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Information on EC 5.6.1.8 - myosin ATPase

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EC Tree
IUBMB Comments
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.
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Word Map
The enzyme appears in viruses and cellular organisms
Reaction Schemes
+
+
myosin bound to actin filament at position n
=
+
+
myosin bound to actin filament at position n+1
Synonyms
myosin, actomyosin, heavy meromyosin, actomyosin atpase, nmiib, myosin-2, myosin-atpase, natural actomyosin, myosin 2, myosin ii atpase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
actin activated myosin ATPase
-
-
actin-stimulated myosin ATPase
-
-
actomyosin
actomyosin 1b ATPase
-
-
actomyosin ATPase
actomyosin-ATPase
-
-
EC 3.6.1.32
-
-
formerly
-
EC 3.6.4.1
-
-
formerly
-
heavy meromyosin
-
truncated form of skeletal muscle myosin
heavy meromyosin ATPase
-
-
HMM ATPase
-
-
matpase
-
-
-
-
myofibril ATPase
myosin
myosin 2 motor domain
-
myosin ATPase
myosin II ATPase
myosin II S1
-
-
myosin Mg-ATPase
-
-
myosin MgATPase
-
-
myosin S1 ATPase
myosin-2 ATPase
-
-
myosin-ATPase
natural actomyosin
-
-
NMIIB
-
-
S1-myosin ATPase
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + H2O + myosin bound to actin filament at position n = ADP + phosphate + myosin bound to actin filament at position n+1
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
-
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 + actin
ADP + phosphate + actin
show the reaction diagram
-
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
show the reaction diagram
CTP + H2O + actin
CDP + phosphate + actin
show the reaction diagram
-
-
-
-
?
CTP + H2O + myosin bound to actin filament at position n
CDP + phosphate + myosin bound to actin filament at position n+1
show the reaction diagram
gTP + H2O + actin
GDP + phosphate + actin
show the reaction diagram
-
-
-
-
?
GTP + H2O + myosin bound to actin filament at position n
GDP + phosphate + myosin bound to actin filament at position n+1
show the reaction diagram
-
-
-
?
ITP + H2O + actin
IDP + phosphate + actin
show the reaction diagram
-
-
-
-
?
ITP + H2O + myosin bound to actin filament at position n
IDP + phosphate + myosin bound to actin filament at position n+1
show the reaction diagram
-
-
-
?
TTP + H2O + actin
TDP + phosphate + actin
show the reaction diagram
-
-
-
-
?
UTP + H2O + actin
UDP + phosphate + actin
show the reaction diagram
-
-
-
-
?
UTP + H2O + myosin bound to actin filament at position n
UDP + phosphate + myosin bound to actin filament at position n+1
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
-
activates
Ni2+
-
activates
Sr2+
-
activates
additional information
-
uterine myosin S1 ATPase activity does not depend on the concentration of Mg2+ in the presence of 5 mM Zn2+
INHIBITOR
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
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
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%
-
cardiac troponin I
-
-
-
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 4-toluene sulfonamide
-
-
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)
Zn2+
-
about 60% residual activity at 5 mM Zn2+. Tetrahydroxythiacalix[4]arene-tetrasulfosphonate and tetrahydroxythiacalix[4]arene-tetraphosphonate restore myosin S1 ATPase activity to the control level in the presence of 5 mM Zn2+
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
-
filamentous actinin
-
the enzyme is inhibited by increasing amount of free Mg2+ concentration above 1mM in the presence of filamentous actin, while in the absence of filamentous actinin the inhibitory effect on the enzyme activity is not observed above 1 mM free Mg2+
-
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
leiomodin2
-
upon its interaction with the filaments leiomodin2 decreases the actin-activated Mg2+-ATPase activity of skeletal muscle myosin
-
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
-
-
Troponin
-
-
-
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 - 0.49
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
pH not specified in the publication, 25°C
0.2745
2,3,4-trichloro-5-(3,5-dichloro-2-methoxyphenyl)-1H-pyrrole
Dictyostelium discoideum
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
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
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
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
pH not specified in the publication, 25°C
0.1822
2-(3,4,5-tribromo-1-methyl-1H-pyrrol-2-yl)phenol
Dictyostelium discoideum
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
0.005
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
0.13
-
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
0.517
-
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
0.707
-
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
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 10
6 - 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
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
-
-
-
Manually annotated by BRENDA team
turkey
-
-
Manually annotated by BRENDA team
mouse
-
-
Manually annotated by BRENDA team
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
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
cell edge
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A0A222DYD0_9HEMI
1956
0
222926
TrEMBL
other Location (Reliability: 1)
A0A2P6QBD6_ROSCH
740
0
82451
TrEMBL
Chloroplast (Reliability: 3)
A0A2P6RKH5_ROSCH
1529
0
172496
TrEMBL
other Location (Reliability: 2)
A0A2G9HVQ0_9LAMI
1010
0
115813
TrEMBL
other Location (Reliability: 3)
B6H0B1_PENRW
Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255)
1120
1
125994
TrEMBL
Secretory Pathway (Reliability: 1)
A0A396JUT8_MEDTR
1108
0
125635
TrEMBL
other Location (Reliability: 4)
A0A396HCB9_MEDTR
1014
0
115639
TrEMBL
other Location (Reliability: 4)
A0A221IRA2_9HEMI
1956
0
223294
TrEMBL
other Location (Reliability: 1)
A0A072US24_MEDTR
1530
0
172638
TrEMBL
other Location (Reliability: 4)
A0A2P6QRS9_ROSCH
1539
0
173586
TrEMBL
Secretory Pathway (Reliability: 5)
A0A2P6SDY6_ROSCH
137
0
15053
TrEMBL
other Location (Reliability: 2)
A3GHA0_PICST
Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545)
1306
0
149242
TrEMBL
other Location (Reliability: 2)
A2R349_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
1129
1
126917
TrEMBL
Secretory Pathway (Reliability: 1)
A0A221IQX6_9HEMI
1971
0
224881
TrEMBL
other Location (Reliability: 1)
A0A221IRA3_9HEMI
1956
0
222778
TrEMBL
other Location (Reliability: 1)
G7KZI6_MEDTR
1510
0
170807
TrEMBL
other Location (Reliability: 3)
A0A0B2QDU3_GLYSO
506
0
56753
TrEMBL
other Location (Reliability: 2)
A0A2P6R4S5_ROSCH
1177
0
132888
TrEMBL
Chloroplast (Reliability: 3)
A0A2P6PVH0_ROSCH
1173
0
132188
TrEMBL
other Location (Reliability: 5)
A0A2G9GVA3_9LAMI
195
0
21753
TrEMBL
other Location (Reliability: 3)
A0A2G9G9B4_9LAMI
515
0
58102
TrEMBL
other Location (Reliability: 3)
A7ASN6_BABBO
1473
0
165191
TrEMBL
other Location (Reliability: 4)
A0A2G9GFS9_9LAMI
760
0
86921
TrEMBL
other Location (Reliability: 2)
A0A2G9H0R5_9LAMI
992
0
112931
TrEMBL
other Location (Reliability: 3)
A0A396JGY7_MEDTR
1582
0
180858
TrEMBL
other Location (Reliability: 3)
A0A221IQU7_9HEMI
1971
0
225003
TrEMBL
other Location (Reliability: 1)
A0A2G9I9S7_9LAMI
1534
0
174940
TrEMBL
other Location (Reliability: 4)
A0A396JLG2_MEDTR
1516
0
173273
TrEMBL
other Location (Reliability: 4)
A0A396JP85_MEDTR
979
1
111459
TrEMBL
other Location (Reliability: 4)
A0A2G9HAZ0_9LAMI
1221
0
137109
TrEMBL
other Location (Reliability: 2)
A0A2P6QBC6_ROSCH
380
0
43702
TrEMBL
other Location (Reliability: 3)
U6MF83_9EIME
330
0
35517
TrEMBL
other Location (Reliability: 2)
B6HG04_PENRW
Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255)
1567
0
179199
TrEMBL
other Location (Reliability: 1)
A7AWK3_BABBO
837
0
93562
TrEMBL
other Location (Reliability: 2)
A0A2G9I6B0_9LAMI
1513
0
172595
TrEMBL
other Location (Reliability: 5)
A0A221IR91_9HEMI
668
0
76290
TrEMBL
other Location (Reliability: 1)
A0A396JJC6_MEDTR
104
0
11779
TrEMBL
other Location (Reliability: 2)
G7I6V3_MEDTR
1072
0
122783
TrEMBL
other Location (Reliability: 3)
A0A2G9HQ29_9LAMI
476
0
54558
TrEMBL
other Location (Reliability: 5)
A0A396JZN0_MEDTR
1176
0
133007
TrEMBL
Chloroplast (Reliability: 4)
A2R9R1_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
1572
0
179690
TrEMBL
other Location (Reliability: 1)
A0A2P6Q1L6_ROSCH
1522
0
173568
TrEMBL
other Location (Reliability: 3)
A0A2G9GJ57_9LAMI
1502
0
168843
TrEMBL
other Location (Reliability: 3)
A0A2G9HRU7_9LAMI
1524
0
173541
TrEMBL
other Location (Reliability: 2)
A0A221IRF8_9HEMI
1971
0
225151
TrEMBL
other Location (Reliability: 1)
A0A221IRH5_9HEMI
1971
0
224867
TrEMBL
other Location (Reliability: 1)
G7IR58_MEDTR
1203
0
136058
TrEMBL
Chloroplast (Reliability: 3)
A0A396JUH3_MEDTR
288
0
32592
TrEMBL
other Location (Reliability: 5)
A0A2P6R5Q6_ROSCH
1555
0
176374
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2G9HQP8_9LAMI
1061
0
120427
TrEMBL
other Location (Reliability: 2)
A0A221IRH6_9HEMI
699
0
80025
TrEMBL
other Location (Reliability: 1)
A0A8J8W6W4_9EURO
2395
0
276451
TrEMBL
Mitochondrion (Reliability: 2)
A7ASD9_BABBO
1651
0
186706
TrEMBL
other Location (Reliability: 3)
A0A221IR99_9HEMI
409
0
45965
TrEMBL
Mitochondrion (Reliability: 5)
A3GI45_PICST
Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545)
1571
0
180188
TrEMBL
other Location (Reliability: 1)
A0A221IRA8_9HEMI
1956
0
222762
TrEMBL
other Location (Reliability: 1)
A0A396JQ47_MEDTR
1027
0
118589
TrEMBL
other Location (Reliability: 5)
A0A0F4YYL7_TALEM
2407
0
277654
TrEMBL
Mitochondrion (Reliability: 3)
A3LSE0_PICST
Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545)
1063
0
121511
TrEMBL
other Location (Reliability: 1)
A0A222DXQ8_9HEMI
1956
0
222792
TrEMBL
other Location (Reliability: 1)
A0A396JJI1_MEDTR
1170
0
132347
TrEMBL
other Location (Reliability: 4)
A0A396JNU0_MEDTR
1513
0
172073
TrEMBL
other Location (Reliability: 3)
A0A0F4YUE0_TALEM
1571
0
179375
TrEMBL
other Location (Reliability: 1)
A2QN88_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
2406
0
277202
TrEMBL
Mitochondrion (Reliability: 3)
A0A2P6PUP5_ROSCH
1515
0
172214
TrEMBL
other Location (Reliability: 4)
A0A396J293_MEDTR
1169
1
134095
TrEMBL
other Location (Reliability: 4)
A0A072TQA3_MEDTR
1178
0
133649
TrEMBL
Chloroplast (Reliability: 5)
A0A061IJ24_CRIGR
2280
0
261171
TrEMBL
other Location (Reliability: 1)
A0A061IFH1_CRIGR
2043
0
234215
TrEMBL
other Location (Reliability: 2)
A0A2G9HJM6_9LAMI
1509
0
170960
TrEMBL
other Location (Reliability: 5)
A0A2G9HVQ3_9LAMI
88
0
10723
TrEMBL
other Location (Reliability: 2)
A0A2G9HD57_9LAMI
140
0
16351
TrEMBL
Secretory Pathway (Reliability: 4)
A0A396HDD1_MEDTR
58
0
6901
TrEMBL
Mitochondrion (Reliability: 2)
MYSN_ACACA
1509
0
171202
Swiss-Prot
-
MYS2_DICDI
2116
0
243786
Swiss-Prot
-
MYOE_DICDI
1005
0
114795
Swiss-Prot
other Location (Reliability: 2)
MYS2_DICDI
2116
0
243786
Swiss-Prot
other Location (Reliability: 5)
MYO1C_HUMAN
1063
0
121682
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
14000
150000
-
myosin IA and IB, sucrose density gradient and eqilibrium centrifugation
16500
-
alpha,beta 1,beta 2, 1 * 20000 + 2 * 16500, at least three species of light chains, SDS-PAGE
17000
170000
-
alpha2,beta2,gamma2, 2 * 170000 + 2 * 17500 + 2 * 17000, two heavy chains and four 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
400000
-
myosin II, sucrose density gradient and eqilibrium centrifugation
SUBUNIT
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
additional information
P13538; P02609; 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; P02609; 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
-
PROTEIN VARIANTS
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
-
Myo1b in which wild-type loop 4 is replaced with loop 4 of Dictyostelium myosin II, GAGEGA
Myo1b-NGLD
-
Myo1b in which wild-type loop 4 is truncated to NGLD
Myo1b1IQ-GAGEGA
-
Myo1b1IQ in which wild-type loop 4 is replaced with loop 4 of Dictyostelium myosin II, GAGEGA
Myo1b1IQ-NGLD
-
Myo1b1IQ in which wild-type loop 4 is truncated to NGLD
Myo1b1IQ-WT
-
wild-type Myo1b truncated after the first IQ domain at amino acid 728 containing the wild-type loop 4 sequence, RMNGLDES
additional information
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
25 - 37
-
100% inhibition after incubation at pH 9.0 and 37°C for 2 min, 10% at 25°C
additional information
P13538; P02609; 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
-
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+)
-
myosin-enriched actomyosin, BioGel, DEAE, myosin II
-
native myosin and myorod from posterior adductor by ammonium sulfate fractionation, dialysis, and gel filtration
-
native myosin from smooth adductor muscle
-
prepared from heart tissue samples
-
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
-
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Saeiki, K.; Yasunaga, T.; Matsuura, Y.; Wakabayashi, T.
Role of residues 230 and 236 of actin in myosin-ATPase activation by actin-tropomyosin
Biochem. Biophys. Res. Commun.
275
428-433
2000
Oryctolagus cuniculus
Manually annotated by BRENDA team
Murphy, C.T.; Spudich, J.A.
The sequence of the myosin 50-20K loop affects myosin's affinity for actin throughout the actin-myosin ATPase cycle and its maximum ATPase activity
Biochemistry
38
3785-3792
1999
Gallus gallus, Oryctolagus cuniculus, Dictyostelium sp.
Manually annotated by BRENDA team
Katoch, S.S.; Soni, A.
Changes in myosin ATPase activity in skeletal muscles of rat during cold stress
Indian J. Biochem. Biophys.
36
204-206
1999
Rattus norvegicus
Manually annotated by BRENDA team
Park, S.; Ajtai, K.; Burghardt, T.P.
Inhibition of myosin ATPase by metal fluoride complexes
Biochim. Biophys. Acta
1430
127-140
1999
Oryctolagus cuniculus
Manually annotated by BRENDA team
Ye, L-H.; Kishi, H.; Nakamura, A.; Okagaki, T.; Tanaka, T.; Oiwa, K.; Kohama, K.
Myosin light-chain kinase of smooth muscle stimulates myosin ATPase activity without phosphorylating myosin light chain
Proc. Natl. Acad. Sci. USA
96
6666-6671
1999
Gallus gallus
Manually annotated by BRENDA team
Degan, P.; Gesser, H.
Ca2+ activated myosin-ATPase in cardiac myofibrils of rainbow trout, freshwater turtle and rat
J. Exp. Zool.
278
381-390
1997
Oncorhynchus mykiss, Trachemys scripta, Rattus norvegicus
Manually annotated by BRENDA team
Rayment, I.
The structural basis of the myosin ATPase activity
J. Biol. Chem.
271
15850-15853
1996
Dictyostelium sp.
Manually annotated by BRENDA team
Hasson, T.; Mooseker, M.S.
Vertebrate unconventional myosins
J. Biol. Chem.
271
16431-16434
1996
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Wank, V.; Bauer, R.; Punkt, K.; Ziegan, J.
Enzyme activity patterns of myosin ATPase, alpha-glycerophosphate dehydrogenase and succinate dehydrogenase within different muscle fibre types
Acta Histochem.
96
213-218
1994
Oryctolagus cuniculus
Manually annotated by BRENDA team
Szymanski, P.T.; Ferguson, D.G.; Paul, R.J.
Polylysine activates smooth muscle myosin ATPase activity via induction of a 10S to 6S transition
Am. J. Physiol.
265
379-386
1993
Gallus gallus
Manually annotated by BRENDA team
Lin, Y.; Ye, L.H.; Ishikawa, R.; Fujita, K.; Kohama, K.
Stimulatory effect of calponin on myosin ATPase activity
J. Biochem.
113
643-645
1993
Gallus gallus
Manually annotated by BRENDA team
Bolognani, L.; Buttafoco, P.; Ferrari, R.; Venturelli, T.; Volpi, N.
Effects of monocarboxylic and dicarboxylic acids on myosin ATPase activity tested by luminometric procedure
Biochem. Int.
26
231-239
1992
Bos taurus
Manually annotated by BRENDA team
Volpi, N.; Bianchini, P.; Bolognani, L.
Competitive inhibition of myosin ATPase activity by different molecular weight heparins
Biochem. Int.
24
243-253
1991
Bos taurus
Manually annotated by BRENDA team
Tuxen, A.
Effect of varying the preincubation and incubation temperature on the reaction pattern for myosin ATPase in rat skeletal muscle
Acta Anat. (Basel)
139
161-163
1990
Rattus norvegicus
Manually annotated by BRENDA team
Abe, M.; Takahashi, K.; Hiwada, K.
Effect of calponin on actin-activated myosin ATPase activity
J. Biochem.
108
835-838
1990
Gallus gallus
Manually annotated by BRENDA team
Srivastava, S.; Sasser, G.; Peterson, D.L.; Driska, S.P.
Characterization of the fluorescein isothiocyanate-reactive site of gizzard myosin ATPase
Biochim. Biophys. Acta
912
230-238
1987
Meleagris gallopavo
Manually annotated by BRENDA team
White, D.C.S.; Ricigliano, W.; Webb, M.R.
Analysis of the ATPase mechanism of myosin subfragment 1 from insect fibrillar flight muscle in the presence and absence of actin, using phosphate-water oxygen exchange measurements
J. Muscle Res. Cell Motil.
8
537-540
1987
Lethocerus griseus, Lethocerus indicus
Manually annotated by BRENDA team
Lynch, T.J.; Albanesi, J.P.; Korn, E.D.; Robinson, E.A.; Bowerst, B.; Fujisaki, H.
ATPase activities and actin-binding properties of subfragments of Acanthamoeba myosin IA
J. Biol. Chem.
261
17156-17162
1986
Acanthamoeba castellanii
Manually annotated by BRENDA team
Kanda, K.; Sobue, K.; Kakiuchi, S.
Phosphorylation of myosin light chain and the actin-activated ATPase activity of adrenal medullary myosin
J. Biochem.
97
961-964
1985
Bos taurus
Manually annotated by BRENDA team
Tamura, Y.; Kudo, T.; Sako, H.; Miyakama, S.; Nishimoto, T.; Saijo, Y.; Orino, S.; Mori, H.
Enzymatic properties of myosin ATPase from the conduction system of bovine heart
Tokushima J. Exp. Med.
32
1-8
1985
Bos taurus
Manually annotated by BRENDA team
Tanii, I.; Osafune, M.; Arata, T.; Inoue, A.
ATPase characterisics of myosin from nematode Caenorhabditis elegans purified by an improved method. Formation of myosin-phosphate-ADP complex and ATP-induced fluorescence enhancement
J. Biochem.
98
1201-1209
1985
Caenorhabditis elegans, Oryctolagus cuniculus
Manually annotated by BRENDA team
Kameyama, S.; Ichikawa, H.; Sunaga, Y.; Nakata, S.; Saito, Y.; Eiki, T.; Watanabe, S.
Biochemical characteristics of cardiac myosin: the pH dependence of Ca-ATPase activity, and that of the absorption spectrum of 2,4,6-trinitrophenyl groups attached to myosin
J. Biochem.
97
625-632
1985
Bos taurus, Gallus gallus, Oryctolagus cuniculus, Sus scrofa
Manually annotated by BRENDA team
Bechet, J.J.; Bachouchi, N.; Janmot, C.; d'Albis, A.
Isoenzymes of myosin subfragments. Chromatographic fractionation on carboxymethylcellulose and actin-activated ATPase activity as a function of temperature
Biochim. Biophys. Acta
703
54-61
1982
Oryctolagus cuniculus
Manually annotated by BRENDA team
Srivastava, S.; Kanungo, M.S.
Aging modulates some properties of skeletal myosin ATPase of rat
Biochem. Med.
28
266-272
1982
Rattus norvegicus, Rattus norvegicus Wistar
Manually annotated by BRENDA team
Korn, E.D.; Collins, J.H.; Maruta, H.
Myosins from Acanthamoeba castellanii
Methods Enzymol.
85
357-363
1982
Acanthamoeba castellanii
Manually annotated by BRENDA team
Yamashita, T.; Tanaka, Y.; Matsuzawa, H.
Cytoplasmic and plasma membrane adenosine triphosphatase of polymorphonuclear neutrophils, comparison of their enzymatic properties and attempt for a direct determination of myosin ATPase activity using polymorphonuclear neutrophil extract
Biochim. Biophys. Acta
599
246-253
1980
Cavia porcellus
Manually annotated by BRENDA team
Takeuchi, K.
Comparison of kinetic properties of the ATPase reaction of arterial smooth muscle myosin with skeletal muscle myosin
J. Biochem.
88
1693-1702
1980
Bos taurus, Oryctolagus cuniculus
Manually annotated by BRENDA team
Pope, B.; Hoh, J.F.Y.; Weeds, A.
The ATPase activities of rat cardiac myosin isoenzymes
FEBS Lett.
118
205-209
1980
Rattus norvegicus
Manually annotated by BRENDA team
Shimizu, T.
Bovine platelet myosin. Properties of Mg- and Ca-ATPase
J. Biochem.
84
607-616
1978
Bos taurus
Manually annotated by BRENDA team
Trentham, D.R.
The adenosine triphosphatase reactions of myosin and actomyosin and their relation to energy transduction in muscle
Biochem. Soc. Trans.
5
5-22
1977
Oryctolagus cuniculus
Manually annotated by BRENDA team
Kielley, W.W.
Myosin adenosine triphosphatase
The Enzymes, 2nd Ed. (Boyer, P. D. , Lardy, H. , Myrbck, K. , eds. )
5
159-168
1961
Canis lupus familiaris, Oryctolagus cuniculus
-
Manually annotated by BRENDA team
Tiago, T.; Aureliano, M.; Gutierrez-Merino, C.
Decavanadate binding to a high affinity site near the myosin catalytic centre inhibits F-actin-stimulated myosin ATPase activity
Biochemistry
43
5551-5561
2004
Oryctolagus cuniculus
Manually annotated by BRENDA team
Trombetta, G.; Adami, R.; Cintio, O.; Grazi, E.
Differential response of fast and slow myosin ATPase from skeletal muscle to F-actin and to phalloidin F-actin
Biochim. Biophys. Acta
1569
135-138
2002
Oryctolagus cuniculus
Manually annotated by BRENDA team
Kobayashi, T.; Saeki, Y.; Chaen, S.; Shirakawa, I.; Sugi, H.
Effect of deuterium oxide on contraction characteristics and ATPase activity in glycerinated single rabbit skeletal muscle fibers
Biochim. Biophys. Acta
1659
46-51
2004
Oryctolagus cuniculus
Manually annotated by BRENDA team
Amitani, I.; Sakamoto, T.; Ando, T.
Link between the enzymatic kinetics and mechanical behavior in an actomyosin motor
Biophys. J.
80
379-397
2001
Oryctolagus cuniculus
Manually annotated by BRENDA team
Moreira, C.M.; Oliveira, E.M.; Bonan, C.D.; Sarkis, J.J.; Vassallo, D.V.
Effects of mercury on myosin ATPase in the ventricular myocardium of the rat
Comp. Biochem. Physiol. C
135C
269-275
2003
Rattus norvegicus
Manually annotated by BRENDA team
Shih, W.M.; Spudich, J.A.
The myosin relay helix to converter interface remains intact throughout the actomyosin ATPase cycle
J. Biol. Chem.
276
19491-19494
2001
Dictyostelium discoideum
Manually annotated by BRENDA team
Wang, F.; Kovacs, M.; Hu, A.; Limouze, J.; Harvey, E.V.; Sellers, J.R.
Kinetic mechanism of non-muscle myosin IIB: Functional adaptations for tension generation and maintenance
J. Biol. Chem.
278
27439-27448
2003
Homo sapiens
Manually annotated by BRENDA team
Lowe, D.A.; Husom, A.D.; Ferrington, D.A.; Thompson, L.V.
Myofibrillar myosin ATPase activity in hindlimb muscles from young and aged rats
Mech. Ageing Dev.
125
619-627
2004
Rattus norvegicus
Manually annotated by BRENDA team
Okafor, C.; Liao, R.; Perreault-Micale, C.; Li, X.; Ito, T.; Stepanek, A.; Doye, A.; de Tombe, P.; Gwathmey, J.K.
Mg-ATPase and Ca+ activated myosin AtPase activity in ventricular myofibrils from non-failing and diseased human hearts--effects of calcium sensitizing agents MCI-154, DPI 201-106, and caffeine
Mol. Cell. Biochem.
245
77-89
2003
Homo sapiens
Manually annotated by BRENDA team
Alahyan, M.; Webb, M.R.; Marston, S.B.; El-Mezgueldi, M.
The mechanism of smooth muscle caldesmon-tropomyosin inhibition of the elementary steps of the actomyosin ATPase
J. Biol. Chem.
281
19433-19448
2006
Oryctolagus cuniculus
Manually annotated by BRENDA team
Prochniewicz, E.; Thomas, D.D.; Thompson, L.V.
Age-related decline in actomyosin function
J. Gerontol.
A
425-431
2005
Rattus norvegicus
Manually annotated by BRENDA team
Burton, K.; White, H.; Sleep, J.
Kinetics of muscle contraction and actomyosin NTP hydrolysis from rabbit using a series of metal-nucleotide substrates
J. Physiol.
563
689-711
2005
Oryctolagus cuniculus
Manually annotated by BRENDA team
Borlak, J.; Zwadlo, C.
The myosin ATPase inhibitor 2,3-butanedione monoxime dictates transcriptional activation of ion channels and Ca(2+)-handling proteins
Mol. Pharmacol.
66
708-717
2004
Rattus norvegicus
Manually annotated by BRENDA team
Paul Ehrlich, H.; Sun, B.; Kainth, K.S.; Kromah, F.
Elucidating the mechanism of wound contraction: rapid versus sustained myosin ATPase activity in attached-delayed-released compared with free-floating fibroblast-populated collagen lattices
Wound Repair Regen.
14
625-632
2006
Homo sapiens
Manually annotated by BRENDA team
Zhong, S.; Thompson, L.V.
The roles of myosin ATPase activity and myosin light chain relative content in the slowing of type IIB fibers with hindlimb unweighting in rats
Am. J. Physiol.
293
C723-C728
2007
Rattus norvegicus
Manually annotated by BRENDA team
Kulikova, N.; Pronina, O.E.; Dabrowska, R.; Borovikov, Y.S.
Caldesmon restricts the movement of both C- and N-termini of tropomyosin on F-actin in ghost fibers during the actomyosin ATPase cycle
Biochem. Biophys. Res. Commun.
345
280-286
2006
Oryctolagus cuniculus
Manually annotated by BRENDA team
Tiago, T.; Simao, S.; Aureliano, M.; Martin-Romero, F.J.; Gutierrez-Merino, C.
Inhibition of skeletal muscle S1-myosin ATPase by peroxynitrite
Biochemistry
45
3794-3804
2006
Oryctolagus cuniculus
Manually annotated by BRENDA team
Lieto-Trivedi, A.; Dash, S.; Coluccio, L.M.
Myosin surface loop 4 modulates inhibition of actomyosin 1b ATPase activity by tropomyosin
Biochemistry
46
2779-2786
2007
Mammalia
Manually annotated by BRENDA team
Borovikov, Y.S.; Kulikova, N.; Pronina, O.E.; Khaimina, S.S.; Wrzosek, A.; Dabrowska, R.
Caldesmon freezes the structure of actin filaments during the actomyosin ATPase cycle
Biochim. Biophys. Acta
1764
1054-1062
2006
Oryctolagus cuniculus
Manually annotated by BRENDA team
Tiago, T.; Martel, P.; Gutierrez-Merino, C.; Aureliano, M.
Binding modes of decavanadate to myosin and inhibition of the actomyosin ATPase activity
Biochim. Biophys. Acta
1774
474-480
2007
Dictyostelium discoideum
Manually annotated by BRENDA team
Padilha, A.S.; Moreira, C.M.; Meira, E.F.; Siman, F.D.; Stefanon, I.; Vassallo, D.V.
Chronic ouabain treatment enhances cardiac myosin ATPase activity in rats
Clin. Exp. Pharmacol. Physiol.
35
801-806
2008
Rattus norvegicus
Manually annotated by BRENDA team
Haagensen, L.; Jensen, D.H.; Gesser, H.
Dependence of myosin-ATPase on structure bound creatine kinase in cardiac myfibrils from rainbow trout and freshwater turtle
Comp. Biochem. Physiol. A
150
404-409
2008
Oncorhynchus mykiss, Trachemys scripta
Manually annotated by BRENDA team
Onishi, H.; Mikhailenko, S.V.; Morales, M.F.
Toward understanding actin activation of myosin ATPase: the role of myosin surface loops
Proc. Natl. Acad. Sci. USA
103
6136-6141
2006
Gallus gallus
Manually annotated by BRENDA team
Blair, D.R.; Funai, K.; Schweitzer, G.G.; Cartee, G.D.
A myosin II ATPase inhibitor reduces force production, glucose transport, and phosphorylation of AMPK and TBC1D1 in electrically stimulated rat skeletal muscle
Am. J. Physiol. Endocrinol. Metab.
296
E993-E1002
2009
Rattus norvegicus
Manually annotated by BRENDA team
Vassallo, D.V.; Lebarch, E.C.; Moreira, C.M.; Wiggers, G.A.; Stefanon, I.
Lead reduces tension development and the myosin ATPase activity of the rat right ventricular myocardium
Braz. J. Med. Biol. Res.
41
789-795
2008
Rattus norvegicus
Manually annotated by BRENDA team
Kronert, W.A.; Dambacher, C.M.; Knowles, A.F.; Swank, D.M.; Bernstein, S.I.
Alternative relay domains of Drosophila melanogaster myosin differentially affect ATPase activity, in vitro motility, myofibril structure and muscle function
J. Mol. Biol.
379
443-456
2008
Drosophila melanogaster
Manually annotated by BRENDA team
Saber, W.; Begin, K.J.; Warshaw, D.M.; VanBuren, P.
Cardiac myosin binding protein-C modulates actomyosin binding and kinetics in the in vitro motility assay
J. Mol. Cell. Cardiol.
44
1053-1061
2008
Gallus gallus
Manually annotated by BRENDA team
Joubert, F.; Wilding, J.R.; Fortin, D.; Domergue-Dupont, V.; Novotova, M.; Ventura-Clapier, R.; Veksler, V.
Local energetic regulation of sarcoplasmic and myosin ATPase is differently impaired in rats with heart failure
J. Physiol.
586
5181-5192
2008
Rattus norvegicus
Manually annotated by BRENDA team
Anderson, T.W.; Vaughan, A.N.; Cramer, L.P.
Retrograde flow and myosin II activity within the leading cell edge deliver F-actin to the lamella to seed the formation of graded polarity actomyosin II filament bundles in migrating fibroblasts
Mol. Biol. Cell
19
5006-5018
2008
Gallus gallus
Manually annotated by BRENDA team
Katayama, T.; Watanabe, M.; Tanaka, H.; Hino, M.; Miyakawa, T.; Ohki, T.; Ye, L.; Xie, C.; Yoshiyama, S.; Nakamura, A.; Ishikawa, R.; Tanokura, M.; Oiwa, K.; Kohama, K.
Stimulatory effects of arachidonic acid on myosin ATPase activity and contraction of smooth muscle via myosin motor domain
Am. J. Physiol. Heart Circ. Physiol.
298
H505-H514
2010
Gallus gallus
Manually annotated by BRENDA team
Caremani, M.; Lehman, S.; Lombardi, V.; Linari, M.
Orthovanadate and orthophosphate inhibit muscle force via two different pathways of the myosin ATPase cycle
Biophys. J.
100
665-674
2011
Oryctolagus cuniculus
Manually annotated by BRENDA team
Cooke, R.
The role of the myosin ATPase activity in adaptive thermogenesis by skeletal muscle
Biophys. Rev.
3
33-45
2011
Oryctolagus cuniculus
Manually annotated by BRENDA team
Preller, M.; Chinthalapudi, K.; Martin, R.; Knolker, H.J.; Manstein, D.J.
Inhibition of myosin ATPase activity by halogenated pseudilins: a structure-activity study
J. Med. Chem.
54
3675-3685
2011
Dictyostelium discoideum (P08799)
Manually annotated by BRENDA team
Ahmad, R.; Hasnain, A.
Ultrasonication of chicken natural actomyosin: effect on ATPase activity, turbidity and SDS-PAGE profiles at different protein concentrations
Am. J. Biochem. Mol. Biol.
3
240-247
2013
Gallus gallus
-
Manually annotated by BRENDA team
Sato, M.K.; Ishihara, T.; Tanaka, H.; Ishijima, A.; Inoue, Y.
Velocity-dependent actomyosin ATPase cycle revealed by in vitro motility assay with kinetic analysis
Biophys. J.
103
711-718
2012
Oryctolagus cuniculus
Manually annotated by BRENDA team
Kiani, F.A.; Fischer, S.
Advances in quantum simulations of ATPase catalysis in the myosin motor
Curr. Opin. Struct. Biol.
31
115-123
2015
Dictyostelium discoideum (P08799)
Manually annotated by BRENDA team
Martin, R.; Risacher, C.; Barthel, A.; Jaeger, A.; Schmidt, A.; Richter, S.; Boehl, M.; Preller, M.; Chinthalapudi, K.; Manstein, D.; Gutzeit, H.; Knoelker, H.
Silver(I)-catalyzed route to pyrroles: synthesis of halogenated pseudilins as allosteric inhibitors for myosin ATPase and x-ray crystal structures of the protein-inhibitor complexes
Eur. J. Org. Chem.
2014
4487-4505
2014
Oryctolagus cuniculus
-
Manually annotated by BRENDA team
Heissler, S.M.; Liu, X.; Korn, E.D.; Sellers, J.R.
Kinetic characterization of the ATPase and actin-activated ATPase activities of Acanthamoeba castellanii myosin-2
J. Biol. Chem.
288
26709-26720
2013
Acanthamoeba castellanii (P05659), Acanthamoeba castellanii
Manually annotated by BRENDA team
Yamada, A.; Yoshio, M.; Oiwa, K.
Myosin Mg-ATPase of molluscan muscles is slightly activated by F-actin under catch state in vitro
J. Muscle Res. Cell Motil.
34
115-123
2013
Mytilus galloprovincialis
Manually annotated by BRENDA team
Matusovsky, O.S.; Shevchenko, U.V.; Matusovskaya, G.G.; Sobieszek, A.; Dobrzhanskaya, A.V.; Sheludko, N.S.
Catch muscle myorod modulates ATPase activity of myosin in a phosphorylation-dependent way
PLoS ONE
10
e0125379
2015
Oryctolagus cuniculus, Crenomytilus grayanus
Manually annotated by BRENDA team
Logvinova, D.S.; Markov, D.I.; Nikolaeva, O.P.; Sluchanko, N.N.; Ushakov, D.S.; Levitsky, D.I.
Does interaction between the motor and regulatory domains of the myosin head occur during ATPase cycle? Evidence from thermal unfolding studies on myosin subfragment 1
PLoS ONE
10
e0137517
2015
Gallus gallus (P13538 and P02609 and P02604)
Manually annotated by BRENDA team
Mizui, T.; Sekino, Y.; Yamazaki, H.; Ishizuka, Y.; Takahashi, H.; Kojima, N.; Kojima, M.; Shirao, T.
Myosin II ATPase activity mediates the long-term potentiation-induced exodus of stable F-actin bound by drebrin A from dendritic spines
PLoS ONE
9
e85367
2014
Rattus norvegicus, Rattus norvegicus Wistar
Manually annotated by BRENDA team
Borovikov, Y.S.; Avrova, S.V.; Rysev, N.A.; Sirenko, V.V.; Simonyan, A.O.; Chernev, A.A.; Karpicheva, O.E.; Piers, A.; Redwood, C.S.
Aberrant movement of beta-tropomyosin associated with congenital myopathy causes defective response of myosin heads and actin during the ATPase cycle
Arch. Biochem. Biophys.
577-578
11-23
2015
Oryctolagus cuniculus
Manually annotated by BRENDA team
Kobayashi, M.; Ramirez, B.E.; Warren, C.M.
Interplay of actin, ADP and Mg2+ interactions with striated muscle myosin Implications of their roles in ATPase
Arch. Biochem. Biophys.
662
101-110
2019
Oryctolagus cuniculus
Manually annotated by BRENDA team
Borovikov, Y.; Simonyan, A.; Karpicheva, O.; Avrova, S.; Rysev, N.; Sirenko, V.; Piers, A.; Redwood, C.
The reason for a high Ca2+-sensitivity associated with Arg91Gly substitution in TPM2 gene is the abnormal behavior and high flexibility of tropomyosin during the ATPase cycle
Biochem. Biophys. Res. Commun.
494
681-686
2017
Oryctolagus cuniculus
Manually annotated by BRENDA team
Ghashghaee, N.; Li, K.; Dong, W.
Direct interaction between troponin and myosin enhances the ATPase activity of heavy meromyosin
Biologia (Poland)
72
702-708
2017
Oryctolagus cuniculus
-
Manually annotated by BRENDA team
Kiani, F.; Fischer, S.
ATP-dependent interplay between local and global conformational changes in the myosin motor
Cytoskeleton (Hoboken)
73
643-651
2016
Homo sapiens
Manually annotated by BRENDA team
Li, J.; Lu, Z.; He, J.; Chen, Q.; Wang, X.; Kang, L.; Li, X.D.
Alternative exon-encoding regions of Locusta migratoria muscle myosin modulate the pH dependence of ATPase activity
Insect Mol. Biol.
25
689-700
2016
Locusta migratoria
Manually annotated by BRENDA team
Labyntseva, R.; Yavorovska, V.; Bevza, O.; Drapaylo, A.; Kalchenko, V.; Kosterin, S.
Thiacalix[4]arenes remove the inhibitory effects of Zn cations on the myosin ATPase activity
Nanoscale Res. Lett.
13
224
2018
Sus scrofa
Manually annotated by BRENDA team
Fujii, T.; Namba, K.
Structure of actomyosin rigour complex at 5.2 A resolution and insights into the ATPase cycle mechanism
Nat. Commun.
8
13969
2017
Oryctolagus cuniculus
Manually annotated by BRENDA team
Chung, C.S.; Mechas, C.; Campbell, K.S.
Myocyte contractility can be maintained by storing cells with the myosin ATPase inhibitor 2,3 butanedione monoxime
Physiol. Rep.
3
e12445
2015
Rattus norvegicus
Manually annotated by BRENDA team
Szatmari, D.; Bugyi, B.; Ujfalusi, Z.; Grama, L.; Dudas, R.; Nyitrai, M.
Cardiac leiomodin2 binds to the sides of actin filaments and regulates the ATPase activity of myosin
PLoS ONE
12
e0186288
2017
Rattus norvegicus
Manually annotated by BRENDA team