Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.7.2.8 - acetylglutamate kinase and Organism(s) Thermotoga maritima and UniProt Accession Q9X2A4

for references in articles please use BRENDA:EC2.7.2.8
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Thermotoga maritima
UNIPROT: Q9X2A4 not found.
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Thermotoga maritima
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, n-acetylglutamate-5-phosphotransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetylglutamate kinase
-
N-acetyl-L-glutamate 5-phosphotransferase
-
N-acetylglutamate kinase
-
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 hide
LITERATURE
phospho group transfer
-
phospho group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:N-acetyl-L-glutamate 5-phosphotransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9027-58-1
-
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
-
-
-
-
?
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
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
L-arginine
-
pH and temperature dependent, sigmoidal dependence on concentration of arginine, Hill coefficient of 4, 1 mM, 37°C, 95% inhibition
L-arginine methyl ester
-
1 mM, 80% inhibition
additional information
-
not inhibitory: D-arginine, agmatine, citrulline, L-canavanine, L-lysine, L-ornithine, guanidinium ions, urea at 1 mM, 37°C
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
-
37°C, pH 7.5
677
-
80°C, pH 7.5
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
30341
-
6 * 30341, MALDI-TOF MS, 6 * 30344, calculated
30344
-
6 * 30341, MALDI-TOF MS, 6 * 30344, calculated
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
hexamer
-
6 * 30341, MALDI-TOF MS, 6 * 30344, calculated
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with arginine
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70
-
1 h, 100% residual activity
80
-
1 h, 80% residual activity
85
-
1 h, 60% residual activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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