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Information on EC 3.6.5.5 - dynamin GTPase and Organism(s) Homo sapiens and UniProt Accession Q05193

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EC Tree
IUBMB Comments
An enzyme with a molecular mass of about 100 kDa that is involved in endocytosis and is instrumental in pinching off membrane vesicles.
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Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: Q05193
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
dynamin, dynamin-related protein 1, dynamin 2, d100, dynamin-2, dynamin 1, dynamin i, optic atrophy 1, dynamin-1, gtpase dynamin, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dynamin 1
-
dynamin I
-
dynamin I GTPase
-
dynI GTPase
-
large GTPase
-
multidomain GTPase
-
B-dynamin
-
-
-
-
D100
-
-
-
-
DLP-1
-
-
Drp1-short
isozyme 3
Dyn1
-
-
dynamin
dynamin 1
-
-
dynamin 2
dynamin 3
-
Dynamin BREDNM19
-
-
-
-
dynamin GTPase
dynamin I
-
-
Dynamin UDNM
-
-
-
-
Dynamin, brain
-
-
-
-
Dynamin, testicular
-
-
-
-
dynamin-1
dynamin-1-like GTPase
-
dynamin-2
-
-
dynamin-like GTPase
-
dynamin-like guanosine-triphosphate hydrolase
-
dynamin-like myxovirus resistance protein A
-
dynamin-like protein 1
-
-
dynamin-related protein 1
-
dynamin-related protein 1 isoform 3
-
dynamin1
-
-
dynamin2
dynamin2 GTPase
-
fission dynamin
-
GTP phosphohydrolase
-
-
-
-
GTPase
GTPase dynamin
-
-
guanine triphosphatase
-
-
-
-
guanosine 5'-triphosphatase
-
-
-
-
guanosine triphosphatase
-
-
-
-
hDrp1 isoform 3
-
large GTPase
-
mitochondrial dynamin
-
-
Mx GTPase
-
myxovirus resistance GTPase
-
optic atrophy 1
-
phosphatase, guanosine tri-
-
-
-
-
ribosomal GTPase
-
-
-
-
Shibire protein
-
-
-
-
T-dynamin
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
GTP + H2O = GDP + phosphate
show the reaction diagram
analysis of the GTPase mechanism of MxA
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
SYSTEMATIC NAME
IUBMB Comments
GTP phosphohydrolase (vesicle-releasing)
An enzyme with a molecular mass of about 100 kDa that is involved in endocytosis and is instrumental in pinching off membrane vesicles.
CAS REGISTRY NUMBER
COMMENTARY hide
9059-32-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
?
GTP + H2O
GDP + phosphate
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
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2-chloro-6-methylpyrimidin-4-yl)butylamine
-
(2-chloro-6-methylpyrimidin-4-yl)cyclohexylamine
-
(2-chloro-6-methylpyrimidin-4-yl)cyclopropylmethylpropylamine
-
(2-chloro-6-methylpyrimidin-4-yl)decylamine
-
(2-chloro-6-methylpyrimidin-4-yl)dimethylamine
-
(2-chloro-6-methylpyrimidin-4-yl)ethylamine
-
(2-chloro-6-methylpyrimidin-4-yl)hexylamine
-
(2-chloro-6-methylpyrimidin-4-yl)octylamine
-
(2-chloro-6-methylpyrimidin-4-yl)propylamine
-
(2-chloro-6-methylpyrimidin-4-yl)tetradecylamine
-
(4-chloro-6-methylpyrimidin-2-yl)(1-cyclopropylmethylpropyl)amine
-
(4-chloro-6-methylpyrimidin-2-yl)-dimethylamine
-
(4-chloro-6-methylpyrimidin-2-yl)butylamine
-
(4-chloro-6-methylpyrimidin-2-yl)cyclohexylamine
-
(4-chloro-6-methylpyrimidin-2-yl)decylamine
-
(4-chloro-6-methylpyrimidin-2-yl)hexylamine
-
(4-chloro-6-methylpyrimidin-2-yl)octylamine
-
(4-chloro-6-methylpyrimidin-2-yl)propylamine
-
(4-chloro-6-methylpyrimidin-2-yl)tetradecylamine
-
2-(2-dimethylaminoethyl)-4-N-(didecylamino)-6-methylpyrimidine
-
2-chloro-4-(2-dimethylaminopropylamine)-6-methylpyrimidine
-
2-chloro-5-methyl-4-(4-methylpiperazin-1-yl)pyrimidine
-
2-chloro-N-(4-methoxybenzyl)-6-methylpyrimidin-4-amine
-
3-sulfo-N-(2-hydroxyethyl)-1,8-naphthalimide
-
4-(2-dimethylaminoethyl)-2-N-(didecylamino)-6-methylpyrimidine
-
4-amino-3-sulfo-N-(2-(dimethylamino)ethyl)-1,8-naphthalimide
-
4-amino-3-sulfo-N-(2-(piperazin-1-yl)ethyl)-1,8-naphthalimide
-
4-amino-3-sulfo-N-(2-aminobenzyl)-1,8-naphthalimide
-
4-amino-3-sulfo-N-(2-aminoethyl)-1,8-naphthalimide
-
4-amino-3-sulfo-N-(2-carboxyethyl)-1,8-naphthalimide
-
4-amino-3-sulfo-N-(2-hydroxyethyl)-1,8-naphthalimide
-
4-amino-3-sulfo-N-(2-mercaptoethyl)-1,8-naphthalimide
-
4-amino-3-sulfo-N-(2-methoxyethyl)-1,8-naphthalimide
-
4-amino-3-sulfo-N-(3-aminobenzyl)-1,8-naphthalimide
-
4-amino-3-sulfo-N-(3-hydroxyphenyl)-1,8-naphthalimide
-
4-amino-3-sulfo-N-(3-hydroxypropyl)-1,8-naphthalimide
-
4-amino-3-sulfo-N-(4-aminobenzyl)-1,8-naphthalimide
-
4-amino-3-sulfo-N-(4-carboxybenzyl)-1,8-naphthalimide
-
4-amino-3-sulfo-N-(4-hydroxybenzyl)-1,8-naphthalimide
-
4-amino-3-sulfo-N-(4-hydroxyphenyl)-1,8-naphthalimide
-
4-amino-3-sulfo-N-(4-methoxyphenyl)-1,8-naphthalimide
-
4-amino-3-sulfo-N-(5-hydroxyhexyl)-1,8-naphthalimide
-
4-amino-3-sulfo-N-(5-hydroxypentyl)-1,8-naphthalimide
-
4-amino-3-sulfo-N-(carboxymethyl)-1,8-naphthalimide
-
4-amino-3-sulfo-N-(phenethyl)-1,8-naphthalimide
-
4-amino-3-sulfo-N-benzyl-1,8-naphthalimide
-
4-amino-3-sulfo-N-phenyl-1,8-naphthalimide
-
4-chloro-6-methyl-2-(4-methylpiperazin-1-yl)pyrimidine
-
4-chloro-N-(4-methoxybenzyl)-6-methylpyrimidin-2-amine
-
4-sulfo-N-(2-hydroxyethyl)-1,8-naphthalimide
-
N'-(2-chloro-6-methylpyrimidin-4-yl)ethane-1,2-diamine
-
N'-(4-Chloro-6-methylpyrimidin-2-yl)-ethane-1,2-diamine
-
N-(2-hydroxyethyl)-1,8-naphthalimide
-
N-benzyl-2-chloro-6-methylpyrimidin-4-amine
-
N-benzyl-4-chloro-6-methylpyrimidin-2-amine
-
N-decyl-N'-(2-dimethylaminoethyl)-pyrimidine-4,6-diamine
-
N-dodecyl-N'-(2-dimethylaminoethyl)pyrimidine-4,6-diamine
-
N1-(4-chloro-6-methylpyrimidin-2-yl)-N3,N3-dimethylpropane-1,3-diamine
-
N2-(2-dimethylaminoethyl)-6-methyl-N4-octadecylpyrimidine-2,4-diamine
-
N2-(2-dimethylaminoethyl)-6-methyl-N4-propylpyrimidine-2,4-diamine
-
N2-(2-dimethylaminoethyl)-6-methyl-N4-tetradecylpyrimidine-2,4-diamine
-
N2-(2-dimethylaminoethyl)-N4-decyl-6-methylpyrimidine-2,4-diamine
-
N2-(2-dimethylaminoethyl)-N4-hexyl-6-methylpyrimidine-2,4-diamine
-
N2-(2-dimethylaminoethyl)-N4-octyl-6-methylpyrimidine-2,4-diamine
-
N2-benzyl-N4-(2-dimethylaminoethyl)-6-methylpyrimidine-2,4-diamine
-
N2-butyl-N4-(2-dimethylaminoethyl)-6-methylpyrimidine-2,4-diamine
-
N2-cyclohexyl-N4-(2-dimethylaminoethyl)-6-methylpyrimidine-2,4-diamine
-
N2-cyclopropylmethyl-N4-(2-dimethylamin-ethyl)-6-methyl-N2-propylpyrimidine-2,4-diamine
-
N2-decyl-N4-(2-dimethylaminoethyl)pyrimidine-2,4-diamine
-
N2-dodecyl-N4-(2-dimethylaminoethyl)-pyrimidine-2,4-diamine
-
N2-sec-butyl-N4-(2-dimethylaminoethyl)-6-methylpyrimidine-2,4-diamine
-
N4-(2-dimethylaminoethyl)-6-methyl-N2-octadecylpyrimidine-2,4-diamine
-
N4-(2-dimethylaminoethyl)-6-methyl-N2-propylpyrimidine-2,4-diamine
-
N4-(2-dimethylaminoethyl)-6-methyl-N2-tetradecylpyrimidine-2,4-diamine
-
N4-(2-dimethylaminoethyl)-N2-decyl-6-methylpyrimidine-2,4-diamine
-
N4-(2-dimethylaminoethyl)-N2-hexyl-6-methylpyrimidine-2,4-diamine
-
N4-(2-dimethylaminoethyl)-N2-octyl-6-methylpyrimidine-2,4-diamine
-
N4-Benzyl-N2-(2-dimethylaminoethyl)-6-methylpyrimidine-2,4-diamine
-
N4-butyl-N2-(2-dimethylaminoethyl)-6-methylpyrimidine-2,4-diamine
-
N4-cyclohexyl-N2-(2-dimethylaminoethyl)-6-methylpyrimidine-2,4-diamine
-
N4-cyclopropylmethyl-N2-(2-dimethylamin-ethyl)-6-methyl-N2-propylpyrimidine-2,4-diamine
-
N4-decyl-N2-(2-dimethylaminoethyl)pyrimidine-2,4-diamine
-
N4-dodecyl-N2-(2-dimethylaminoethyl)pyrimidine-2,4-diamine
-
N4-sec-butyl-N2-(2-dimethylaminoethyl)-6-methylpyrimidine-2,4-diamine
-
sec-butyl-(2-chloro-6-methylpyrimidin-4-yl)amine
-
sec-butyl-(4-chloro-6-methylpyrimidin-2-yl)amine
-
[2-(2-chloro-6-methylpyrimidin-4-ylamino)ethyl]carbamic acid tert-butyl ester
-
[2-(4-chloro-6-methylpyrimidin-2-ylamino)ethyl]carbamic acid tert-butyl ester
-
(5Z)-3-(prop-2-en-1-yl)-5-(quinoxalin-2-ylmethylidene)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-3-benzyl-5-(2H-chromen-3-ylmethylidene)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-3-benzyl-5-(3,5-dichlorobenzylidene)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-3-benzyl-5-(4-bromobenzylidene)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-3-benzyl-5-(biphenyl-4-ylmethylidene)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-3-benzyl-5-(quinoxalin-2-ylmethylidene)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-3-benzyl-5-[(5-chloro-1-benzothiophen-3-yl)methylidene]-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-3-benzyl-5-[(6,8-dichloro-4-oxo-4H-chromen-3-yl)methylidene]-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-3-benzyl-5-[4-[3-(dimethylamino)propoxy]benzylidene]-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-3-ethyl-5-(quinoxalin-2-ylmethylidene)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-(2,1,3-benzothiadiazol-5-ylmethylidene)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-(2,1,3-benzothiadiazol-5-ylmethylidene)-3-(prop-2-en-1-yl)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-(2,1,3-benzothiadiazol-5-ylmethylidene)-3-benzyl-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-(2,1,3-benzothiadiazol-5-ylmethylidene)-3-ethyl-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-(2,1,3-benzoxadiazol-5-ylmethylidene)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-(2,1,3-benzoxadiazol-5-ylmethylidene)-3-(prop-2-en-1-yl)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-(2,1,3-benzoxadiazol-5-ylmethylidene)-3-benzyl-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-(2,1,3-benzoxadiazol-5-ylmethylidene)-3-ethyl-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-(2H-chromen-3-ylmethylidene)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-(2H-chromen-3-ylmethylidene)-3-(prop-2-en-1-yl)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-(2H-chromen-3-ylmethylidene)-3-ethyl-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-(3,5-dichlorobenzylidene)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-(3,5-dichlorobenzylidene)-3-(prop-2-en-1-yl)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-(3,5-dichlorobenzylidene)-3-ethyl-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-(4-bromobenzylidene)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-(4-bromobenzylidene)-3-(prop-2-en-1-yl)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-(4-bromobenzylidene)-3-ethyl-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-(biphenyl-4-ylmethylidene)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-(biphenyl-4-ylmethylidene)-3-(prop-2-en-1-yl)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-(biphenyl-4-ylmethylidene)-3-ethyl-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-(quinoxalin-2-ylmethylidene)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-[(5-chloro-1-benzothiophen-3-yl)methylidene]-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-[(5-chloro-1-benzothiophen-3-yl)methylidene]-3-(prop-2-en-1-yl)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-[(5-chloro-1-benzothiophen-3-yl)methylidene]-3-ethyl-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-[(6,8-dichloro-4-oxo-4H-chromen-3-yl)methylidene]-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-[(6,8-dichloro-4-oxo-4H-chromen-3-yl)methylidene]-3-(prop-2-en-1-yl)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-[(6,8-dichloro-4-oxo-4H-chromen-3-yl)methylidene]-3-ethyl-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-[4-[3-(dimethylamino)propoxy]benzylidene]-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-[4-[3-(dimethylamino)propoxy]benzylidene]-3-(prop-2-en-1-yl)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-[4-[3-(dimethylamino)propoxy]benzylidene]-3-ethyl-2-thioxo-1,3-thiazolidin-4-one
-
-
3-[(5Z)-4-oxo-5-(quinoxalin-2-ylmethylidene)-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
-
-
3-[(5Z)-5-(2,1,3-benzothiadiazol-5-ylmethylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
-
-
3-[(5Z)-5-(2,1,3-benzoxadiazol-5-ylmethylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
-
-
3-[(5Z)-5-(2H-chromen-3-ylmethylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
-
-
3-[(5Z)-5-(3,5-dichlorobenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
-
-
3-[(5Z)-5-(4-bromobenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
-
-
3-[(5Z)-5-(biphenyl-4-ylmethylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
-
-
3-[(5Z)-5-[(5-chloro-1-benzothiophen-3-yl)methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
-
-
3-[(5Z)-5-[(6,8-dichloro-4-oxo-4H-chromen-3-yl)methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
-
-
3-[(5Z)-5-[4-[3-(dimethylamino)propoxy]benzylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
-
-
dynasore
heterotrimeric G protein betagamma subunit complex
-
oligomerization of dynamin prevents inhibition
-
oligomeric beta-amyloid
-
induces dynamin 1 cleavage and depletion, 0.001 mM of A-705253 potently inhibits oligomeric beta-amyloid-induced dynamin 1 cleavage
-
[(5Z)-4-oxo-5-(quinoxalin-2-ylmethylidene)-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
-
-
[(5Z)-5-(2,1,3-benzothiadiazol-5-ylmethylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
-
-
[(5Z)-5-(2,1,3-benzoxadiazol-5-ylmethylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
-
-
[(5Z)-5-(2H-chromen-3-ylmethylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
-
-
[(5Z)-5-(3,5-dichlorobenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
-
-
[(5Z)-5-(4-bromobenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
-
-
[(5Z)-5-(biphenyl-4-ylmethylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
-
-
[(5Z)-5-[(5-chloro-1-benzothiophen-3-yl)methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
-
-
[(5Z)-5-[(6,8-dichloro-4-oxo-4H-chromen-3-yl)methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
-
-
[(5Z)-5-[4-[3-(dimethylamino)propoxy]benzylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
liposome
liposome-stimulated GTPase activity of Dyn1
-
actin
antibodies
-
stimulate by crosslinking through the C-terminal proline-rich domain of dynamin
-
cardiolipin
ionomycin
a calcium ionophore, causes rapid mitochondrial accumulation of actin filaments followed by Drp1 accumulation at the fission site, and increases fission rate
Mff protein
mitocjondrial protein Mff alone causes only a slight increase in Drp1 GTPase activity at the concentrations tested, while the combination of Mff and actin filaments causes a substantial increase in Drp1 activity, far beyond the additive effects of either Mff or actin alone
-
Mff-proteoliposome
lipid-stimulated GTPase activity
-
microtubule
-
activates GTPase activity
-
mitochondrial fission factor
Mff, stimulates Drp1 independently of, but synergistically with cardiolipin
-
phosphatidylinositol-4,5-bisphosphate
-
activates
Phospholipid
-
mixed-lineage kinase 2-SH2 domain binds dynamin and greatly enhances activation of GTPase by phospholipid
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0034 - 2.115
GTP
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0003 - 3.08
GTP
additional information
additional information
-
kinetic data, temperature-dependent effects on kinetic parameters
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.264
2-chloro-4-(2-dimethylaminopropylamine)-6-methylpyrimidine
Homo sapiens
pH and temperature not specified in the publication
0.3
3-sulfo-N-(2-hydroxyethyl)-1,8-naphthalimide
Homo sapiens
pH 7.4, 37°C
0.509
4-amino-3-sulfo-N-(2-(dimethylamino)ethyl)-1,8-naphthalimide
Homo sapiens
pH 7.4, 37°C
0.155
4-amino-3-sulfo-N-(2-aminobenzyl)-1,8-naphthalimide
Homo sapiens
pH 7.4, 37°C
0.3
4-amino-3-sulfo-N-(2-aminoethyl)-1,8-naphthalimide
Homo sapiens
pH 7.4, 37°C
0.094
4-amino-3-sulfo-N-(2-carboxyethyl)-1,8-naphthalimide
Homo sapiens
pH 7.4, 37°C
0.193
4-amino-3-sulfo-N-(2-hydroxyethyl)-1,8-naphthalimide
Homo sapiens
pH 7.4, 37°C
0.088
4-amino-3-sulfo-N-(3-aminobenzyl)-1,8-naphthalimide
Homo sapiens
pH 7.4, 37°C
0.159
4-amino-3-sulfo-N-(3-hydroxyphenyl)-1,8-naphthalimide
Homo sapiens
pH 7.4, 37°C
0.093
4-amino-3-sulfo-N-(3-hydroxypropyl)-1,8-naphthalimide
Homo sapiens
pH 7.4, 37°C
0.123
4-amino-3-sulfo-N-(4-aminobenzyl)-1,8-naphthalimide
Homo sapiens
pH 7.4, 37°C
0.0185
4-amino-3-sulfo-N-(4-carboxybenzyl)-1,8-naphthalimide
Homo sapiens
pH 7.4, 37°C
0.0448
4-amino-3-sulfo-N-(4-hydroxybenzyl)-1,8-naphthalimide
Homo sapiens
pH 7.4, 37°C
0.296
4-amino-3-sulfo-N-(4-hydroxyphenyl)-1,8-naphthalimide
Homo sapiens
pH 7.4, 37°C
0.113
4-amino-3-sulfo-N-(5-hydroxyhexyl)-1,8-naphthalimide
Homo sapiens
pH 7.4, 37°C
0.062
4-amino-3-sulfo-N-(5-hydroxypentyl)-1,8-naphthalimide
Homo sapiens
pH 7.4, 37°C
0.0191
4-amino-3-sulfo-N-(carboxymethyl)-1,8-naphthalimide
Homo sapiens
pH 7.4, 37°C
0.0703
4-amino-3-sulfo-N-benzyl-1,8-naphthalimide
Homo sapiens
pH 7.4, 37°C
0.3
4-amino-3-sulfo-N-phenyl-1,8-naphthalimide
Homo sapiens
pH 7.4, 37°C
0.3
4-sulfo-N-(2-hydroxyethyl)-1,8-naphthalimide
Homo sapiens
pH 7.4, 37°C
0.327
N1-(4-chloro-6-methylpyrimidin-2-yl)-N3,N3-dimethylpropane-1,3-diamine
Homo sapiens
pH and temperature not specified in the publication
0.05
(5Z)-3-benzyl-5-(3,5-dichlorobenzylidene)-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
pH and temperature not specified in the publication
0.134
(5Z)-3-benzyl-5-(4-bromobenzylidene)-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0074
(5Z)-3-benzyl-5-[(6,8-dichloro-4-oxo-4H-chromen-3-yl)methylidene]-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
pH and temperature not specified in the publication
0.022
(5Z)-3-benzyl-5-[4-[3-(dimethylamino)propoxy]benzylidene]-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0074
(5Z)-5-(2,1,3-benzoxadiazol-5-ylmethylidene)-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
pH and temperature not specified in the publication
0.053
(5Z)-5-(2,1,3-benzoxadiazol-5-ylmethylidene)-3-benzyl-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
pH and temperature not specified in the publication
0.09
(5Z)-5-(2H-chromen-3-ylmethylidene)-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0075
(5Z)-5-(3,5-dichlorobenzylidene)-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
pH and temperature not specified in the publication
0.031
(5Z)-5-(3,5-dichlorobenzylidene)-3-(prop-2-en-1-yl)-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0031
(5Z)-5-(3,5-dichlorobenzylidene)-3-ethyl-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
pH and temperature not specified in the publication
0.043
(5Z)-5-(quinoxalin-2-ylmethylidene)-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0055
(5Z)-5-[(5-chloro-1-benzothiophen-3-yl)methylidene]-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
pH and temperature not specified in the publication
0.029
(5Z)-5-[(6,8-dichloro-4-oxo-4H-chromen-3-yl)methylidene]-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0051
(5Z)-5-[(6,8-dichloro-4-oxo-4H-chromen-3-yl)methylidene]-3-ethyl-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0045
(5Z)-5-[4-[3-(dimethylamino)propoxy]benzylidene]-3-(prop-2-en-1-yl)-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0071
(5Z)-5-[4-[3-(dimethylamino)propoxy]benzylidene]-3-ethyl-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0235
3-[(5Z)-5-(2H-chromen-3-ylmethylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0044
3-[(5Z)-5-(3,5-dichlorobenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.096
3-[(5Z)-5-(4-bromobenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.042
3-[(5Z)-5-(biphenyl-4-ylmethylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.048
3-[(5Z)-5-[(5-chloro-1-benzothiophen-3-yl)methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.01
3-[(5Z)-5-[(6,8-dichloro-4-oxo-4H-chromen-3-yl)methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0055
[(5Z)-5-(3,5-dichlorobenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.073
[(5Z)-5-(biphenyl-4-ylmethylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0123
[(5Z)-5-[(5-chloro-1-benzothiophen-3-yl)methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0034
[(5Z)-5-[(6,8-dichloro-4-oxo-4H-chromen-3-yl)methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
additional information
additional information
Homo sapiens
IC50 values, overview
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
assay at
7 - 7.4
assay at
7 - 8
-
assay at
7.2
-
radioactive assay for the GTPase activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at
23
GTPase and polymerization assay at
30
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22 - 37
-
both the basal and assembly-stimulated rates of GTP hydrolysis for wild-type dynamin are 10fold lower when assayed at 22°C compared with 37°C, effect of these temperatures on the Km
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
isozymes dymain 1, dymanin 2, and dynamin 3
Manually annotated by BRENDA team
-
isozymes dymanin 2 and dynamin 3
Manually annotated by BRENDA team
dynamin 3 participates in the growth and development of megakaryocytes
Manually annotated by BRENDA team
-
isozymes dymanin 2 and dynamin 3
Manually annotated by BRENDA team
invasive bladder cancer cell
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
dynamin 2 localizes with lytic granules and polarizes to the natural killer cell-target interface where it regulates the final fusion of lytic granules with the plasma membrane
Manually annotated by BRENDA team
the enzyme is expressed in the cytoplasm and is partly associated with membranes of the smooth endoplasmic reticulum
Manually annotated by BRENDA team
isozyme dynamin2 only, localization in bladder cancer cells, overview
Manually annotated by BRENDA team
-
dynamin-related protein 1, DRP1
Manually annotated by BRENDA team
Drp1 is a cytosolic protein that translocates to the outer mitochondrial membrane
Manually annotated by BRENDA team
-
dynamin-related protein 1, DRP1
Manually annotated by BRENDA team
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
dynamin is the prototype of a family of large multidomain GTPases. Dynamins and dynamin related proteins constitute a large family of atypical multidomain GTPases that share the common properties of low affinity for guanine nucleotides, high rate of GTP hydrolysis and the ability to oligomerize into helical structures
malfunction
the pleckstrin homology domain (PHD) conformational switch is impaired by a centronuclear myopathy-causing disease mutation, S619L, highlighting the physiological significance of its role in regulating dynamin function
physiological function
evolution
malfunction
metabolism
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DYN1_HUMAN
864
0
97408
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
169624
recombinant enzyme, analytical equilibrium sedimentation analysis
330000
-
recombinant enzyme, gel filtration
40923
x * 40923, nucleotide-free GTPase-GTPase effector domain fusion protein of Drp1, mass spectrometry
45000
-
4 * 80000, SDS-PAGE, 4 * 45000, isolated PH-like domain, SDS-PAGE
80000
-
4 * 80000, SDS-PAGE, 4 * 45000, isolated PH-like domain, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 78000-85000, recombinant enzyme, SDS-PAGE
heterotetramer
-
Dyn1 can interfere with Dyn2 or Dyn2 mutants, Dyn2-Dyn1, Dyn2S45N-Dyn1 and Dyn2-Dyn1I690K heteromers are formed
homotetramer
-
-
monomer
-
1 * isolated GTPase domain, SDS-PAGE
oligomer
in solution, Drp1 exists in a number of oligomeric states, including dimers, tetramers, and higher-order oligomers. Actin filaments can organize Drp1 into a productive oligomer
tetramer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
actin filaments target the oligomeric maturation of the dynamin GTPase Drp1 to mitochondrial fission sites
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
GTPase domain and the bundle signalling element of dynamin in the GDP-bound state, GG1, hanging drop vapour diffusion method, mixing of 0.0015 ml of 10 mg/ml GG1 protein solution containing 2 mM GDP and 2 mM MgCl2 with 0.0015 ml of reservoir solution containing 0.1 M Tris, pH 8.0, 26% PEG 3350, and 0.2 M NaSCN, and equilibration against 0.7 ml of reservoir solution, one week, 4°C, X-ray diffraction structure determination and analysis at 1.7-1.8 A resolution, molecular replacement using GG1GDP.AlFx (PDB ID 2X2E) as search model
purified recombinant dynamin-related protein 1 GTPase-GTPase effector domain fusion protein, sitting drop vapour diffusion method, mixing of 0.0004 ml of protein solution and reservoir solution, the latter containing 0.2 M lithium sulfate, 0.1 M Bis-Tris, pH 5.5, 25% v/v PEG 3350 or 0.1 M sodium citrate, pH 5.5, 20% PEG 3000, 20°C, X-ray diffraction structure determination and analysis at 2.67 A resolution
purified wild-type and mutants of DNM1L isoform 2, mixing of 0.001 ml of 1.2 mg/ml protein with 0.001 ml of reservoir solution containing 0.1 M sodium citrate pH 5, 27.5% PEG 3000, equilibration against 0.4 ml of reservoir solution, 3-5 days, for co-crystallization of the enzyme with a non-hydrolyzable GTP analogue the protein is incubated with 1 mM GMP-PNP and 4 mM MgCl2, and then purified by gel filtration, X-ray diffraction structure determination and analysis at 2.3 A resolution, molecular replacement using human dynamin-1 structure, PDB ID 3SNH
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K44A
dominant-negative dynamin mutant
S619L
site-directed mutagenesis, the pleckstrin homology domain (PHD) conformational switch is impaired by the centronuclear myopathy-causing disease mutation. The temperature-sensitive phenotype of the Dyn1S619L mutant reflects temperature-sensitive changes in the steady-state conformation(s) adopted by the PHD
Y354C
site-directed mutagenesis, interaction analysis with Dyn2L354C-IAEDANS mutant, membrane binding and consequent opening of PHD in mutants Dyn1Y354C-IAEDANS and Dyn2L354C-IAEDANS, overview
D146A
site-directed mutagenesis
D190A
site-directed mutagenesis
D218A
site-directed mutagenesis
D250N
site-directed mutagenesis, a monomeric mutant, loss of nucleotide binding
D253N
site-directed mutagenesis, a monomeric mutant
DynII690K
-
point mutation to render Dyn1 defective in oligomerization and self-assembly
E81A
site-directed mutagenesis
E81A/E82A
site-directed mutagenesis
G149A
site-directed mutagenesis
G255E
site-directed mutagenesis, a monomeric mutant
G350D
-
middle domain mutant, the mutant shows impaired GTPase activity, but unaffected protein tetramerization and liposome-binding properties
I697A
-
mutation inhibits oligomerization substantially
K216A
site-directed mutagenesis
K83A
site-directed mutagenesis, the mutant shows reduced dimerization
M527D
site-directed mutagenesis, a monomeric mutant
M527D/D250N
site-directed mutagenesis, a monomeric mutant
M527D/D250N/D253N
site-directed mutagenesis, a monomeric mutant
M527D/D253N
site-directed mutagenesis, a monomeric mutant
M527D/K83A
site-directed mutagenesis, a monomeric mutant
M527D/T103A
site-directed mutagenesis, a monomeric mutant
N246A
site-directed mutagenesis
Q34A
site-directed mutagenesis
R365S
-
middle domain mutant, the mutant shows impaired GTPase activity, but unaffected protein tetramerization and liposome-binding properties
R399A
-
the mutant displays a severe defect in quaternary structure in solution and on membranes, no detectable membrane tubulation is observed with R399A, nor is R399A capable of mediating membrane fission, R399A is also unable to inhibit fission catalyzed by wild type dynamin
S35A
site-directed mutagenesis
S39A
site-directed mutagenesis
S40A
site-directed mutagenesis
S45N
-
the mutant is defective in GTP binding
S61A
-
mutation lowers the rate of assembly-stimulated GTP hydrolysis without altering the Km for GTP, kinetic data
S61D
-
kinetic data
T103A
site-directed mutagenesis, a monomeric mutant
T141A
-
mutation increases the rate of assembly-stimulated GTP hydrolysis without altering the Km for GTP, kinetic data
T141D
-
kinetic data
T59A
site-directed mutagenesis
T65A
-
mutation dramatically lowers both the rate of assembly-stimulated GTP hydrolysis and the affinity for GTP, kinetic data
T65D
-
mutation dramatically lowers both the rate of assembly-stimulated GTP hydrolysis and the affinity for GTP, kinetic data
T65H
-
mutation dramatically lowers both the rate of assembly-stimulated GTP hydrolysis and the affinity for GTP, kinetic data
V268M
site-directed mutagenesis, the mutant shows reduced dimerization
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant dynamin 1 GTPase domain GG1 from Escherichia coli strain BL21 (DE3) by glutathione affinity chromatography, tag cleavage by TEV protease, ultrafiltration, and gel filtration
recombinant dynamin-1
-
recombinant GST- and His-tagged MxA from Escherichia coli strain BL21(DE3) by nickel affinity and glutathione affinity chromatography, and gel filtration
recombinant His-tagged DLP-1 isozyme 2 from Escherichia coli strain C41 (DE3) by nickel affinity chromatography, anion exchange chromatography, and gel filtration
-
recombinant N-terminally Strep-tagged Drp1 from Escherichia coli strain BL21 Star (DE3) by affinity chromatography, followed by tag cleavage by HRV3C protease, and gel filtration
recombinant N-terminally Strep-tagged Drp1 from Saccharomyces cerevisiae strain JSY9612 by affinity chromatography, followed by tag cleavage by PreScission protease, and dialysis
recombinant nucleotide-free GTPase-GTPase effector domain fusion protein of human Drp1, and wild-type and mutant full-length enzymes from Escherichia coli strain BL21(DE3)
recombinant wild-type and K44A mutant dynamin-1, expressed in Sf9 cells
-
using Ni-NTA and hydroxyapatite chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in a fibroblastoid cell line and in embryonic stem cells
gene DNM1, recombinant expression of the dynamin 1 GTPase domain GG1 from modified pGEX-4T1 vector containing a TEV protease site. The fragments are connected by a linker composed of eight amino acid residues (KHGTDSRV) in Escherichia coli strain BL21 (DE3)
a 6-His N-terminal-tagged human dynamin2, lacking the C-terminal proline-rich domain, is constructed, cloned into the pET28a vector for expression in Escherichia coli BL21DE3 cells
-
dynamin 2 genotyping
expressed in CHO cells
-
expressed in umbilical cord blood CD34+ cells
expressed in Vero cells
expression in COS-7 cells
-
expression of His-tagged DLP-1 isozyme 2 in Escherichia coli strain C41 (DE3)
-
expression of wild-type and K44A mutant dynamin in HeLa cells
-
expression of wild-type and K44A mutant dynamin-1 in HeLa cells and in Sf9 cells
-
gene DNM1, recombinant expression of Drp1 containing an N-terminal PreScission protease cleavage site and a FLAG-One-Strep-tag (IBA) from plasmid pRS415-DNM1 in Saccharomyces cerevisiae strain JSY9612 lacking all fission proteins (MATa, can1, ade2, trp1, ura3, his3, leu2, pep4::HIS3, prb1::LEU2, bar1::HISG, lys2::GAL1/10-GAL4), coexpression with Saccharomyces cerevisiae mitochondrial fission 1 protein, Fis1 (UniProt ID P40515)
gene DNM2, enzyme expression analysis
gene DNMTL1, recombinant expression of the splice variants of Drp1 in Escherichia coli strain BL21 Star (DE3)
gene for dynamin1, expression in HEK293-cre4 cells
-
human dynamin is expressed in SF9 insect cells, using the Bac-to-Bac baculovirus expression system a full-length cDNA encoding human dynamin1 containing a 6His-tag is subcloned into pFastBac, a bacmid is generated after transposition in Escherichia coli
-
overexpression in Chineses hamster ovary cells
-
overexpression of human neuronal dynamin in Sf9 insect cells
-
recombinant expression of C-terminally His6-tagged wild-type and mutants of DNM1L isoform 2
recombinant expression of GST- and His-tagged MxA in Escherichia coli strain BL21(DE3)
recombinant expression of N-terminally Strep-tagged Drp1 with an HRV3C protease site from pET16b vector in Escherichia coli strain BL21 Star (DE3), stable recombinant expression of GFP-tagged DrpI in U2OS cells with partial shRNA suppression of endogenous Drp1 (gDrp-U2OS), GFP-Drp1 functionally compensates for endogenous Drp1 in these cells
recombinant expression of nucleotide-free GTPase-GTPase effector domain fusion protein of enzyme Drp1, and wild-type and mutant full-length enzymes in Escherichia coli strain BL21(DE3)
the vectors pcDNA3.1 and pADT3T7tet are used, recombinant adenoviruses are produced in HEK293-Cre cells
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rasmussen, R.K.; Rusak, J.; Price, G.; Robinson, P.J.; Simpson, R.J.; Dorow, D.S.
Mixed-lineage kinase 2-SH2 domain binds dynamin and greatly enhances activation of GTPase by phospholipid
Biochem. J.
335
119-124
1998
Ovis aries, Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Lin, H.C.; Gilman, A.G.
Regulation of dynamin I GTPase activity by G protein betagamma subunits and phosphatidylinositol 4,5-bisphosphate
J. Biol. Chem.
271
27979-27982
1996
Bos taurus, Homo sapiens
Manually annotated by BRENDA team
Warnock, D.E.; Terlecky, L.J.; Schmid, S.L.
Dynamin GTPase is stimulated by crosslinking through the C-terminal proline-rich domain
EMBO J.
14
1322-1328
1995
Homo sapiens
Manually annotated by BRENDA team
Fish, K.N.; Schmid, S.L.; Damke, H.
Evidence that dynamin-2 functions as a signal-transducing GTPase
J. Cell Biol.
150
145-154
2000
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Omata, W.; Shibata, H.; Suzuki, Y.; Tanaka, S.; Suzuki, T.; Takata, K.; Kojima, I.
Subcellular distribution of GLUT4 in Chineses hamster ovary cells overexpressing mutant dynamin: evidence that dynamin is a regulatory GTPase in GLUT4 endocytosis
Biochem. Biophys. Res. Commun.
241
401-406
1997
Homo sapiens
Manually annotated by BRENDA team
Warnock, D.E.; Schmid, S.L.
Dynamin GTPase, a force-generating molecular switch
Bioessays
18
885-893
1996
Drosophila sp. (in: flies), Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Wilkowsky, S.E.; Barbieri, M.A.; Stahl, P.D.; Isola, E.L.D.
Regulation of Trypanosoma cruzi invasion of nonphagocytic cells by the endocytically active GTPases dynamin, Rab5, and Rab7
Biochem. Biophys. Res. Commun.
291
516-521
2002
Homo sapiens
Manually annotated by BRENDA team
Song, B.D.; Leonard, M.; Schmid, S.L.
Dynamin GTPase domain mutants that differentially affect GTP binding, GTP hydrolysis, and clathrin-mediated endocytosis
J. Biol. Chem.
279
40431-40436
2004
Homo sapiens
Manually annotated by BRENDA team
Damke, H.; Baba, T.; Warnock, D.E.; Schmid, S.L.
Induction of mutant dynamin specifically blocks endocytic coated vesicle formation
J. Cell. Biol.
127
915-934
1994
Homo sapiens
Manually annotated by BRENDA team
Macia, E.; Ehrlich, M.; Massol, R.; Boucrot, E.; Brunner, C.; Kirchhausen, T.
Dynasore, a cell-permeable inhibitor of dynamin
Dev. Cell
10
839-850
2006
Homo sapiens
Manually annotated by BRENDA team
Chugh, J.; Chatterjee, A.; Kumar, A.; Mishra, R.K.; Mittal, R.; Hosur, R.V.
Structural characterization of the large soluble oligomers of the GTPase effector domain of dynamin
FEBS J.
273
388-397
2006
Homo sapiens
Manually annotated by BRENDA team
Ivanov, V.N.; Ronai, Z.; Hei, T.K.
Opposite roles of FAP-1 and dynamin in the regulation of Fas (CD95) translocation to the cell surface and susceptibility to Fas ligand-mediated apoptosis
J. Biol. Chem.
281
1840-1852
2006
Homo sapiens
Manually annotated by BRENDA team
Sauvonnet, N.; Dujeancourt, A.; Dautry-Varsat, A.
Cortactin and dynamin are required for the clathrin-independent endocytosis of gammac cytokine receptor
J. Cell Biol.
168
155-163
2005
Homo sapiens
Manually annotated by BRENDA team
Varadi, A.; Johnson-Cadwell, L.I.; Cirulli, V.; Yoon, Y.; Allan, V.J.; Rutter, G.A.
Cytoplasmic dynein regulates the subcellular distribution of mitochondria by controlling the recruitment of the fission factor dynamin-related protein-1
J. Cell Sci.
117
4389-4400
2004
Homo sapiens
Manually annotated by BRENDA team
Sever, S.; Skoch, J.; Bacskai, B.J.; Newmyer, S.L.
Assays and functional properties of auxilin-dynamin interactions
Methods Enzymol.
404
570-585
2005
Homo sapiens
Manually annotated by BRENDA team
Praefcke, G.J.; McMahon, H.T.
The dynamin superfamily: universal membrane tubulation and fission molecules?
Nat. Rev. Mol. Cell Biol.
5
133-147
2004
Homo sapiens, Drosophila melanogaster (P27619), Drosophila melanogaster, Arabidopsis thaliana (Q9SE83), Arabidopsis thaliana, Caenorhabditis elegans (Q9U9I9), Caenorhabditis elegans
Manually annotated by BRENDA team
Soulet, F.; Schmid, S.L.; Damke, H.
Domain requirements for an endocytosis-independent, isoform-specific function of dynamin-2
Exp. Cell Res.
312
3539-3545
2006
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Kirchhausen, T.; Macia, E.; Pelish, H.E.
Use of dynasore, the small molecule inhibitor of dynamin, in the regulation of endocytosis
Methods Enzymol.
438
77-93
2008
Homo sapiens
Manually annotated by BRENDA team
Bosch, B.; Grigorov, B.; Senserrich, J.; Clotet, B.; Darlix, J.L.; Muriaux, D.; Este, J.A.
A clathrin-dynamin-dependent endocytic pathway for the uptake of HIV-1 by direct T cell-T cell transmission
Antiviral Res.
80
185-193
2008
Homo sapiens (P50570)
Manually annotated by BRENDA team
Vela, E.M.; Colpitts, T.M.; Zhang, L.; Davey, R.A.; Aronson, J.F.
Pichinde virus is trafficked through a dynamin 2 endocytic pathway that is dependent on cellular Rab5- and Rab7-mediated endosomes
Arch. Virol.
153
1391-1396
2008
Homo sapiens (P50570)
Manually annotated by BRENDA team
Liu, X.; Yuan, Z.; Chung, M.
MUC1 intra-cellular trafficking is clathrin, dynamin, and rab5 dependent
Biochem. Biophys. Res. Commun.
376
688-693
2008
Homo sapiens
Manually annotated by BRENDA team
Pucadyil, T.J.; Schmid, S.L.
Real-time visualization of dynamin-catalyzed membrane fission and vesicle release
Cell
135
1263-1275
2008
Homo sapiens
Manually annotated by BRENDA team
Bashkirov, P.V.; Akimov, S.A.; Evseev, A.I.; Schmid, S.L.; Zimmerberg, J.; Frolov, V.A.
GTPase cycle of dynamin is coupled to membrane squeeze and release, leading to spontaneous fission
Cell
135
1276-1286
2008
Homo sapiens
Manually annotated by BRENDA team
Reems, J.A.; Wang, W.; Tsubata, K.; Abdurrahman, N.; Sundell, B.; Tijssen, M.R.; van der Schoot, E.; Di Summa, F.; Patel-Hett, S.; Italiano, J.; Gilligan, D.M.
Dynamin 3 participates in the growth and development of megakaryocytes
Exp. Hematol.
36
1714-1727
2008
Homo sapiens (Q9UQ16), Homo sapiens
Manually annotated by BRENDA team
Shin, N.; Ahn, N.; Chang-Ileto, B.; Park, J.; Takei, K.; Ahn, S.G.; Kim, S.A.; Di Paolo, G.; Chang, S.
SNX9 regulates tubular invagination of the plasma membrane through interaction with actin cytoskeleton and dynamin 2
J. Cell Sci.
121
1252-1263
2008
Homo sapiens
Manually annotated by BRENDA team
Arneson, L.N.; Segovis, C.M.; Gomez, T.S.; Schoon, R.A.; Dick, C.J.; Lou, Z.; Billadeau, D.D.; Leibson, P.J.
Dynamin 2 regulates granule exocytosis during NK cell-mediated cytotoxicity
J. Immunol.
181
6995-7001
2008
Homo sapiens
Manually annotated by BRENDA team
Liu, Y.W.; Surka, M.C.; Schroeter, T.; Lukiyanchuk, V.; Schmid, S.L.
Isoform and splice-variant specific functions of dynamin-2 revealed by analysis of conditional knock-out cells
Mol. Biol. Cell
19
5347-5359
2008
Rattus norvegicus (P21575), Rattus norvegicus (P39052), Rattus norvegicus (Q08877), Homo sapiens (Q05193)
Manually annotated by BRENDA team
Fernandez, N.; Monczor, F.; Baldi, A.; Davio, C.; Shayo, C.
Histamine H2 receptor trafficking: role of arrestin, dynamin, and clathrin in histamine H2 receptor internalization
Mol. Pharmacol.
74
1109-1118
2008
Homo sapiens
Manually annotated by BRENDA team
Sinjoanu, R.C.; Kleinschmidt, S.; Bitner, R.S.; Brioni, J.D.; Moeller, A.; Ferreira, A.
The novel calpain inhibitor A-705253 potently inhibits oligomeric beta-amyloid-induced dynamin 1 and tau cleavage in hippocampal neurons
Neurochem. Int.
53
79-88
2008
Homo sapiens
Manually annotated by BRENDA team
Robertson, M.; Hadzic, G.; Ambrus, J.; Pome, D.; Hyde, E.; Whiting, A.; Mariana, A.; Von Kleist, L.; Chau, N.; Haucke, V.; Robinson, P.; McCluskey, A.
The rhodadyns, a new class of small molecule inhibitors of dynamin GTPase activity
ACS Med. Chem. Lett.
3
352-356
2012
Homo sapiens
Manually annotated by BRENDA team
Zhang, Y.; Gao, X.; Garavito, R.M.
Biochemical characterization of human dynamin-like protein 1
J. Biochem.
150
627-633
2011
Homo sapiens
Manually annotated by BRENDA team
Ferguson, S.M.; De Camilli, P.
Dynamin, a membrane-remodelling GTPase
Nat. Rev. Mol. Cell Biol.
13
75-88
2012
Caenorhabditis elegans, Drosophila melanogaster, Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Klinglmayr, E.; Wenger, J.; Mayr, S.; Bossy-Wetzel, E.; Puehringer, S.
Purification, crystallization and X-ray diffraction analysis of human dynamin-related protein 1 GTPase-GED fusion protein
Acta Crystallogr. Sect. F
68
1217-1221
2012
Homo sapiens (O00429), Homo sapiens
Manually annotated by BRENDA team
Belenguer, P.; Pellegrini, L.
The dynamin GTPase OPA1: more than mitochondria?
Biochim. Biophys. Acta
1833
176-183
2013
Homo sapiens (O60313), Mus musculus (P58281)
Manually annotated by BRENDA team
Boehm, J.; Biancalana, V.; Dechene, E.T.; Bitoun, M.; Pierson, C.R.; Schaefer, E.; Karasoy, H.; Dempsey, M.A.; Klein, F.; Dondaine, N.; Kretz, C.; Haumesser, N.; Poirson, C.; Toussaint, A.; Greenleaf, R.S.; Barger, M.A.; Mahoney, L.J.; Kang, P.B.; Zanoteli, E.; Vissing, J.; Witting, N.; Echaniz-Laguna, A.
Mutation spectrum in the large GTPase dynamin 2, and genotype-phenotype correlation in autosomal dominant centronuclear myopathy
Hum. Mutat.
33
949-959
2012
Homo sapiens (P50570)
Manually annotated by BRENDA team
Dick, A.; Graf, L.; Olal, D.; von der Malsburg, A.; Gao, S.; Kochs, G.; Daumke, O.
Role of nucleotide binding and GTPase domain dimerization in dynamin-like myxovirus resistance protein A for GTPase activation and antiviral activity
J. Biol. Chem.
290
12779-12792
2015
Homo sapiens (P20591), Homo sapiens
Manually annotated by BRENDA team
Abdel-Hamid, M.K.; Macgregor, K.A.; Odell, L.R.; Chau, N.; Mariana, A.; Whiting, A.; Robinson, P.J.; McCluskey, A.
1,8-Naphthalimide derivatives: new leads against dynamin I GTPase activity
Org. Biomol. Chem.
13
8016-8028
2015
Homo sapiens (Q05193)
Manually annotated by BRENDA team
Wenger, J.; Klinglmayr, E.; Froehlich, C.; Eibl, C.; Gimeno, A.; Hessenberger, M.; Puehringer, S.; Daumke, O.; Goettig, P.
Functional mapping of human dynamin-1-like GTPase domain based on x-ray structure analyses
PLoS ONE
8
e71835
2013
Homo sapiens (O00429), Homo sapiens
Manually annotated by BRENDA team
Anand, R.; Eschenburg, S.; Reubold, T.F.
Crystal structure of the GTPase domain and the bundle signalling element of dynamin in the GDP state
Biochem. Biophys. Res. Commun.
469
76-80
2016
Homo sapiens (Q05193)
Manually annotated by BRENDA team
Zhang, Y.; Nolan, M.; Yamada, H.; Watanabe, M.; Nasu, Y.; Takei, K.; Takeda, T.
Dynamin2 GTPase contributes to invadopodia formation in invasive bladder cancer cells
Biochem. Biophys. Res. Commun.
480
409-414
2016
Rattus norvegicus (P39052), Homo sapiens (P50570), Homo sapiens
Manually annotated by BRENDA team
Ji, W.K.; Hatch, A.L.; Merrill, R.A.; Strack, S.; Higgs, H.N.
Actin filaments target the oligomeric maturation of the dynamin GTPase Drp1 to mitochondrial fission sites
eLife
4
e11553
2015
Homo sapiens (O00429)
Manually annotated by BRENDA team
Srinivasan, S.; Dharmarajan, V.; Reed, D.K.; Griffin, P.R.; Schmid, S.L.
Identification and function of conformational dynamics in the multidomain GTPase dynamin
EMBO J.
35
443-457
2016
Homo sapiens (Q05193)
Manually annotated by BRENDA team
Macdonald, P.J.; Francy, C.A.; Stepanyants, N.; Lehman, L.; Baglio, A.; Mears, J.A.; Qi, X.; Ramachandran, R.
Distinct splice variants of dynamin-related protein 1 differentially utilize mitochondrial fission factor as an effector of cooperative GTPase activity
J. Biol. Chem.
291
493-507
2016
Homo sapiens (O00429), Rattus norvegicus (O35303)
Manually annotated by BRENDA team
Odell, L.R.; Abdel-Hamid, M.K.; Hill, T.A.; Chau, N.; Young, K.A.; Deane, F.M.; Sakoff, J.A.; Andersson, S.; Daniel, J.A.; Robinson, P.J.; McCluskey, A.
Pyrimidine-based inhibitors of dynamin I GTPase activity competitive inhibition at the pleckstrin homology domain
J. Med. Chem.
60
349-361
2017
Homo sapiens (Q05193)
Manually annotated by BRENDA team
Koirala, S.; Guo, Q.; Kalia, R.; Bui, H.T.; Eckert, D.M.; Frost, A.; Shaw, J.M.
Interchangeable adaptors regulate mitochondrial dynamin assembly for membrane scission
Proc. Natl. Acad. Sci. USA
110
E1342-E1351
2013
Homo sapiens (O00429), Saccharomyces cerevisiae (P54861), Saccharomyces cerevisiae
Manually annotated by BRENDA team