Any feedback?
Information on EC 2.7.2.8 - acetylglutamate kinase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9SCL7
for references in articles please use BRENDA:EC2.7.2.8Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.7.2.8 acetylglutamate kinaseSpecify your search results
Word Map
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
n-acetyl-l-glutamate kinase, acetylglutamate kinase, n-acetylglutamate kinase, n-acetyl glutamate kinase, mmnags/k, ynagk, n-acetylglutamate 5-phosphotransferase, ccnagk, ecnagk, n-acetylglutamate-5-phosphotransferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetylglutamate phosphokinase
-
-
-
-
kinase, acetylglutamate (phosphorylating)
-
-
-
-
N-acetylglutamate 5-phosphotransferase
-
-
-
-
N-acetylglutamate kinase
-
-
-
-
N-acetylglutamate phosphokinase
-
-
-
-
N-acetylglutamate-5-phosphotransferase
-
-
-
-
N-acetylglutamic 5-phosphotransferase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
phospho group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
ATP:N-acetyl-L-glutamate 5-phosphotransferase
-
CAS REGISTRY NUMBER
COMMENTARY
9027-58-1
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamyl 5-phosphate
-
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
-
-
-
-
?
additional information
?
-
-
NAGK strongly interacts with PII protein only in the presence of Mg-ATP, this process is reversed by 2-oxoglutarate
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
-
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
-
-
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
-
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
-
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamyl 5-phosphate
-
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
-
-
-
-
?
additional information
?
-
-
NAGK strongly interacts with PII protein only in the presence of Mg-ATP, this process is reversed by 2-oxoglutarate
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
L-arginine
complete inhibition at 3-5 mM, PII-mediated relief from L-arginine inhibition is antagonized by 2-oxoglutarate
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
2-ketoglutarate shows no additive effect to the activation of PII protein
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.3
ATP
in the absence of protein PII, in 50 mM imidazole, pH 7.5
0.4
ATP
in the absence of protein PII, in 50 mM imidazole, pH 7.5
0.85
N-acetyl-L-glutamate
in the absence of protein PII, in 50 mM imidazole, pH 7.5
0.87
N-acetyl-L-glutamate
in the absence of protein PII, in 50 mM imidazole, pH 7.5
9.45
N-acetyl-L-glutamate
in complex with PII protein and 2-ketoglutarate
85
N-acetyl-L-glutamate
in the presence of 1 mM L-arginine, in 50 mM imidazole, pH 7.5
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
115
N-acetyl-L-glutamate
in the presence of 1 mM L-arginine, in 50 mM imidazole, pH 7.5
126.1
N-acetyl-L-glutamate
in the absence of protein PII, in 50 mM imidazole, pH 7.5
187.5
N-acetyl-L-glutamate
in the presence of protein PII, in 50 mM imidazole, pH 7.5
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.3
N-acetyl-L-glutamate
in the presence of 1 mM L-arginine, in 50 mM imidazole, pH 7.5
145
N-acetyl-L-glutamate
in the absence of protein PII, in 50 mM imidazole, pH 7.5
220
N-acetyl-L-glutamate
in the presence of protein PII, in 50 mM imidazole, pH 7.5
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1
L-arginine
Arabidopsis thaliana
in the absence of protein PII, in 50 mM imidazole, pH 7.5
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
enzyme mutations lower pollen tube competitiveness. Mutant pollen tubes grow more slowly than wild type pollen tubes. Mutant female gametophytes are defective in micropylar pollen tube guidance. Loss-of-function of enzyme results in Arabidopsis embryos not developing beyond the four-celled embryo stage
metabolism
the enzyme catalyzes the second step of arginine biosynthesis
physiological function
the enzyme is required for both gametophyte function and embryo development
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). NAGK_ARATH
347
0
36595
Swiss-Prot
Chloroplast (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
affinity chromatography and gel filtration by binding to the PII protein, Ni-nitrilotriacetic acid agarose to purify the recombinant protein
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in enzyme-deficient Escherichia coli mutant strain JW5553-1
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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 (Q9SCL7)
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 (Q9SCL7), Arabidopsis thaliana
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, Arabidopsis thaliana (Q9SCL7)
Feria Bourrellier, A.; Ferrario-Mry, 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
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)
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
Synechococcus elongatus, Arabidopsis thaliana (Q9SCL7), Arabidopsis thaliana
EXTERNAL LINKS (specific for EC-Number 2.7.2.8)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
