaced with loop 4 of Dictyostelium myosin II, GAGEGA
Myo1b1IQ-NGLD
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Myo1b1IQ in which wild-type loop 4 is truncated to NGLD
Myo1b1IQ-WT
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wild-type Myo1b truncated after the first IQ domain at amino acid 728 containing the wild-type loop 4 sequence, RMNGLDES
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine