Literature summary extracted from

Ramon-Maiques, S.; Fernandez-Murga, M.L.; Gil-Ortiz, F.; Vagin, A.; Fita, I.; Rubio, V.
Structural bases of feed-back control of arginine biosynthesis, revealed by the structures of two hexameric N-acetylglutamate kinases, from Thermotoga maritima and Pseudomonas aeruginosa (2006), J. Mol. Biol., 356, 695-713.

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
2.7.2.8	in complex with arginine	Thermotoga maritima
2.7.2.8	without arginine	Pseudomonas aeruginosa

Inhibitors

EC Number	Inhibitors	Comment	Organism	Structure
2.7.2.8	arginine	-	Pseudomonas aeruginosa
2.7.2.8	arginine	-	Thermotoga maritima

Organism

EC Number	Organism	UniProt	Comment	Textmining
2.7.2.8	Pseudomonas aeruginosa	Q9HTN2	-	-
2.7.2.8	Thermotoga maritima	Q9X2A4	-	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2.7.2.8	ATP + N-acetyl-L-glutamate	-	Thermotoga maritima	ADP + N-acetyl-L-glutamate 5-phosphate	-	?
2.7.2.8	ATP + N-acetyl-L-glutamate	-	Pseudomonas aeruginosa	ADP + N-acetyl-L-glutamate 5-phosphate	-	?

Subunits

EC Number	Subunits	Comment	Organism
2.7.2.8	hexamer	three homodimers are linked to form a ring-like hexamer	Thermotoga maritima
2.7.2.8	hexamer	three homodimers are linked to form a ring-like hexamer	Pseudomonas aeruginosa

Synonyms

EC Number	Synonyms	Comment	Organism
2.7.2.8	acetylglutamate kinase	-	Thermotoga maritima
2.7.2.8	acetylglutamate kinase	-	Pseudomonas aeruginosa
2.7.2.8	N-acetyl-L-glutamate 5-phosphotransferase	-	Thermotoga maritima
2.7.2.8	N-acetyl-L-glutamate 5-phosphotransferase	-	Pseudomonas aeruginosa
2.7.2.8	N-acetylglutamate kinase	-	Thermotoga maritima
2.7.2.8	N-acetylglutamate kinase	-	Pseudomonas aeruginosa
2.7.2.8	NagK	-	Thermotoga maritima
2.7.2.8	NagK	-	Pseudomonas aeruginosa
2.7.2.8	NAGS-K	-	Thermotoga maritima
2.7.2.8	NAGS-K	-	Pseudomonas aeruginosa

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Release 2023.1 (January 2023)