Literature summary for 1.4.1.3 extracted from

Kato, Y.; Kihara, H.; Fukui, K.; Kojima, M.
A ternary complex model of sirtuin4-NAD+-glutamate dehydrogenase (2018), Comput. Biol. Chem., 74, 94-104 .

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Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
mitochondrion	-	Homo sapiens	5739	-

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P00367	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
additional information	the ADP-ribosylation of glutamate dehydrogenase is catalyzed by Sirt4, and downregulates the TCA cycle. In the ternary complex model of Sirt4-NAD+-GDH, the acetylated lysine 171 of GDH is located close to NAD+. This suggests a possible mechanism underlying the ADP-ribosylation at cysteine 172, which may occur through a transient intermediate with ADP-ribosylation at the acetylated lysine 171	Homo sapiens

General Information

General Information	Comment	Organism
drug target	the ADP-ribosylation of glutamate dehydrogenase is catalyzed by Sirt4, and downregulates the TCA cycle. In the ternary complex model of Sirt4-NAD+-GDH, the acetylated lysine 171 of GDH is located close to NAD+. This suggests a possible mechanism underlying the ADP-ribosylation at cysteine 172, which may occur through a transient intermediate with ADP-ribosylation at the acetylated lysine 171	Homo sapiens

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Release 2023.1 (January 2023)