Literature summary for 2.7.11.26 extracted from

Ranganadha Reddy, A.; Venkateswarulu, T.; John Babu, D.; Shyamala Devi, N.
Homology modeling, simulation and docking studies of Tau-protein kinase (2014), Res. J. Pharm. Technol., 7, 376-388.

No PubMed abstract available

Search for more literature for 2.7.11.26

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + [tau-protein]	Homo sapiens	-	ADP + O-phospho-[tau-protein]	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
brain	-	Homo sapiens	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + [tau-protein]	-	Homo sapiens	ADP + O-phospho-[tau-protein]	-	?
ATP + [tau-protein]	the enzyme is a serine/threonine protein kinase	Homo sapiens	ADP + O-phospho-[tau-protein]	-	?

Synonyms

Synonyms	Comment	Organism
tauprotein kinase	-	Homo sapiens

Cofactor

Cofactor	Comment	Organism	Structure
ATP	-	Homo sapiens

General Information

General Information	Comment	Organism
additional information	homology modeling, simulation and docking studies with L-glutamic acid, memantine, tacrine, and ropinirol ligands, of Tau-protein kinase, overview	Homo sapiens
physiological function	the pathogenesis of Alzheimer's disease includes hyperphosphorylation of tau protein which results in the self-assembly of tangles of paired helical fragments and straight filaments. Defective tau protein causes the dementia leading to Alzheimer's disease	Homo sapiens

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)