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Information on EC 2.7.2.8 - acetylglutamate kinase and Organism(s) Synechococcus elongatus and UniProt Accession Q6V1L5

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This record set is specific for:
Synechococcus elongatus
UNIPROT: Q6V1L5 not found.
Word Map
The taxonomic range for the selected organisms is: Synechococcus elongatus
The enzyme appears in selected viruses and cellular organisms
Synonyms
acetylglutamate kinase, acetylglutamate phosphokinase, amino-acid acetyltransferase, argB, CcNAGK, EcNAGK, kinase, acetylglutamate (phosphorylating), mmNAGS/K, N-acetyl-glutamate 5-phosphotransferase, N-acetyl-L-glutamate 5-phosphotransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetylglutamate phosphokinase
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kinase, acetylglutamate (phosphorylating)
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N-acetyl-L-glutamate kinase
277225
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N-acetylglutamate 5-phosphotransferase
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N-acetylglutamate kinase
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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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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
additional information
?
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NAGK interacts with PII protein
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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
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?
additional information
?
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NAGK interacts with PII protein
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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required, maximum activity above 20 mM
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ADP
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inhibitor of complex formation with PII protein
arginine
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feedback inhibition
L-arginine
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complete inhibition at 0.1-1.0 mM, PII-mediated relief from L-arginine inhibition is antagonized by 2-oxoglutarate
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
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maximum activity at 10 mM
PII protein
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.6 - 1.1
ATP
2.7 - 27.4
N-acetyl-L-glutamate
additional information
additional information
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formation of complex between enzyme and signal transduction protein PII decreases Km-value by a factor of 10 and increases Vmax 4fold
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
13.1 - 40.4
N-acetyl-L-glutamate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.7 - 13
N-acetyl-L-glutamate
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.02 - 0.19
L-arginine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
13.3
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pH 7.5, complex of enzyme and PII protein
3.3
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pH 7.5, free enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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both free enzyme and complex with protein PII
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
180000
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sedimentation anaylsis
32000
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6 * 32000, calculated
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
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6 * 32000, calculated
additional information
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enzyme hexamer forms a complex with PII signaling protein trimer; in vivo complex of enzyme with signal transduction protein PII
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of the complex between acetylglutamate kinase and PII of Synechococcus elongatus, at 2.75 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R233A
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mutant does not interact in vitro with PII protein of wild-type sequence in yeast two-hybrid analysis. Mutant interacts with PII variants containing I86N or I86T mutation
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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 (Q6V1L5), Synechococcus elongatus
Manually annotated by BRENDA team
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, Arabidopsis thaliana (Q9SCL7), Synechococcus elongatus
Manually annotated by BRENDA team
Fokina, O.; Chellamuthu, V.R.; Zeth, K.; Forchhammer, K.
A novel signal transduction protein P(II) variant from Synechococcus elongatus PCC 7942 indicates a two-step process for NAGK-P(II) complex formation
J. Mol. Biol.
399
410-421
2010
Synechococcus elongatus
Manually annotated by BRENDA team
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