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Information on EC 3.6.5.5 - dynamin GTPase and Organism(s) Drosophila melanogaster and UniProt Accession P27619

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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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This record set is specific for:
Drosophila melanogaster
UNIPROT: P27619
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Word Map
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The taxonomic range for the selected organisms is: Drosophila melanogaster
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
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GTP
+
H2O
=
GDP
+
phosphate
+
=
+
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
B-dynamin
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-
-
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D100
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-
-
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Dyn2aa
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isoform
Dyn2ab
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isoform
dynamin 1
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isoform, originally identified as a microtubule-binding protein
dynamin 2
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isoform, plays a key role in endocytosis, actin dynamics, and membrane trafficking and is the only isoform that functions during cytokinesis
dynamin 3
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isoform
Dynamin BREDNM19
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-
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Dynamin UDNM
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-
-
-
Dynamin, brain
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-
-
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Dynamin, testicular
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-
-
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GTP phosphohydrolase
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GTPase
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GTPase dynamin
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guanine triphosphatase
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-
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guanosine 5'-triphosphatase
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guanosine triphosphatase
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phosphatase, guanosine tri-
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ribosomal GTPase
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Shibire protein
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T-dynamin
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
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-
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
?
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-
dynamin is a midbody protein associated with membrane remodelling that is also required for cytokinesis. Dynamin may also function as a link between the plasma membrane and actin filaments through interactions with proteins like Abp1, profilin, or cortacin. Alternatively, dynamin assembled on plasma membranes can act as structural component that organizes and stabilizes acti filaments at the furrow membrane, therefore being a platform from which the contractile ring forms.
-
-
?
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
involved in vesicle scission
-
-
?
additional information
?
-
-
dynamin is a midbody protein associated with membrane remodelling that is also required for cytokinesis. Dynamin may also function as a link between the plasma membrane and actin filaments through interactions with proteins like Abp1, profilin, or cortacin. Alternatively, dynamin assembled on plasma membranes can act as structural component that organizes and stabilizes acti filaments at the furrow membrane, therefore being a platform from which the contractile ring forms.
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
dynamin is a general component of clathrin-coated endocytic pits
Manually annotated by BRENDA team
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isoform Dyn2aa is localized to plasma membrane and Golgi apparatus
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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dynamin gene muta­tions are responsible for the temperature-sensitive paralytic phenotype of Drosophila melanogaster shibire mutants. The mutants show paralysis resulting from the neuronal activity-dependent depletion of synaptic vesicles, which is accompanied by the accumulation of arrested collared endocytic pits at the presynaptic plasma membrane
metabolism
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GTPase dynamin is the founding member of a family of GTPases that have diverse roles in membrane-remodelling events through­out the cell
physiological function
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dynamin drives membrane fission, mechanism, overview. Dynamin is directly involved in the generation of an endocytic vesicle requiring the recruitment of various proteins from the cytosol that orchestrate the bending inward of the plasma membrane to form a deeply invaginated bud and subsequently promote its fission. Dynamin assembles into helical polymers at the necks of budding vesicles and its GTP hydrolysis-dependent conformational change promotes fission of the under­lying tubular membrane to generate a free endocytic vesicle. It acts at fission sites for clathrin-mediated endocytosis. Dynamin interacts both directly and indirectly with the cytoskeleton, overview
additional information
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structure-function relationship, overview. Many proteins that bind dynamin's Pro-rich domain via an SRC homology 3 domain also contain Bin-amphiphysin-Rvs, i.e. BAR, domains, which are protein modules with curvature-generating and -sensing properties
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DYN_DROME
877
0
97809
Swiss-Prot
other Location (Reliability: 4)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
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a dimer of dimers, the stalk of dynamin dimerizes in a cross-like fashion to yield a dynamin dimer in which the two G domains are oriented in opposite directions
additional information
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structure-function relationship, overview. Domain organization, dynamin has an N-terminal G domain, a middle or stalk region, a pleckstrin homology PH domain, a GTPase effector domain GED, interacting with the G domain, and a C-terminal Pro-rich region, PRD
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Bonner, M.K.; Skop, A.R.
Cell division screens and dynamin
Biochem. Soc. Trans.
36
431-435
2008
Danio rerio, Saccharomyces cerevisiae, Caenorhabditis elegans, Caenorhabditis elegans (P39055), Drosophila melanogaster
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