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Information on EC 2.7.2.8 - acetylglutamate kinase and Organism(s) Escherichia coli and UniProt Accession P0A6C8

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Escherichia coli
UNIPROT: P0A6C8 not found.
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The taxonomic range for the selected organisms is: Escherichia coli
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, acetylglutamate phosphokinase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N-acetylglutamate kinase
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acetylglutamate phosphokinase
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-
-
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EcNAGK
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
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-
-
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N-acetylglutamate phosphokinase
-
-
-
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N-acetylglutamate-5-phosphotransferase
-
-
-
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N-acetylglutamic 5-phosphotransferase
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-
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate
show the reaction diagram
mechanism
ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate
show the reaction diagram
using an elastic network model representation a normal mode analysis shows that the conformational mechanisms for substrate binding by NAGK strongly correlate with the intrinsic dynamics of the enzyme in the unbound form. The conformational change observed between the open and closed forms of EcNAGK are essentially accomplished by movements along a small subset of modes
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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-
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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
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-glutamyl 5-phosphate
show the reaction diagram
-
-
-
?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
arginine
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enzyme has no allosteric properties and its activity is influenced neither by arginine nor by any of the intermediates of the arginine biosynthetic pathway
additional information
the enzyme is L-arginine-insensitive
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.29 - 7.9
ATP
0.2 - 898
N-acetyl-L-glutamate
1 - 13.4
ATP
1.3 - 6
N-acetyl-L-glutamate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
30.4 - 41.5
ATP
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.54
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pH 7.4, 37°C
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
2 * 27000, SDS-PAGE
dimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with MgADP-, N-acetyl-glutamte, AlF4-, with MgADP-, N-acetyl-glutamte, with ADp and SO42-
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D162E
about 0.1% of wild-type activity
K8R
substantial although diminished activity
N158K
substantial although diminished activity
R66K
substantial although diminished activity
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
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
loss of activity on repeated freezing and thawing
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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, Escherichia coli Wc2
Manually annotated by BRENDA team
Vogel, H.J.; McLellan, W.L.
N-Acetyl-gamma-glutamokinase (Escherichia coli)
Methods Enzymol.
17A
251-255
1970
Escherichia coli, Escherichia coli W2D / ATCC 25542
-
Manually annotated by BRENDA team
Denes, G.
N-Acetylglutamate-5-phosphotransferase
The Enzymes,3rd Ed. (Boyer,P. D. ,ed. )
9
511-520
1973
Chlamydomonas reinhardtii, Escherichia coli
-
Manually annotated by BRENDA team
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 (P0A6C8)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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 (P0A6C8), Escherichia coli
Manually annotated by BRENDA team
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
J. Mol. Biol.
399
476-490
2010
Escherichia coli (A0A140NEG9), Escherichia coli
Manually annotated by BRENDA team
Marcos, E.; Crehuet, R.; Bahar, I.
Changes in dynamics upon oligomerization regulate substrate binding and allostery in amino acid kinase family members
PLoS Comput. Biol.
7(9)
e1002201
2011
Escherichia coli
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