Information on EC 2.7.2.8 -

Information on EC 2.7.2.8 - acetylglutamate kinase:

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EC NUMBER	COMMENTARY
2.7.2.8	-

RECOMMENDED NAME	GeneOntology No.
acetylglutamate kinase	GO:0003991

REACTION	REACTION DIAGRAM	COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate		enzyme has to interact stoichiometrically with acetylglutamate synthase in order to be active	Saccharomyces cerevisiae	-	390290, 486081
ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate		-	-	-	-
ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate		random bi-bi mechanism	Pisum sativum	-	642358
ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate		mechanism	Escherichia coli	-	642359
ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate		-	Xanthomonas campestris	Q8P8J7	671144, 672794
ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate		-	Arabidopsis thaliana	-	673641, 674751, 674874
ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate		-	Pseudomonas aeruginosa	-	675366
ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate		-	Thermotoga maritima	Q9X2A4	675366

REACTION TYPE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
Acyl group transfer	Xanthomonas campestris	Q8P8J7	-	671144, 672794
phospho group transfer	-	-	-	-
phospho group transfer	Xanthomonas campestris	Q8P8J7	-	671144, 672794
phospho group transfer	Arabidopsis thaliana	-	-	673641, 674751, 674874
phospho group transfer	Pseudomonas aeruginosa	-	-	675366
phospho group transfer	Thermotoga maritima	Q9X2A4	-	675366

PATHWAY	KEGG Link	MetaCyc Link
arginine biosynthesis II (acetyl cycle)	-	ARGSYNBSUB-PWY
arginine biosynthesis III	-	PWY-5154
ornithine biosynthesis	-	GLUTORN-PWY

SYSTEMATIC NAME	IUBMB Comments
ATP:N-acetyl-L-glutamate 5-phosphotransferase	-

SYNONYMS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
acetylglutamate kinase	Xanthomonas campestris	Q8P8J7	-	671144, 672794
acetylglutamate kinase	Arabidopsis thaliana	-	-	673641, 674751, 674874
acetylglutamate kinase	Pseudomonas aeruginosa	-	-	675366
acetylglutamate kinase	Thermotoga maritima	Q9X2A4	-	675366
acetylglutamate phosphokinase	-	-	-	-
amino-acid acetyltransferase	Xanthomonas campestris	-	-	671144
kinase, acetylglutamate (phosphorylating)	-	-	-	-
N-acetyl-L-glutamate 5-phosphotransferase	Pseudomonas aeruginosa	-	-	675366
N-acetyl-L-glutamate 5-phosphotransferase	Thermotoga maritima	Q9X2A4	-	675366
N-acetyl-L-glutamate kinase	Arabidopsis thaliana	-	-	702066, 704614, 705148
N-acetyl-L-glutamate kinase	Pseudomonas aeruginosa	-	-	704614
N-acetyl-L-glutamate kinase	Synechococcus elongatus	-	-	705148
N-acetylglutamate 5-phosphotransferase	-	-	-	-
N-acetylglutamate kinase	-	-	-	-
N-acetylglutamate kinase	Xanthomonas campestris	Q8P8J7	-	671144, 672794
N-acetylglutamate kinase	Arabidopsis thaliana	-	-	673641, 674751, 674874
N-acetylglutamate kinase	Pseudomonas aeruginosa	-	-	675366, 692856
N-acetylglutamate kinase	Thermotoga maritima	Q9X2A4	-	675366
N-acetylglutamate kinase	Streptococcus mutans	-	-	689895
N-acetylglutamate phosphokinase	-	-	-	-
N-acetylglutamate-5-phosphotransferase	-	-	-	-
N-acetylglutamic 5-phosphotransferase	-	-	-	-
NagK	Pseudomonas aeruginosa	-	-	659050, 675366, 692856, 704614
NagK	Thermotoga maritima	-	-	659050, 675366
NagK	Xanthomonas campestris	Q8P8J7	-	671144, 672794
NagK	Arabidopsis thaliana	-	-	673641, 674751, 702066, 704614, 705148
NagK	Arabidopsis thaliana	-	;	674874
NagK	Synechococcus elongatus	-	-	689765, 705148
NagK	Streptococcus mutans	-	-	689895
NAGK1	Oryza sativa	-	-	660146
NAGS-K	Xanthomonas campestris	Q8P8J7	-	671144, 672794
NAGS-K	Arabidopsis thaliana	-	-	673641, 674751
NAGS-K	Pseudomonas aeruginosa	-	-	675366
NAGS-K	Thermotoga maritima	Q9X2A4	-	675366

CAS REGISTRY NUMBER	COMMENTARY
9027-58-1	-

ORGANISM	COMMENTARY	LITERATURE	SEQUENCE CODE	SEQUENCE DB	SOURCE
Arabidopsis thaliana	-	673641, 674874	Q8LA25	SwissProt
Arabidopsis thaliana	-	674751, 705148	Q9SCL7	UniProt
Arabidopsis thaliana	-	674874, 702066, 704614	-	-
Chlamydomonas reinhardtii	-	642353, 642354	-	-
Escherichia coli	-	642359, 659704	P0A6C8	Uniprot
Escherichia coli	-	642363	-	-
Escherichia coli	ATCC 25542	642354	-	-
Escherichia coli	strain W2D, ATCC 25542, derepressed mutant	642351	-	-
Escherichia coli	strain Wc2	390278	-	-
Escherichia coli W2D	strain W2D, ATCC 25542, derepressed mutant	642351	-	-
Neurospora crassa	-	642357	-	-
Oryza sativa	-	660146	-	-
Pisum sativum	-	642358	-	-
Pseudomonas aeruginosa	-	642355, 642356, 642361, 692856	-	-
Pseudomonas aeruginosa	-	675366, 704614	Q9HTN2	SwissProt
Pseudomonas aeruginosa	recombinant enzyme	659050	-	-
Saccharomyces cerevisiae	-	390290, 486081	-	-
Streptococcus mutans	-	689895	-	-
Synechococcus elongatus	-	689765	Q6V1L5	UniProt
Synechococcus elongatus	-	705148	-	-
Synechococcus elongatus	strain PCC 7942, recombinant protein with His6-tag	659433	-	-
Thermotoga maritima	-	675366	Q9X2A4	UniProt
Thermotoga maritima	recombinant enzyme	659050	-	-
Xanthomonas campestris	-	671144, 672794	Q8P8J7	UniProt

GENERAL INFORMATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

SUBSTRATE	PRODUCT	REACTION DIAGRAM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY/ Substrate	LITERATURE/ Substrate	COMMENTARY/ Product	LITERATURE/ Product	Reversibility r=reversible ir=irreversible ?=not specified
acetyl-CoA + L-glutamate	coenzyme A + N-acetyl-L-glutamate		Xanthomonas campestris	Q8P8J7	-	671144	ancestral bifunctional N-acetylglutamate synthase and kinase	-	?
acetyl-CoA + L-glutamate	coenzyme A + N-acetyl-L-glutamate		Xanthomonas campestris	-	-	672794	ancestral bifunctional N-acetylglutamate synthase and kinase	-	?
ATP + N-acetyl-L-glutamate	ADP + N-acetyl-L-glutamate 5-phosphate		Escherichia coli	-	-	642351	-	642351	-
ATP + N-acetyl-L-glutamate	ADP + N-acetyl-L-glutamate 5-phosphate		Escherichia coli	-	-	659704	-	-	-
ATP + N-acetyl-L-glutamate	ADP + N-acetyl-L-glutamate 5-phosphate		Escherichia coli	-	-	390278	-	-	?
ATP + N-acetyl-L-glutamate	ADP + N-acetyl-L-glutamate 5-phosphate		Escherichia coli	-	-	642351	-	642351	?
ATP + N-acetyl-L-glutamate	ADP + N-acetyl-L-glutamate 5-phosphate		Saccharomyces cerevisiae	-	-	390290	-	-	?
ATP + N-acetyl-L-glutamate	ADP + N-acetyl-L-glutamate 5-phosphate		Arabidopsis thaliana	-	-	702066, 704614, 705148	-	-	?
ATP + N-acetyl-L-glutamate	ADP + N-acetyl-L-glutamate 5-phosphate		Pseudomonas aeruginosa	-	-	659050	-	-	-
ATP + N-acetyl-L-glutamate	ADP + N-acetyl-L-glutamate 5-phosphate		Pseudomonas aeruginosa	-	-	642355, 704614	-	-	?
ATP + N-acetyl-L-glutamate	ADP + N-acetyl-L-glutamate 5-phosphate		Thermotoga maritima	-	-	659050	-	-	-
ATP + N-acetyl-L-glutamate	ADP + N-acetyl-L-glutamate 5-phosphate		Synechococcus elongatus	-	-	659433	-	-	-
ATP + N-acetyl-L-glutamate	ADP + N-acetyl-L-glutamate 5-phosphate		Synechococcus elongatus	-	-	705148	-	-	?
ATP + N-acetyl-L-glutamate	ADP + N-acetyl-L-glutamate 5-phosphate		Arabidopsis thaliana	-	-	674874	-	-	-
ATP + N-acetyl-L-glutamate	ADP + N-acetyl-L-glutamate 5-phosphate		Xanthomonas campestris	Q8P8J7	-	671144	-	-	?
ATP + N-acetyl-L-glutamate	ADP + N-acetyl-L-glutamate 5-phosphate		Xanthomonas campestris	-	-	672794	-	-	?
ATP + N-acetyl-L-glutamate	ADP + N-acetyl-L-glutamate 5-phosphate		Arabidopsis thaliana	Q9SCL7	-	674751	-	-	?
ATP + N-acetyl-L-glutamate	ADP + N-acetyl-L-glutamate 5-phosphate		Thermotoga maritima	Q9X2A4	-	675366	-	-	?
ATP + N-acetyl-L-glutamate	ADP + N-acetyl-L-glutamate 5-phosphate		Pseudomonas aeruginosa	Q9HTN2	-	675366	-	-	?
ATP + N-acetyl-L-glutamate	ADP + N-acetyl-L-glutamate 5-phosphate		Chlamydomonas reinhardtii	-	-	642353	in presence of hydroxylamine formation of N-acetyl-L-glutamate 5-hydroxamate + ADP + phosphate	642353	?
ATP + N-acetyl-L-glutamate	ADP + N-acetyl-L-glutamate 5-phosphate		Pseudomonas aeruginosa	-	-	642356	in presence of hydroxylamine formation of N-acetyl-L-glutamate 5-hydroxamate + ADP + phosphate	642356	?
ATP + N-acetyl-L-glutamate	ADP + N-acetyl-L-glutamate 5-phosphate		Chlamydomonas reinhardtii, Escherichia coli	-	highly specific for ATP and N-acetyl-L-glutamate	642354	in presence of hydroxylamine formation of N-acetyl-L-glutamate 5-hydroxamate + ADP + phosphate	642354	?
ATP + N-acetyl-L-glutamate	ADP + N-acetyl-L-glutamate 5-phosphate		Chlamydomonas reinhardtii	-	key enzyme in regulation of arginine biosynthesis	642353	-	642353	-
ATP + N-acetyl-L-glutamate	ADP + N-acetyl-L-glutamate 5-phosphate		Chlamydomonas reinhardtii, Escherichia coli	-	key enzyme in regulation of arginine biosynthesis	642354	-	642354	-
ATP + N-acetyl-L-glutamate	ADP + N-acetyl-L-glutamate 5-phosphate		Pseudomonas aeruginosa	-	enzyme synthesis not repressed by exogenous L-arginine or its precursors, second enzyme of arginine biosynthesis	642355	-	-	-
ATP + N-acetyl-L-glutamate	ADP + N-acetyl-L-glutamyl 5-phosphate		Pseudomonas aeruginosa	-	NAGK catalyzes the second step of arginine biosynthesis. In Pseudomonas aeruginosa, this step is rate limiting, and feedback regulated and sigmoidally inhibited by arginine	692856	-	-	?
ATP + N-acetyl-L-glutamate (1)	ADP + N-acetyl-L-glutamate 5-phosphate		Arabidopsis thaliana	Q8LA25	-	673641	-	-	-
ATP + N-carbamoyl-L-glutamate	ADP + N-carbamoyl-L-glutamate 5-phosphate		Pseudomonas aeruginosa	-	at 33% of the activity with N-acetyl-L-glutamate	642356	-	-	-
ATP + N-formyl-L-glutamate	ADP + N-formyl-L-glutamate 5-phosphate		Pseudomonas aeruginosa	-	at 20% of the activity with N-acetyl-L-glutamate	642356	-	-	-
dATP + N-acetyl-L-glutamate	dADP + N-acetyl-L-glutamate 5-phosphate		Pseudomonas aeruginosa	-	as effective as ATP	642356	-	-	-
additional information	?	-	Pseudomonas aeruginosa	-	not: ITP	642356	-	-	-
additional information	?	-	Chlamydomonas reinhardtii	-	not: GTP	642354	-	-	-
additional information	?	-	Escherichia coli	-	not: GTP	642351, 642354	-	-	-
additional information	?	-	Pseudomonas aeruginosa	-	not: GTP	642356	-	-	-
additional information	?	-	Chlamydomonas reinhardtii	-	not: N-benzoyl-L-glutamate, L-glutamate, D-glutamate	642354	-	-	-
additional information	?	-	Escherichia coli	-	not: N-benzoyl-L-glutamate, L-glutamate, D-glutamate	642351, 642354	-	-	-
additional information	?	-	Pseudomonas aeruginosa	-	N-propionyl-L-glutamate almost inactive	642356	-	-	-
additional information	?	-	Arabidopsis thaliana	-	NAGK strongly interacts with PII protein only in the presence of Mg-ATP, this process is reversed by 2-oxoglutarate	702066	-	-	-

NATURAL SUBSTRATES	NATURAL PRODUCTS	REACTION DIAGRAM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY SUBSTRATE	LITERATURE (Substrate)	COMMENTARY PRODUCT	LITERATURE (Product)
ATP + N-acetyl-L-glutamate	ADP + N-acetyl-L-glutamate 5-phosphate		Escherichia coli	-	-	642351	-	642351
ATP + N-acetyl-L-glutamate	ADP + N-acetyl-L-glutamate 5-phosphate		Arabidopsis thaliana	-	-	704614, 705148	-	-
ATP + N-acetyl-L-glutamate	ADP + N-acetyl-L-glutamate 5-phosphate		Pseudomonas aeruginosa	-	-	704614	-	-
ATP + N-acetyl-L-glutamate	ADP + N-acetyl-L-glutamate 5-phosphate		Synechococcus elongatus	-	-	705148	-	-
ATP + N-acetyl-L-glutamate	ADP + N-acetyl-L-glutamate 5-phosphate		Chlamydomonas reinhardtii	-	key enzyme in regulation of arginine biosynthesis	642353	-	642353
ATP + N-acetyl-L-glutamate	ADP + N-acetyl-L-glutamate 5-phosphate		Chlamydomonas reinhardtii, Escherichia coli	-	key enzyme in regulation of arginine biosynthesis	642354	-	642354
ATP + N-acetyl-L-glutamate	ADP + N-acetyl-L-glutamate 5-phosphate		Pseudomonas aeruginosa	-	enzyme synthesis not repressed by exogenous L-arginine or its precursors, second enzyme of arginine biosynthesis	642355	-	-
ATP + N-acetyl-L-glutamate	ADP + N-acetyl-L-glutamyl 5-phosphate		Pseudomonas aeruginosa	-	NAGK catalyzes the second step of arginine biosynthesis. In Pseudomonas aeruginosa, this step is rate limiting, and feedback regulated and sigmoidally inhibited by arginine	692856	-	-
additional information	?	-	Arabidopsis thaliana	-	NAGK strongly interacts with PII protein only in the presence of Mg-ATP, this process is reversed by 2-oxoglutarate	702066	-	-

COFACTOR	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
ATP	Pseudomonas aeruginosa	-	-	692856, 704614	2D-image
ATP	Arabidopsis thaliana	-	-	702066, 704614, 705148	2D-image
ATP	Synechococcus elongatus	-	-	705148	2D-image

METALS and IONS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
Ca2+	Pseudomonas aeruginosa	-	Mn2+, Zn2+, Co2+ and Ca2+ in this order can partially replace Mg2+	642356
Co2+	Chlamydomonas reinhardtii	-	Mg2+ or Co2+ required	642353, 642354
Co2+	Pseudomonas aeruginosa	-	Mn2+, Zn2+, Co2+ and Ca2+ in this order can partially replace Mg2+	642356
Mg2+	Escherichia coli	-	employed in assay mixture	390278, 642351
Mg2+	Chlamydomonas reinhardtii	-	Mg2+ or Co2+ required	642353
Mg2+	Chlamydomonas reinhardtii	-	Mg2+ or Co2+ required; required	642354
Mg2+	Escherichia coli	-	-	642354
Mg2+	Pseudomonas aeruginosa	-	required	642355
Mg2+	Pseudomonas aeruginosa	-	30 mM, slight inhibition; required	642356
Mg2+	Synechococcus elongatus	-	required, maximum activity above 20 mM	659433
Mg2+	Arabidopsis thaliana	-	-	673641
Mg2+	Pseudomonas aeruginosa	-	-	692856
Mg2+	Arabidopsis thaliana	-	required	702066
Mn2+	Chlamydomonas reinhardtii	-	less effective than Mg2+ and Co2+ in activation	642353
Mn2+	Pseudomonas aeruginosa	-	Mn2+, Zn2+, Co2+ and Ca2+ in decreasing order can partially replace Mg2+	642356
Zn2+	Pseudomonas aeruginosa	-	Mn2+, Zn2+, Co2+ and Ca2+ in this order can partially replace Mg2+	642356

INHIBITORS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
2-oxoglutarate	Arabidopsis thaliana	-	complete inhibition at 0.5 mM	705148	2D-image
ADP	Pseudomonas aeruginosa	-	-	642356	2D-image
ADP	Synechococcus elongatus	-	inhibitor of complex formation with PII protein	659433	2D-image
arginine	Saccharomyces cerevisiae	-	feedback regulation of enzyme and N-acetylglutamate synthase is mutually interdependent, enzymes form a complex	486081	2D-image
arginine	Chlamydomonas reinhardtii	-	pH-optimum for inhibition is 7.5	642353	2D-image
arginine	Chlamydomonas reinhardtii	-	allosteric enzyme which is inhibited by arginine	642354	2D-image
arginine	Escherichia coli	-	enzyme has no allosteric properties and its activity is influenced neither by arginine nor by any of the intermediates of the arginine biosynthetic pathway	642354	2D-image
arginine	Pseudomonas aeruginosa	-	feedback inhibition is markedly dependent on pH, above pH 9 no inhibition	642356	2D-image
arginine	Neurospora crassa	-	feedback inhibition is markedly dependent on pH, above pH 9 no inhibition	642357	2D-image
arginine	Pseudomonas aeruginosa	-	1 mM, 96% inhibition	642361	2D-image
arginine	Synechococcus elongatus	-	feedback inhibition	659433	2D-image
arginine	Pseudomonas aeruginosa	-	-	675366	2D-image
arginine	Thermotoga maritima	Q9X2A4	-	675366	2D-image
ATP	Escherichia coli	-	-	659704	2D-image
L-arginine	Thermotoga maritima	-	pH and temperature dependent, sigmoidal dependence on concentration of arginine, Hill coefficient of 4, 1 mM, 37�C, 95% inhibition	659050	2D-image
L-arginine	Xanthomonas campestris	-	only for N-acetylglutamate synthase activity	672794	2D-image
L-arginine	Arabidopsis thaliana	-	less inhibitory in the presence of the PII protein	674751	2D-image
L-arginine	Pseudomonas aeruginosa	-	sigmoidal arginine inhibition kinetics, feedback inhibition, indentification of the N-terminal arginine site, mutational analysis, the mobile alphaH-beta16 loop of the arginine site is the modulatory signal receiver, overview	692856	2D-image
L-arginine	Arabidopsis thaliana, Pseudomonas aeruginosa	-	-	704614	2D-image
L-arginine	Arabidopsis thaliana	-	complete inhibition at 3-5 mM, PII-mediated relief from L-arginine inhibition is antagonized by 2-oxoglutarate	705148	2D-image
L-arginine	Synechococcus elongatus	-	complete inhibition at 0.1-1.0 mM, PII-mediated relief from L-arginine inhibition is antagonized by 2-oxoglutarate	705148	2D-image
L-arginine methyl ester	Thermotoga maritima	-	1 mM, 80% inhibition	659050	2D-image
L-canavanine	Chlamydomonas reinhardtii	-	-	642353	2D-image
L-citrulline	Chlamydomonas reinhardtii	-	-	642353	2D-image
L-citrulline	Pseudomonas aeruginosa	-	-	642356	2D-image
MgCl2	Chlamydomonas reinhardtii	-	inhibition above 20 mM	642354	2D-image
MgCl2	Pseudomonas aeruginosa	-	30 mM, slight inhibition	642356	2D-image
additional information	Thermotoga maritima	-	not inhibitory: D-arginine, agmatine, citrulline, L-canavanine, L-lysine, L-ornithine, guanidinium ions, urea at 1 mM, 37�C	659050	-

ACTIVATING COMPOUND	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
2-Ketoglutarate	Arabidopsis thaliana	-	only if bound to the PII protein ATP complex	674751	2D-image
PII protein	Arabidopsis thaliana	-	-	673641, 705148	-
PII protein	Arabidopsis thaliana	-	prevents inhibition by arginine	674751	-
PII protein	Synechococcus elongatus	-	-	705148	-
ATP	Synechococcus elongatus	-	maximum activity at 10 mM	659433	2D-image
additional information	Arabidopsis thaliana	-	2-ketoglutarate shows no additive effect to the activation of PII protein	673641	-

KM VALUE [mM]	KM VALUE [mM] Maximum	SUBSTRATE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
1.3	-	AcCoA	Xanthomonas campestris	-	only for N-acetylglutamate synthase activity	672794	2D-image
0.29	-	ATP	Escherichia coli	-	wild-type, pH 7.0, 25�C	659704	2D-image
0.3	-	ATP	Arabidopsis thaliana	-	in the absence of protein PII, in 50 mM imidazole, pH 7.5	705148	2D-image
0.4	-	ATP	Arabidopsis thaliana	-	in the absence of protein PII, in 50 mM imidazole, pH 7.5	705148	2D-image
0.46	-	ATP	Escherichia coli	-	mutant D162E, pH 7.0, 25�C	659704	2D-image
0.6	-	ATP	Synechococcus elongatus	-	in the absence of protein PII, in 50 mM imidazole, pH 7.5	705148	2D-image
1	-	ATP	Escherichia coli	-	-	642354	2D-image
1.1	-	ATP	Synechococcus elongatus	-	in the absence of protein PII, in 50 mM imidazole, pH 7.5	705148	2D-image
1.6	-	ATP	Chlamydomonas reinhardtii	-	pH 5.5, 37�C	642353	2D-image
1.7	-	ATP	Pisum sativum	-	pH 7.5, 30�C	642358	2D-image
1.74	-	ATP	Arabidopsis thaliana	-	without PII protein	674751	2D-image
2.03	-	ATP	Arabidopsis thaliana	-	in complex with PII protein	674751	2D-image
2.47	-	ATP	Arabidopsis thaliana	-	in complex with PII protein and 2-ketoglutarate	674751	2D-image
3	-	ATP	Chlamydomonas reinhardtii	-	pH 8.0, 37�C, allosteric	642354	2D-image
3	-	ATP	Pseudomonas aeruginosa	-	pH 7.2, 37�C	642356	2D-image
3.1	-	ATP	Pseudomonas aeruginosa	-	wild-type enzyme	692856	2D-image
3.3	-	ATP	Escherichia coli	-	mutant K8R, pH 7.0, 25�C	659704	2D-image
5.2	-	ATP	Escherichia coli	-	mutant R66K, pH 7.0, 25�C	659704	2D-image
7.9	-	ATP	Escherichia coli	-	mutant N158Q, pH 7.0, 25�C	659704	2D-image
0.2	-	N-acetyl-L-glutamate	Escherichia coli	-	wild-type, pH 7.0, 25�C	659704	2D-image
0.37	-	N-acetyl-L-glutamate	Escherichia coli	-	mutant D162E, pH 7.0, 25�C	659704	2D-image
0.85	-	N-acetyl-L-glutamate	Arabidopsis thaliana	-	in the absence of protein PII, in 50 mM imidazole, pH 7.5	705148	2D-image
0.87	-	N-acetyl-L-glutamate	Arabidopsis thaliana	-	in the absence of protein PII, in 50 mM imidazole, pH 7.5	705148	2D-image
1.9	-	N-acetyl-L-glutamate	Pisum sativum	-	two Km-values: 1.9 and 6.2, pH 7.5, 30�C	642358	2D-image
2	-	N-acetyl-L-glutamate	Pseudomonas aeruginosa	-	pH 7.2, 37�C	642356	2D-image
2.3	-	N-acetyl-L-glutamate	Escherichia coli	-	mutant K8R, pH 7.0, 25�C	659704	2D-image
2.7	-	N-acetyl-L-glutamate	Synechococcus elongatus	-	pH 7.5, complex of enzyme and PII protein	659433	2D-image
3.1	-	N-acetyl-L-glutamate	Pseudomonas aeruginosa	-	wild-type enzyme	692856	2D-image
3.1	-	N-acetyl-L-glutamate	Synechococcus elongatus	-	in the absence of protein PII, in 50 mM imidazole, pH 7.5	705148	2D-image
4	-	N-acetyl-L-glutamate	Chlamydomonas reinhardtii	-	pH 8.0, 37�C, allosteric	642354	2D-image
6	-	N-acetyl-L-glutamate	Escherichia coli	-	pH 5.5, 37�C	642354	2D-image
6.2	-	N-acetyl-L-glutamate	Pisum sativum	-	2 Km-values: 1.9 and 6.2, pH 7.5, 30�C	642358	2D-image
7.08	-	N-acetyl-L-glutamate	Arabidopsis thaliana	-	without PII protein	674751	2D-image
7.4	-	N-acetyl-L-glutamate	Synechococcus elongatus	-	in the absence of protein PII, in 50 mM imidazole, pH 7.5	705148	2D-image
7.55	-	N-acetyl-L-glutamate	Arabidopsis thaliana	-	in complex with PII protein	674751	2D-image
9.45	-	N-acetyl-L-glutamate	Arabidopsis thaliana	-	in complex with PII protein and 2-ketoglutarate	674751	2D-image
15	-	N-acetyl-L-glutamate	Chlamydomonas reinhardtii	-	pH 5.5, 37�C	642353	2D-image
15	-	N-acetyl-L-glutamate	Chlamydomonas reinhardtii	-	-	642354	2D-image
27.4	-	N-acetyl-L-glutamate	Synechococcus elongatus	-	pH 7.5, free enzyme	659433	2D-image
85	-	N-acetyl-L-glutamate	Arabidopsis thaliana	-	in the presence of 1 mM L-arginine, in 50 mM imidazole, pH 7.5	705148	2D-image
600	-	N-acetyl-L-glutamate	Escherichia coli	-	mutant N158Q, pH 7.0, 25�C	659704	2D-image
898	-	N-acetyl-L-glutamate	Escherichia coli	-	mutant R66K, pH 7.0, 25�C	659704	2D-image
2.8	-	L-glutamate	Xanthomonas campestris	-	only for N-acetylglutamate synthase activity	672794	2D-image
additional information	-	additional information	Synechococcus elongatus	-	formation of complex between enzyme and signal transduction protein PII decreases Km-value by a factor of 10 and increases Vmax 4fold	659433	-
additional information	-	additional information	Pseudomonas aeruginosa	-	kinetics of enzyme mutants, overview	692856	-

TURNOVER NUMBER [1/s]	TURNOVER NUMBER MAXIMUM[1/s]	SUBSTRATE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
13.1	-	N-acetyl-L-glutamate	Synechococcus elongatus	-	in the absence of protein PII, in 50 mM imidazole, pH 7.5	705148	2D-image
40.4	-	N-acetyl-L-glutamate	Synechococcus elongatus	-	in the presence of protein PII, in 50 mM imidazole, pH 7.5	705148	2D-image
115	-	N-acetyl-L-glutamate	Arabidopsis thaliana	-	in the presence of 1 mM L-arginine, in 50 mM imidazole, pH 7.5	705148	2D-image
126.1	-	N-acetyl-L-glutamate	Arabidopsis thaliana	-	in the absence of protein PII, in 50 mM imidazole, pH 7.5	705148	2D-image
187.5	-	N-acetyl-L-glutamate	Arabidopsis thaliana	-	in the presence of protein PII, in 50 mM imidazole, pH 7.5	705148	2D-image

kcat/KM VALUE [1/mMs^-1]	kcat/KM VALUE [1/mMs^-1] Maximum	SUBSTRATE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
1.3	-	N-acetyl-L-glutamate	Arabidopsis thaliana	-	in the presence of 1 mM L-arginine, in 50 mM imidazole, pH 7.5	705148	13560
1.7	-	N-acetyl-L-glutamate	Synechococcus elongatus	-	in the absence of protein PII, in 50 mM imidazole, pH 7.5	705148	13560
13	-	N-acetyl-L-glutamate	Synechococcus elongatus	-	in the presence of protein PII, in 50 mM imidazole, pH 7.5	705148	13560
145	-	N-acetyl-L-glutamate	Arabidopsis thaliana	-	in the absence of protein PII, in 50 mM imidazole, pH 7.5	705148	13560
220	-	N-acetyl-L-glutamate	Arabidopsis thaliana	-	in the presence of protein PII, in 50 mM imidazole, pH 7.5	705148	13560

Ki VALUE [mM]	Ki VALUE [mM] Maximum	INHIBITOR	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
30.4	-	ATP	Escherichia coli	-	wild-type, pH 7.0, 25�C	659704	2D-image
41.5	-	ATP	Escherichia coli	-	mutant N158Q, pH 7.0, 25�C	659704	2D-image

IC50 VALUE [mM]	IC50 VALUE [mM] Maximum	INHIBITOR	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
0.02	-	L-arginine	Synechococcus elongatus	-	in the absence of protein PII, in 50 mM imidazole, pH 7.5	705148	2D-image
0.19	-	L-arginine	Synechococcus elongatus	-	in the presence of protein PII, in 50 mM imidazole, pH 7.5	705148	2D-image
1	-	L-arginine	Arabidopsis thaliana	-	in the absence of protein PII, in 50 mM imidazole, pH 7.5	705148	2D-image
5.9	-	L-arginine	Arabidopsis thaliana	-	in the presence of protein PII, in 50 mM imidazole, pH 7.5	705148	2D-image

SPECIFIC ACTIVITY [µmol/min/mg]	SPECIFIC ACTIVITY MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
0.54	-	Escherichia coli	-	pH 7.4, 37�C	642351
1.95	-	Xanthomonas campestris	-	-	672794
3.3	-	Synechococcus elongatus	-	pH 7.5, free enzyme	659433
7.21	-	Neurospora crassa	-	-	642357
12	-	Arabidopsis thaliana	-	without PII protein	673641
13.3	-	Synechococcus elongatus	-	pH 7.5, complex of enzyme and PII protein	659433
24	-	Arabidopsis thaliana	-	with PII protein	673641
45	-	Thermotoga maritima	-	37�C, pH 7.5	659050
130	-	Pseudomonas aeruginosa	-	37�C, pH 7.5	659050
677	-	Thermotoga maritima	-	80�C, pH 7.5	659050
additional information	-	Escherichia coli	-	-	642351
additional information	-	Pseudomonas aeruginosa	-	-	642355

pH OPTIMUM	pH MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
5.5	-	Chlamydomonas reinhardtii	-	-	642353, 642354
6	-	Xanthomonas campestris	-	-	672794
6.5	9	Pseudomonas aeruginosa	-	-	642356
6.8	7.8	Escherichia coli	-	-	642351, 642354
7	-	Pseudomonas aeruginosa	-	assay at	642355
7.4	-	Escherichia coli	-	assay at	390278, 642351
7.5	-	Synechococcus elongatus	-	both free enzyme and complex with protein PII	659433
7.5	-	Pseudomonas aeruginosa	-	assay at	692856

pH RANGE	pH RANGE MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
4.6	7	Chlamydomonas reinhardtii	-	pH 4.6: about 75% of maximum activity, pH 7: about 60% of maximum activity	642353
5	7.5	Xanthomonas campestris	-	-	672794
5.5	8.5	Chlamydomonas reinhardtii	-	-	642354

TEMPERATURE OPTIMUM	TEMPERATURE OPTIMUM MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
25	-	Pseudomonas aeruginosa	-	assay at	642355
30	-	Neurospora crassa	-	assay at	642357
37	-	Escherichia coli	-	assay at	390278, 642351
37	-	Chlamydomonas reinhardtii	-	assay at	642353
37	-	Pseudomonas aeruginosa	-	assay at	692856
80	-	Thermotoga maritima	-	-	659050

TEMPERATURE RANGE	TEMPERATURE MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

pI VALUE	pI VALUE MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

SOURCE TISSUE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	SOURCE
cotyledon	Pisum sativum	-	-	642358
leaf	Oryza sativa	-	sheath and blade, coordinate expression of enzyme and PII-like protein GlnB during the life span	660146
root	Oryza sativa	-	-	660146
spikelet	Oryza sativa	-	-	660146

LOCALIZATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	GeneOntology No.	LITERATURE	SOURCE
chloroplast	Oryza sativa	-	-	9507	660146
chloroplast	Arabidopsis thaliana	-	-	9507	673641, 674751, 702066
mitochondrion	Neurospora crassa	-	-	5739	642357

PDB	SCOP	CATH	ORGANISM
2rd5, download	SCOP (2rd5)	CATH (2rd5)	Arabidopsis thaliana
1gs5, download	SCOP (1gs5)	CATH (1gs5)	Escherichia coli (strain K12)
1gsj, download	SCOP (1gsj)	CATH (1gsj)	Escherichia coli (strain K12)
1oh9, download	SCOP (1oh9)	CATH (1oh9)	Escherichia coli (strain K12)
1oha, download	SCOP (1oha)	CATH (1oha)	Escherichia coli (strain K12)
1ohb, download	SCOP (1ohb)	CATH (1ohb)	Escherichia coli (strain K12)
2wxb, download	SCOP (2wxb)	CATH (2wxb)	Escherichia coli (strain K12)
2x2w, download	SCOP (2x2w)	CATH (2x2w)	Escherichia coli (strain K12)
1gs5, download	SCOP (1gs5)	CATH (1gs5)	Escherichia coli O157:H7
1gsj, download	SCOP (1gsj)	CATH (1gsj)	Escherichia coli O157:H7
1oh9, download	SCOP (1oh9)	CATH (1oh9)	Escherichia coli O157:H7
1oha, download	SCOP (1oha)	CATH (1oha)	Escherichia coli O157:H7
1ohb, download	SCOP (1ohb)	CATH (1ohb)	Escherichia coli O157:H7
3s6g, download	SCOP (3s6g)	CATH (3s6g)	Maricaulis maris (strain MCS10)
3s6h, download	SCOP (3s6h)	CATH (3s6h)	Maricaulis maris (strain MCS10)
3s7y, download	SCOP (3s7y)	CATH (3s7y)	Maricaulis maris (strain MCS10)
2ap9, download	SCOP (2ap9)	CATH (2ap9)	Mycobacterium tuberculosis
2buf, download	SCOP (2buf)	CATH (2buf)	Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
3zzf, download	SCOP (3zzf)	CATH (3zzf)	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
3zzg, download	SCOP (3zzg)	CATH (3zzg)	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
3zzh, download	SCOP (3zzh)	CATH (3zzh)	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
3zzi, download	SCOP (3zzi)	CATH (3zzi)	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
4ab7, download	SCOP (4ab7)	CATH (4ab7)	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
3l86, download	SCOP (3l86)	CATH (3l86)	Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
2jj4, download	SCOP (2jj4)	CATH (2jj4)	Synechococcus elongatus (strain PCC 7942)
2v5h, download	SCOP (2v5h)	CATH (2v5h)	Synechococcus elongatus (strain PCC 7942)
2bty, download	SCOP (2bty)	CATH (2bty)	Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
3s6k, download	SCOP (3s6k)	CATH (3s6k)	Xanthomonas campestris pv. campestris (strain 8004)
3t7b, download	SCOP (3t7b)	CATH (3t7b)	Yersinia pestis

MOLECULAR WEIGHT	MOLECULAR WEIGHT MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
30000	-	Arabidopsis thaliana	-	recombinant protein, SDS-PAGE	673641
33000	-	Arabidopsis thaliana	-	mass spectrometry	674751
93000	-	Pisum sativum	-	gel filtration	642358
180000	-	Pseudomonas aeruginosa, Thermotoga maritima	-	gel filtration	659050
180000	-	Synechococcus elongatus	-	sedimentation anaylsis	659433
190000	-	Pisum sativum	-	gel filtration in presence of N-acetylglutamate	642358
198000	-	Arabidopsis thaliana	-	calculated from amino acid sequence	702066
230000	-	Pseudomonas aeruginosa	-	gel filtration	642355
400000	-	Chlamydomonas reinhardtii	-	gel filtration	642354

SUBUNITS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
?	Saccharomyces cerevisiae	-	x * 52000, SDS-PAGE	390290
?	Pseudomonas aeruginosa	-	x * 29000, SDS-PAGE	642355
?	Pisum sativum	-	dimer or tetramer, 1 or 2 * 43000 + 1 or 2 * 53000, SDS-PAGE	642358
dimer	Pseudomonas aeruginosa	-	2 * 30000, SDS-PAGE	642361
dimer	Escherichia coli	-	crystalline structure	642363
hexamer	Thermotoga maritima	-	6 * 30341, MALDI-TOF MS, 6 * 30344, calculated	659050
hexamer	Synechococcus elongatus	-	6 * 32000, calculated	659433
hexamer	Pseudomonas aeruginosa	-	three homodimers are linked to form a ring-like hexamer	675366
hexamer	Thermotoga maritima	Q9X2A4	three homodimers are linked to form a ring-like hexamer	675366
hexamer	Pseudomonas aeruginosa	-	with an extra N-terminal-linked helix interlinking three dimers, the hexameric architecture is not essential for arginine inhibition but is functionally essential for physiologically relevant arginine control of NAGK	692856
hexamer	Arabidopsis thaliana	-	-	702066
monomer	Streptococcus mutans	-	-	689895
additional information	Pseudomonas aeruginosa	-	due to the capacity for self-association the enzyme can exist in different states of aggregation depending on the nature of the ligands and the concentration of phosphate buffer	642355
additional information	Synechococcus elongatus	-	enzyme hexamer forms a complex with PII signaling protein trimer; in vivo complex of enzyme with signal transduction protein PII	659433
additional information	Oryza sativa	-	possible interaction of enzyme with PII signal proteins in vivo	660146

POSTTRANSLATIONAL MODIFICATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
side-chain modification	Xanthomonas campestris	-	methylation of surface lysine residues	671144

Crystallization/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
as complex with PII protein, NAGK binds Mg2+, ADP, arginine and N-acetylglutamate; hanging drop vapor diffusion method at room temperature, crystal structure of a complex formed between two homotrimers of PII and a single hexamer of enzyme bound to the metabolites N-acetylglutamate, ADP, ATP, and arginine	Arabidopsis thaliana	-	674874
-	Escherichia coli	-	642363
in complex with MgADP-, N-acetyl-glutamte, AlF4-, with MgADP-, N-acetyl-glutamte, with ADp and SO42-	Escherichia coli	-	642359
-	Pseudomonas aeruginosa	-	642361
without arginine	Pseudomonas aeruginosa	-	675366
hanging-drop vapor diffusion method	Streptococcus mutans	-	689895
crystal structure of the complex between acetylglutamate kinase and PII of Synechococcus elongatus, at 2.75 A resolution	Synechococcus elongatus	Q6V1L5	689765
in complex with arginine	Thermotoga maritima	Q9X2A4	675366
of the recombinant wild type protein, the selenomethionine substituted enzyme, the mutants and the methylated enzyme, cocrystallization with ATP, ADP, acetyl-CoA, CoA, N-acetyl-L-glutamate, adenylylimidodiphosphate, arginine	Xanthomonas campestris	-	671144

pH STABILITY	pH STABILITY MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

TEMPERATURE STABILITY	TEMPERATURE STABILITY MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
64	-	Chlamydomonas reinhardtii	-	10 min, 75% loss of activity without stabilizer, about 40% loss of activity with 75 mM N-acetyl-L-glutamate, 10 min, 10% loss of activity with 1 mM L-arginine	642353
70	-	Pseudomonas aeruginosa	-	30 min, complete inactivation	659050
70	-	Thermotoga maritima	-	1 h, 100% residual activity	659050
80	-	Thermotoga maritima	-	1 h, 80% residual activity	659050
85	-	Thermotoga maritima	-	1 h, 60% residual activity	659050
additional information	-	Chlamydomonas reinhardtii	-	-	642354

GENERAL STABILITY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
L-arginine protects against inactivating effects of high concentrations of urea	Chlamydomonas reinhardtii	-	642353
L-arginine protects against the inactivating effects of heat	Chlamydomonas reinhardtii	-	642353, 642354
urea, 4.0 M, complete loss of activity after 120 min	Chlamydomonas reinhardtii	-	642353
loss of activity on repeated freezing and thawing	Escherichia coli	-	642351
loss of activity on repeated freezing and thawing	Pseudomonas aeruginosa	-	642355

ORGANIC SOLVENT	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

OXIDATION STABILITY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
No entries in this field

STORAGE STABILITY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
-20�C, stable over extended periods	Pseudomonas aeruginosa	-	642355
4�C, 0.1 M phosphate buffer, stable	Pseudomonas aeruginosa	-	642355

Purification/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
-	Arabidopsis thaliana	-	674874, 705148
affinity chromatography and gel filtration by binding to the PII protein, Ni-nitrilotriacetic acid agarose to purify the recombinant protein	Arabidopsis thaliana	-	674751
His-Select nickel affinity gel column chromatography	Arabidopsis thaliana	-	702066
of the recombinant protein	Arabidopsis thaliana	-	673641
-	Chlamydomonas reinhardtii	-	642353, 642354
-	Escherichia coli	-	642351, 642354
-	Pisum sativum	-	642358
-	Pseudomonas aeruginosa	-	642355, 642356
-	Streptococcus mutans	-	689895
-	Synechococcus elongatus	-	705148
recombinant enzyme	Thermotoga maritima	-	659050
of the recombinant protein	Xanthomonas campestris	Q8P8J7	671144, 672794

Cloned/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
expressed in Escherichia coli	Arabidopsis thaliana	-	702066
expressed in Escherichia coli BL21(DE3) cells	Arabidopsis thaliana	-	705148
expression in Escherichia coli	Arabidopsis thaliana	-	673641, 674751, 674874
-	Pseudomonas aeruginosa	-	642361
expression in Escherichia coli	Streptococcus mutans	-	689895
expressed in Escherichia coli BL21(DE3) cells	Synechococcus elongatus	-	705148
expression in Escherichia coli	Xanthomonas campestris	-	672794
expression in Escherichia coli, selenomethionine substituted enzyme, site directed mutagenesis	Xanthomonas campestris	-	671144

EXPRESSION	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
No entries in this field

ENGINEERING	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
D162E	Escherichia coli	-	about 0.1% of wild-type activity	659704
K8R	Escherichia coli	-	substantial although diminished activity	659704
N158K	Escherichia coli	-	substantial although diminished activity	659704
R66K	Escherichia coli	-	substantial although diminished activity	659704
E17A	Pseudomonas aeruginosa	-	site-directed mutagenesis, the mutant shows reduced Vmax, the mutation results in decreased affinity of NAGK for arginine	692856
E17D	Pseudomonas aeruginosa	-	site-directed mutagenesis, the mutant shows reduced Vmax, the mutation results in decreased affinity of NAGK for arginine	692856
E17Q	Pseudomonas aeruginosa	-	site-directed mutagenesis, the mutant shows reduced Vmax, the mutation results in decreased affinity of NAGK for arginine	692856
E284D	Pseudomonas aeruginosa	-	site-directed mutagenesis, the mutant shows reduced Vmax and altered Km for the substrates	692856
G290A	Pseudomonas aeruginosa	-	site-directed mutagenesis, the mutant shows reduced Vmax and altered Km for the substrates	692856
H271N	Pseudomonas aeruginosa	-	site-directed mutagenesis, the mutant shows reduced Vmax and altered Km for the substrates	692856
Q10A	Pseudomonas aeruginosa	-	site-directed mutagenesis, the mutant shows reduced Vmax and altered Km for the substrates	692856
R24E	Pseudomonas aeruginosa	-	site-directed mutagenesis, the mutant shows reduced Vmax , the mutation results in increased affinity of NAGK for arginine	692856
Y21A	Pseudomonas aeruginosa	-	site-directed mutagenesis, the mutant shows reduced Vmax and altered Km for the substrates	692856
E186A/E387A	Xanthomonas campestris	-	to improve resolution in crystallization	671144
E416A/K417A	Xanthomonas campestris	-	to improve resolution in crystallization	671144
E94A/K95A	Xanthomonas campestris	-	to improve resolution in crystallization	671144
K26A/E27A	Xanthomonas campestris	-	to improve resolution in crystallization	671144
K279A/E280A	Xanthomonas campestris	-	to improve resolution in crystallization	671144
K419A	Xanthomonas campestris	-	to improve resolution in crystallization	671144
K213	Pseudomonas aeruginosa	-	site-directed mutagenesis, the mutant shows reduced Vmax and altered Km for the substrates	692856
additional information	Pseudomonas aeruginosa	-	N-helix N-terminal deletions spanning 16 residues dissociate NAGK to active dimers, those of 20 residues decrease the apparent affinity for arginine, and complete N-helix deletion of 26 residues abolishes arginine inhibition, overview	692856

Renatured/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
No entries in this field

APPLICATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

REF.	AUTHORS	TITLE	JOURNAL	VOL.	PAGES	YEAR	ORGANISM	LINK TO PUBMED	SOURCE
390278	Baich, A.; Vogel, H.J.	N-acetyl-gamma-glutamokinase and N-acetylglutamic gamma-semialdehyde dehydrogenase: Repressible enzymes of arginine synthesis in Escherichia coli	Biochem. Biophys. Res. Commun.	7	491-496	1962	Escherichia coli	PubMed
390290	Abadjieva, A.; Pauwels, K.; Hilven, P.; Crabeel, M.	A new yeast metabolon involving at least the two first enzymes of arginine biosynthesis. Acetylglutamate synthase activity requires complex formation with acetylglutamate kinase	J. Biol. Chem.	276	42869-42880	2001	Saccharomyces cerevisiae	PubMed
486081	Pauwels, K.; Abadjieva, A.; Hilven, P.; Stankiewicz, A.; Crabeel, M.	The N-acetylglutamate synthase/N-acetylglutamate kinase metabolon of Saccharomyces cerevisiae allows co-ordinated feedback regulation of the first two steps in arginine biosynthesis	Eur. J. Biochem.	270	1014-1024	2003	Saccharomyces cerevisiae	PubMed
642351	Vogel, H.J.; McLellan, W.L.	N-Acetyl-gamma-glutamokinase (Escherichia coli)	Methods Enzymol.	17A	251-255	1970	Escherichia coli	-
642353	Farago, A.; Denes, G.	Mechanism of arginine biosynthesis in Chlamydomonas reinhardti. II. Purification and properties of N-acetylglutamate 5-phosphotransferase, the allosteric enzyme of the pathway	Biochim. Biophys. Acta	136	6-18	1967	Chlamydomonas reinhardtii	PubMed
642354	Denes, G.	N-Acetylglutamate-5-phosphotransferase	The Enzymes,3rd Ed. (Boyer,P.D.,ed.)	9	511-520	1973	Chlamydomonas reinhardtii, Escherichia coli	-
642355	Haas, D.; Leisinger, T.	N-acetylglutamate 5-phosphotransferase of Pseudomonas aeruginosa. Purification and ligand-directed association-dissociation	Eur. J. Biochem.	52	365-375	1975	Pseudomonas aeruginosa	PubMed
642356	Haas, D.; Leisinger, T.	N-acetylglutamate 5-phosphotransferase of Pseudomonas aeruginosa. Catalytic and regulatory properties	Eur. J. Biochem.	52	377-383	1975	Pseudomonas aeruginosa	PubMed
642357	Wolf, E.C.; Weiss, R.L.	Acetylglutamate kinase. A mitochondrial feedback-sensitive enzyme of arginine biosynthesis in Neurospora crassa	J. Biol. Chem.	255	9189-9195	1980	Neurospora crassa	PubMed
642358	McKay, G.; Shargool, P.D.	Purification and characterization of N-acetylglutamate 5-phosphotransferase from pea (Pisum sativum) cotyledons	Biochem. J.	195	71-81	1981	Pisum sativum	PubMed
642359	Gil-Ortiz, F.; Ramon-Maiques, S.; Fita, I.; Rubio, V.	The course of phosphorus in the reaction of N-acetyl-L-glutamate kinase, determined from the structures of crystalline complexes, including a complex with an AlF(4)(-) transition state mimic	J. Mol. Biol.	331	231-244	2003	Escherichia coli	PubMed
642361	Fernandez-Murga, M.L.; Ramon-Maiques, S.; Gil-Ortiz, F.; Fita, I.; Rubio, V.	Towards structural understanding of feedback control of arginine biosynthesis: cloning and expression of the gene for the arginine-inhibited N-acetyl-L-glutamate kinase from Pseudomonas aeruginosa, purification and crystallization of the recombinant enzyme and preliminary X-ray studies	Acta Crystallogr. Sect. D	58	1045-1047	2002	Pseudomonas aeruginosa	PubMed
642363	Ramon-Maiques, S.; Marina, A.; Gil-Ortiz, F.; Fita, I.; Rubio, V.	Structure of acetylglutamate kinase, a key enzyme for arginine biosynthesis and a prototype for the amino acid kinase enzyme family, during catalysis	Structure	10	329-342	2002	Escherichia coli	PubMed
659050	Fernandez-Murga, M.L.; Gil-Ortiz, F.; Llacer, J.L.; Rubio, V.	Arginine biosynthesis in Thermotoga maritima: characterization of the arginine-sensitive N-acetyl-L-glutamate kinase	J. Bacteriol.	186	6142-6149	2004	Pseudomonas aeruginosa, Thermotoga maritima	PubMed
659433	Maheswaran, M.; Urbanke, C.; Forchhammer, K.	Complex formation and catalytic activation by the PII signaling protein of N-acetyl-L-glutamate kinase from Synechococcus elongatus strain PCC 7942	J. Biol. Chem.	279	55202-55210	2004	Synechococcus elongatus	PubMed
659704	Marco-Marin, C.; Ramon-Maiques, S.; Tavarez, S.; Rubio, V.	Site-directed mutagenesis of Escherichia coli acetylglutamate kinase and aspartokinase III probes the catalytic and substrate-binding mechanisms of these amino acid kinase family enzymes and allows three-dimensional modelling of aspartokinase	J. Mol. Biol.	334	459-476	2003	Escherichia coli	PubMed
660146	Sugiyama, K.; Hayakawa, T.; Kudo, T.; Ito, T.; Yamaya, T.	Interaction of N-acetylglutamate kinase with a PII-like protein in rice	Plant Cell Physiol.	45	1768-1778	2004	Oryza sativa	PubMed
671144	Shi, D.; Caldovic, L.; Jin, Z.; Yu, X.; Qu, Q.; Roth, L.; Morizono, H.; Hathout, Y.; Allewell, N.M.; Tuchman, M.	Expression, crystallization and preliminary crystallographic studies of a novel bifunctional N-acetylglutamate synthase/kinase from Xanthomonas campestris homologous to vertebrate N-acetylglutamate synthase	Acta Crystallogr. Sect. F	F62	1218-1222	2006	Xanthomonas campestris	PubMed
672794	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	BMC Biochem.	8	4-16	2007	Xanthomonas campestris	PubMed
673641	Ferrario-Mery, S.; Besin, E.; Pichon, O.; Meyer, C.; Hodges, M.	The regulatory PII protein controls arginine biosynthesis in Arabidopsis	FEBS Lett.	580	2015-2020	2006	Arabidopsis thaliana	PubMed
674751	Chen, Y.M.; Ferrar, T.S.; Lohmeir-Vogel, E.; Morrice, N.; Mizuno, Y.; Berenger, B.; Ng, K.K.; Muench, D.G.; Moorhead, G.B.	The PII signal transduction protein of Arabidopsis thaliana forms an arginine-regulated complex with plastid N-acetyl glutamate kinase	J. Biol. Chem.	281	5726-5733	2006	Arabidopsis thaliana	PubMed
674874	Mizuno, Y.; Moorhead, G.B.; Ng, K.K.	Structural basis for the regulation of N-acetylglutamate kinase by PII in Arabidopsis thaliana	J. Biol. Chem.	282	35733-35740	2007	Arabidopsis thaliana	PubMed
675366	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	J. Mol. Biol.	356	695-713	2006	Pseudomonas aeruginosa, Thermotoga maritima	PubMed
689765	Llacer, J.L.; Contreras, A.; Forchhammer, K.; Marco-Marin, C.; Gil-Ortiz, F.; Maldonado, R.; Fita, I.; Rubio, V.	The crystal structure of the complex of PII and acetylglutamate kinase reveals how PII controls the storage of nitrogen as arginine	Proc. Natl. Acad. Sci. USA	104	17644-17649	2007	Synechococcus elongatus	PubMed
689895	Wu, C.W.; Li, L.F.; Liu, X.; Gao, X.Z.; Lei, J.; Su, X.D.; Zhao, X.; Liang, Y.H.	Protein preparation, crystallization and preliminary X-ray crystallographic analysis of N-acetylglutamate kinase from Streptococcus mutans	Protein Pept. Lett.	15	541-543	2008	Streptococcus mutans	PubMed
692856	Fernandez-Murga, M.L.; Rubio, V.	Basis of arginine sensitivity of microbial N-acetyl-L-glutamate kinases: mutagenesis and protein engineering study with the Pseudomonas aeruginosa and Escherichia coli enzymes	J. Bacteriol.	190	3018-3025	2008	Pseudomonas aeruginosa	PubMed
702066	Feria Bourrellier, A.; Ferrario-M�ry, S.; Vidal, J.; Hodges, M.	Metabolite regulation of the interaction between Arabidopsis thaliana PII and N-acetyl-l-glutamate kinase	Biochem. Biophys. Res. Commun.	387	700-704	2009	Arabidopsis thaliana	PubMed
704614	Min, L.; Jin, Z.; Caldovic, L.; Morizono, H.; Allewell, N.M.; Tuchman, M.; Shi, D.	Mechanism of allosteric inhibition of N-acetyl-L-glutamate synthase by L-arginine	J. Biol. Chem.	284	4873-4880	2009	Arabidopsis thaliana, Pseudomonas aeruginosa	PubMed
705148	Beez, S.; Fokina, O.; Herrmann, C.; Forchhammer, K.	N-acetyl-L-glutamate kinase (NAGK) from oxygenic phototrophs: P(II) signal transduction across domains of life reveals novel insights in NAGK control	J. Mol. Biol.	389	748-758	2009	Arabidopsis thaliana, Synechococcus elongatus	PubMed

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