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Information on EC 2.7.2.8 - acetylglutamate kinase and Organism(s) Saccharomyces cerevisiae and UniProt Accession Q01217

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Saccharomyces cerevisiae
UNIPROT: Q01217 not found.
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetylglutamate phosphokinase
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kinase, acetylglutamate (phosphorylating)
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N-acetyl glutamate kinase
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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
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate
show the reaction diagram
enzyme has to interact stoichiometrically with acetylglutamate synthase in order to be active
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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
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?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamate 5-phosphate
show the reaction diagram
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?
ATP + N-acetyl-L-glutamate
ADP + N-acetyl-L-glutamyl 5-phosphate
show the reaction diagram
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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-glutamyl 5-phosphate
show the reaction diagram
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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10 mM used in assay conditions
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
arginine
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feedback regulation of enzyme and N-acetylglutamate synthase is mutually interdependent, enzymes form a complex
L-arginine
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wild type enzyme activity drastically decreases by addition of 0.2 mM L-Arg, and consequently decreases when L-Arg concentration is increased, indicating that the enzyme activity is subject to feedback inhibition by L-Arg. Enzyme activity is almost lost in the presence of 1.0 mM L-Arg
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
15.3 - 20.1
ATP
10 - 13.3
N-acetyl-L-glutamate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7.7 - 13
ATP
4.9 - 8.4
N-acetyl-L-glutamate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
400
L-arginine
DELTA357-513 (truncated mutant lacking C-terminal 150 amino acids), pH not specified, 37°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.44 - 0.97
L-arginine
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
52000
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x * 52000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 52000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures of both the DUF619 domain-lacking yNAGK, ligand-free as well as complexed with acetylglutamate or acetylglutamate and arginine, and of complete mature yNAGK are determined. yNAGK has as central structure a flat tetramer formed by two dimers of amino acid kinase domains
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DELTA357-513
truncated mutant lacking C-terminal 150 amino acids (spanning residues 38-356), belonging to the DUF619 domain family, shows that is it stabilizes yNAGK, slows catalysis and modulates feed-back inhibition by arginine. Truncated yNAGK shows doubled kcat compared to wild-type, Km is almost not affected. IC50 (L-arginine) is lowered compared to wild-type. Truncated mutand shows lower thermal stability compared to wild-type
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
using Ni-NTA chromatography
Ni Sepharose column chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli as a His-tagged fusion protein
wild type and mutant enzyme T340I are expressed in Escherichia coli DH5alpha and BL21 (DE3) cells
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Abadjieva, A.; Pauwels, K.; Hilven, P.; Crabeel, M.
A new yeast metabolon involving at least the two first enzymes of arginine biosynthesis. Acetylglutamate synthase activity requires complex formation with acetylglutamate kinase
J. Biol. Chem.
276
42869-42880
2001
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Pauwels, K.; Abadjieva, A.; Hilven, P.; Stankiewicz, A.; Crabeel, M.
The N-acetylglutamate synthase/N-acetylglutamate kinase metabolon of Saccharomyces cerevisiae allows co-ordinated feedback regulation of the first two steps in arginine biosynthesis
Eur. J. Biochem.
270
1014-1024
2003
Saccharomyces cerevisiae
Manually annotated by BRENDA team
de Cima, S.; Gil-Ortiz, F.; Crabeel, M.; Fita, I.; Rubio, V.
Insight on an arginine synthesis metabolon from the tetrameric structure of yeast acetylglutamate kinase
PLoS ONE
7
e34734
2012
Saccharomyces cerevisiae (Q01217), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Ohashi, M.; Nasuno, R.; Isogai, S.; Takagi, H.
High-level production of ornithine by expression of the feedback inhibition-insensitive N-acetyl glutamate kinase in the sake yeast Saccharomyces cerevisiae
Metab. Eng.
62
1-9
2020
Saccharomyces cerevisiae, Saccharomyces cerevisiae K901
Manually annotated by BRENDA team