Literature summary for 2.7.2.8 extracted from

Qu, Q.; Morizono, H.; Shi, D.; Tuchman, M.; Caldovic, L.
A novel bifunctional N-acetylglutamate synthase-kinase from Xanthomonas campestris that is closely related to mammalian N-acetylglutamate synthase (2007), BMC Biochem., 8, 4.

Search for more literature for 2.7.2.8

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Xanthomonas campestris

Inhibitors

Inhibitors	Comment	Organism	Structure
L-arginine	only for N-acetylglutamate synthase activity	Xanthomonas campestris

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
1.3	-	AcCoA	only for N-acetylglutamate synthase activity	Xanthomonas campestris
2.8	-	L-glutamate	only for N-acetylglutamate synthase activity	Xanthomonas campestris

Organism

Organism	UniProt	Comment	Textmining
Xanthomonas campestris	Q8P8J6	-	-

Purification (Commentary)

Purification (Comment)	Organism
of the recombinant protein	Xanthomonas campestris

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
1.95	-	-	Xanthomonas campestris

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
acetyl-CoA + L-glutamate	-	Xanthomonas campestris	coenzyme A + N-acetyl-L-glutamate	ancestral bifunctional N-acetylglutamate synthase and kinase	?
ATP + N-acetyl-L-glutamate	-	Xanthomonas campestris	ADP + N-acetyl-L-glutamate 5-phosphate	-	?

Synonyms

Synonyms	Comment	Organism
acetylglutamate kinase	-	Xanthomonas campestris
N-acetylglutamate kinase	-	Xanthomonas campestris
NagK	-	Xanthomonas campestris
NAGS-K	-	Xanthomonas campestris

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
6	-	-	Xanthomonas campestris

pH Range

pH Minimum	pH Maximum	Comment	Organism
5	7.5	-	Xanthomonas campestris

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Release 2023.1 (January 2023)