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Information on EC 2.7.2.8 - acetylglutamate kinase and Organism(s) Pseudomonas aeruginosa and UniProt Accession Q9HTN2

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Pseudomonas aeruginosa
UNIPROT: Q9HTN2 not found.
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The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
n-acetyl-l-glutamate kinase, acetylglutamate kinase, n-acetylglutamate kinase, mmnags/k, n-acetyl glutamate kinase, ynagk, n-acetylglutamate 5-phosphotransferase, ccnagk, ecnagk, acetylglutamate phosphokinase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetylglutamate kinase
-
N-acetyl-L-glutamate 5-phosphotransferase
-
N-acetyl-L-glutamate kinase
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N-acetylglutamate kinase
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acetylglutamate phosphokinase
-
-
-
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kinase, acetylglutamate (phosphorylating)
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-
-
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N-acetylglutamate 5-phosphotransferase
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-
-
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N-acetylglutamate kinase
N-acetylglutamate phosphokinase
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-
-
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N-acetylglutamate-5-phosphotransferase
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-
-
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N-acetylglutamic 5-phosphotransferase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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phospho group transfer
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:N-acetyl-L-glutamate 5-phosphotransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
9027-58-1
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
show the reaction diagram
-
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamyl 5-phosphate
show the reaction diagram
-
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
show the reaction diagram
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamyl 5-phosphate
show the reaction diagram
ATP + N-carbamoyl-L-glutamate
ADP + N-carbamoyl-L-glutamate 5-phosphate
show the reaction diagram
-
at 33% of the activity with N-acetyl-L-glutamate
-
-
?
ATP + N-formyl-L-glutamate
ADP + N-formyl-L-glutamate 5-phosphate
show the reaction diagram
-
at 20% of the activity with N-acetyl-L-glutamate
-
-
?
dATP + N-acetyl-L-glutamate
dADP + N-acetyl-L-glutamate 5-phosphate
show the reaction diagram
-
as effective as ATP
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
show the reaction diagram
-
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamyl 5-phosphate
show the reaction diagram
-
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
show the reaction diagram
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamyl 5-phosphate
show the reaction diagram
-
NAGK catalyzes the second step of arginine biosynthesis. In Pseudomonas aeruginosa, this step is rate limiting, and feedback regulated and sigmoidally inhibited by arginine
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
Mn2+, Zn2+, Co2+ and Ca2+ in this order can partially replace Mg2+
Co2+
-
Mn2+, Zn2+, Co2+ and Ca2+ in this order can partially replace Mg2+
Mn2+
-
Mn2+, Zn2+, Co2+ and Ca2+ in decreasing order can partially replace Mg2+
Zn2+
-
Mn2+, Zn2+, Co2+ and Ca2+ in this order can partially replace Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
arginine
L-arginine
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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
L-citrulline
-
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MgCl2
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30 mM, slight inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3 - 3.1
ATP
2 - 3.1
N-acetyl-L-glutamate
additional information
additional information
-
kinetics of enzyme mutants, overview
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
130
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37°C, pH 7.5
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
180000
-
gel filtration
230000
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gel filtration
29000
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x * 29000, SDS-PAGE
30000
-
2 * 30000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
?
-
x * 29000, SDS-PAGE
dimer
-
2 * 30000, SDS-PAGE
hexamer
-
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
additional information
-
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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E17A
-
site-directed mutagenesis, the mutant shows reduced Vmax, the mutation results in decreased affinity of NAGK for arginine
E17D
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site-directed mutagenesis, the mutant shows reduced Vmax, the mutation results in decreased affinity of NAGK for arginine
E17Q
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site-directed mutagenesis, the mutant shows reduced Vmax, the mutation results in decreased affinity of NAGK for arginine
E284D
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site-directed mutagenesis, the mutant shows reduced Vmax and altered Km for the substrates
G290A
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site-directed mutagenesis, the mutant shows reduced Vmax and altered Km for the substrates
H271N
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site-directed mutagenesis, the mutant shows reduced Vmax and altered Km for the substrates
K213
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site-directed mutagenesis, the mutant shows reduced Vmax and altered Km for the substrates
Q10A
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site-directed mutagenesis, the mutant shows reduced Vmax and altered Km for the substrates
R24E
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site-directed mutagenesis, the mutant shows reduced Vmax , the mutation results in increased affinity of NAGK for arginine
Y21A
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site-directed mutagenesis, the mutant shows reduced Vmax and altered Km for the substrates
additional information
-
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70
-
30 min, complete inactivation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
loss of activity on repeated freezing and thawing
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, stable over extended periods
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4°C, 0.1 M phosphate buffer, stable
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
Haas, D.; Leisinger, T.
N-acetylglutamate 5-phosphotransferase of Pseudomonas aeruginosa. Catalytic and regulatory properties
Eur. J. Biochem.
52
377-383
1975
Pseudomonas aeruginosa
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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 (Q9HTN2), Pseudomonas aeruginosa, Thermotoga maritima (Q9X2A4), Thermotoga maritima
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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 (Q9HTN2)
Manually annotated by BRENDA team
Yang, X.
Conformational dynamics play important roles upon the function of N-acetylglutamate kinase
Appl. Microbiol. Biotechnol.
101
3485-3492
2017
Escherichia coli (P0A6C8), Corynebacterium glutamicum (Q59281), Pseudomonas aeruginosa (Q9HTN2), Thermotoga maritima (Q9X2A4), Corynebacterium glutamicum ATCC 13032 (Q59281)
Manually annotated by BRENDA team