Literature summary for 2.7.2.8 extracted from

Gil-Ortiz, F.; Ramon-Maiques, S.; Fernandez-Murga, M.L.; Fita, I.; Rubio, V.
Two crystal structures of Escherichia coli N-acetyl-L-glutamate kinase demonstrate the cycling between open and closed conformations (2010), J. Mol. Biol., 399, 476-490.

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structures of EcNAGK free from substrates or complexed with the product N-acetyl-L-glutamyl-5-phosphate (NAGP) and with sulfate are determined at 2 A resolution. Structures reveal a novel, very open NAGK conformation to which substrates associate and from which roducts dissociate. In this conformation, the C-domain, which hosts most of the nucleotide site, rotates 24°-28° away from the N-domain, which hosts the acetylglutamate site, whereas the empty ATP site also exhibits some changes	Escherichia coli

Crystallization (Comment)

Organism

crystal structures of EcNAGK free from substrates or complexed with the product N-acetyl-L-glutamyl-5-phosphate (NAGP) and with sulfate are determined at 2 A resolution. Structures reveal a novel, very open NAGK conformation to which substrates associate and from which roducts dissociate. In this conformation, the C-domain, which hosts most of the nucleotide site, rotates 24°-28° away from the N-domain, which hosts the acetylglutamate site, whereas the empty ATP site also exhibits some changes

Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
G11A	G11A does not hamper recombinant enzyme expression or purification. Mutant shows a 10fold decrease in Vmax values and it selectively increases 8fold the Km for ATP, affecting much less (3fold increase) the apparent Km for N-acetyl-L-glutamate	Escherichia coli

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism
1.1	-	ATP	pH 7.5, 37°C, wild-type, Vmax: 72.6	Escherichia coli
1.3	-	N-acetyl-L-glutamate	pH 7.5, 37°C, wild-type, Vmax: 80	Escherichia coli
5.1	-	N-acetyl-L-glutamate	pH 7.5, 37°C, mutant G11A, Vmax: 9.7	Escherichia coli
13.4	-	ATP	pH 7.5, 37°C, mutant G11A, Vmax: 11.1	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	A0A140NEG9	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + N-acetyl-L-glutamate	-	Escherichia coli	ADP + N-acetyl-L-glutamate 5-phosphate	-	?

Subunits

Subunits	Comment	Organism
homodimer	-	Escherichia coli

Synonyms

Synonyms	Comment	Organism
EcNAGK	-	Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Escherichia coli

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.5	-	assay at	Escherichia coli