Literature summary for 4.1.1.15 extracted from

Chen, C.H.; Battaglioli, G.; Martin, D.L.; Hobart, S.A.; Colon, W.
Distinctive interactions in the holoenzyme formation for two isoforms of glutamate decarboxylase (2003), Biochim. Biophys. Acta, 1645, 63-71.

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Organism

Organism	UniProt	Comment	Textmining
Rattus norvegicus	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
brain	-	Rattus norvegicus	-

Cofactor

Cofactor	Comment	Organism	Structure
pyridoxal 5'-phosphate	slower binding of pyridoxal 5'-phosphate to GAD67 than to GAD65, and less ease to dissociate pyridoxal 5'-phosphate from holoGAD67 than holoGAD54. TGAD67 is more highly saturated by the cofactor than GAD65. The two binding sites of GAD65 exhibit similar affinities for pyridoxal 5'-phosphate. One binding site of GAD67 exhibits a significantly higher affinity for pyridoxal 5'-phosphate than the other binding site	Rattus norvegicus

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Release 2023.1 (January 2023)