Literature summary for 3.6.5.6 extracted from

Buey, R.M.; Diaz, J.F.; Andreu, J.M.
The nucleotide switch of tubulin and microtubule assembly: a polymerization-driven structural change (2006), Biochemistry, 45, 5933-5938.

Search for more literature for 3.6.5.6

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
GTP + H2O	Rattus norvegicus	GTP-binding proteins from the tubulin family, including alpha,beta-tubulin are key components of the cytoskeleton and play central roles in chromosome segregation and cell division. The nucleotide switch of alpha,beta-tubulin is triggered by GTP hydrolysis and regulates microtubule assembly dynamics. Unassembled tubulin-GTP is in the inactive, curved conformation as in tubulin-GDP rings, and is driven into the straight microtubule conformation by the assembly contacts. Binding of the GTP gamma-phosphate only lowers the free energy difference between the curved and straight forms	GDP + phosphate	-	?
GTP + H2O	Bos taurus	GTP-binding proteins from the tubulin family, including alpha,beta-tubulin are key components of the cytoskeleton and play central roles in chromosome segregation and cell division. The nucleotide switch of alpha,beta-tubulin is triggered by GTP hydrolysis and regulates microtubule assembly dynamics. Unassembled tubulin-GTP is in the inactive, curved conformation as in tubulin-GDP rings, and is driven into the straight microtubule conformation by the assembly contacts. Binding of the GTP gamma-phosphate only lowers the free energy difference between the curved and straight forms	GDP + phosphate	-	?

Organism

Organism	UniProt	Comment	Textmining
Bos taurus	-	-	-
Rattus norvegicus	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
brain	-	Rattus norvegicus	-
brain	-	Bos taurus	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
GTP + H2O	-	Rattus norvegicus	GDP + phosphate	-	?
GTP + H2O	-	Bos taurus	GDP + phosphate	-	?
GTP + H2O	GTP-binding proteins from the tubulin family, including alpha,beta-tubulin are key components of the cytoskeleton and play central roles in chromosome segregation and cell division. The nucleotide switch of alpha,beta-tubulin is triggered by GTP hydrolysis and regulates microtubule assembly dynamics. Unassembled tubulin-GTP is in the inactive, curved conformation as in tubulin-GDP rings, and is driven into the straight microtubule conformation by the assembly contacts. Binding of the GTP gamma-phosphate only lowers the free energy difference between the curved and straight forms	Rattus norvegicus	GDP + phosphate	-	?
GTP + H2O	GTP-binding proteins from the tubulin family, including alpha,beta-tubulin are key components of the cytoskeleton and play central roles in chromosome segregation and cell division. The nucleotide switch of alpha,beta-tubulin is triggered by GTP hydrolysis and regulates microtubule assembly dynamics. Unassembled tubulin-GTP is in the inactive, curved conformation as in tubulin-GDP rings, and is driven into the straight microtubule conformation by the assembly contacts. Binding of the GTP gamma-phosphate only lowers the free energy difference between the curved and straight forms	Bos taurus	GDP + phosphate	-	?

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Release 2023.1 (January 2023)