Literature summary for 3.6.5.5 extracted from

Narayanan, R.; Leonard, M.; Song, B.D.; Schmid, S.L.; Ramaswami, M.
An internal GAP domain negatively regulates presynaptic dynamin in vivo: a two-step model for dynamin function (2005), J. Cell Biol., 169, 117-126.

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Protein Variants

Protein Variants	Comment	Organism
additional information	mutations in shibire, the Drosophila dynamin, cause temperature-sensitive defects in endocytosis. The ts2 mutation, which occurs in the switch 2 region of dynamins GTPase domain, compromises GTP binding affinity. Three second-site suppressor mutations, one in the switch 1 region of the GTPase domain and two in the GTPase effector domain, dynamins putative GAP, fully rescue the shi ts2 defects in synaptic vesicle recycling	Drosophila sp. (in: flies)

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
GTP + H2O	Drosophila sp. (in: flies)	-	GDP + phosphate	-	?

Organism

Organism	UniProt	Comment	Textmining
Drosophila sp. (in: flies)	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
GTP + H2O	-	Drosophila sp. (in: flies)	GDP + phosphate	-	?

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Release 2023.1 (January 2023)