Information on EC 2.7.2.8 - acetylglutamate kinase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY hide
2.7.2.8
-
RECOMMENDED NAME
GeneOntology No.
acetylglutamate kinase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-arginine biosynthesis III (via N-acetyl-L-citrulline)
-
-
L-arginine biosynthesis II (acetyl cycle)
-
-
L-arginine biosynthesis IV (archaebacteria)
-
-
L-ornithine biosynthesis I
-
-
arginine metabolism
-
-
Arginine biosynthesis
-
-
Metabolic pathways
-
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Biosynthesis of secondary metabolites
-
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Biosynthesis of antibiotics
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:N-acetyl-L-glutamate 5-phosphotransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
9027-58-1
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain W2D, ATCC 25542, derepressed mutant
-
-
Manually annotated by BRENDA team
strain Wc2
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
pv. campestris
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
-
argB gene coding the N-acetyl-L-glutamate kinase is first overexpressed in the strain SYPA5-5, whereas the L-arginine production is narrowly increased by 15.4%
metabolism
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + L-glutamate
coenzyme A + N-acetyl-L-glutamate
show the reaction diagram
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-carbamoyl-L-glutamate
ADP + N-carbamoyl-L-glutamate 5-phosphate
show the reaction diagram
-
at 33% of the activity with N-acetyl-L-glutamate
-
-
-
ATP + N-formyl-L-glutamate
ADP + N-formyl-L-glutamate 5-phosphate
show the reaction diagram
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at 20% of the activity with N-acetyl-L-glutamate
-
-
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dATP + N-acetyl-L-glutamate
dADP + N-acetyl-L-glutamate 5-phosphate
show the reaction diagram
-
as effective as ATP
-
-
-
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
Mn2+, Zn2+, Co2+ and Ca2+ in this order can partially replace Mg2+
Zn2+
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Mn2+, Zn2+, Co2+ and Ca2+ in this order can partially replace Mg2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-oxoglutarate
-
complete inhibition at 0.5 mM
arginine
L-arginine
L-arginine methyl ester
-
1 mM, 80% inhibition
L-citrulline
MgCl2
trichloroacetic acid
complete inactivation at 30%
additional information
-
not inhibitory: D-arginine, agmatine, citrulline, L-canavanine, L-lysine, L-ornithine, guanidinium ions, urea at 1 mM, 37C
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-Ketoglutarate
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only if bound to the PII protein ATP complex
ATP
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maximum activity at 10 mM
L-arginine
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slight activation is observed at 1 mM L-arginine
PII protein
-
additional information
-
2-ketoglutarate shows no additive effect to the activation of PII protein
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.3
AcCoA
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only for N-acetylglutamate synthase activity
0.29 - 20.1
ATP
2.8
L-glutamate
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only for N-acetylglutamate synthase activity
0.2 - 898
N-acetyl-L-glutamate
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7.7 - 13
ATP
2 - 187.5
N-acetyl-L-glutamate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.3 - 220
N-acetyl-L-glutamate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
30.4 - 41.5
ATP
400
L-arginine
DELTA357-513 (truncated mutant lacking C-terminal 150 amino acids), pH not specified, 37C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.02 - 784
L-arginine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0008
-
pH 8.0, 70C, activity in cell culture in growth medium with 0.2% yeast extract
0.003
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pH 8.0, 70C, activity in cell culture in minimal growth medium with 20 mM glucose and 5 mM NH4+
0.47
purified mutant K364H enzyme, pH 8.5, 30C
0.54
-
pH 7.4, 37C
1.66
purified mutant R394K enzyme, pH 8.5, 30C
3.11
purified mutant N399Q enzyme, pH 8.5, 30C
3.3
-
pH 7.5, free enzyme
4.97
purified mutant S387A enzyme, pH 8.5, 30C
6.81
purified recominant wild-type enzyme, pH 8.5, 30C
12
-
without PII protein
13.3
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pH 7.5, complex of enzyme and PII protein
20.1
-
pH 7.4, 37C
24
-
with PII protein
39.87
purified mutant S387A enzyme, pH 8.5, 30C
44.05
purified recominant wild-type enzyme, pH 8.5, 30C
45
-
37C, pH 7.5
130
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37C, pH 7.5
677
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80C, pH 7.5
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.6 - 7
-
pH 4.6: about 75% of maximum activity, pH 7: about 60% of maximum activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
sheath and blade, coordinate expression of enzyme and PII-like protein GlnB during the life span
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain B / BL21-DE3)
Escherichia coli (strain B / BL21-DE3)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
Synechococcus elongatus (strain PCC 7942)
Synechococcus elongatus (strain PCC 7942)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29000
-
x * 29000, SDS-PAGE
30341
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6 * 30341, MALDI-TOF MS, 6 * 30344, calculated
30344
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6 * 30341, MALDI-TOF MS, 6 * 30344, calculated
32000
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6 * 32000, calculated
33000
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mass spectrometry
43000
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dimer or tetramer, 1 or 2 * 43000 + 1 or 2 * 53000, SDS-PAGE
52000
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x * 52000, SDS-PAGE
53000
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dimer or tetramer, 1 or 2 * 43000 + 1 or 2 * 53000, SDS-PAGE
93000
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gel filtration
180000
190000
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gel filtration in presence of N-acetylglutamate
198000
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calculated from amino acid sequence
230000
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gel filtration
400000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
homodimer
C6EE50
-
tetramer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
side-chain modification
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methylation of surface lysine residues
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
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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
C6EE50
in complex with MgADP-, N-acetyl-glutamte, AlF4-, with MgADP-, N-acetyl-glutamte, with ADp and SO42-
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crystal structure of Maricaulis maris NAGS/K (mmNAGS/K) at 2.7 A resolution shows that it is a tetramer
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purified enzyme in complex with L-arginine, sitting drop vapor diffusion method, mixing of 10 mg/ml protein in 50 mM Tris-HCl, pH 8.0, 50 mM NaCl, 10% glycerol, 5 mM 2-mercaptoethanol, and 1 mM EDTA with 1 mM L-arginine, and 10 mM N-acetyl-L-glutamate for 30 min, 0.002 ml of this protein solution is mixed with 0.002 ml of reservoir solution containing 100 mM sodium cacodylate trihydrate, pH 6.2, 25% PEG P400 and 200 mM magnesium chloride, X-ray diffraction structure determination and analysis at 2.8 A resolution. In contrast to the structure of mmNAGS/K in the absence of L-arginine where there are conformational differences between the four subunits in the asymmetric unit, all four subunits in the L-arginine liganded structure have very similar conformations
without arginine
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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
hanging-drop vapor diffusion method
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crystal structure of the complex between acetylglutamate kinase and PII of Synechococcus elongatus, at 2.75 A resolution
in complex with arginine
of the recombinant wild type protein, the selenomethionine substituted enzyme, the mutants and the methylated enzyme, cocrystallization with ATP, ADP, acetyl-CoA, CoA, N-acetyl-L-glutamate, adenylylimidodiphosphate, arginine
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
64
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10 min, 75% loss of activity without stabilizer, about 40% loss of activity with 75 mM N-acetyl-L-glutamate, 10 min, 10% loss of activity with 1 mM L-arginine
80
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1 h, 80% residual activity
85
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1 h, 60% residual activity
additional information
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
L-arginine protects against inactivating effects of high concentrations of urea
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L-arginine protects against the inactivating effects of heat
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loss of activity on repeated freezing and thawing
urea, 4.0 M, complete loss of activity after 120 min
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, stable over extended periods
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4C, 0.1 M phosphate buffer, stable
-
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
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His-Select nickel affinity gel column chromatography
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of the recombinant protein
recombinant enzyme
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recombinant His-tagged wild-type and mutant enzymes from Escherichia coli BL21(DE3) by nickel affinity chromatography
using Ni-NTA chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expressed in Escherichia coli as a His-tagged fusion protein
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
expression in Escherichia coli, selenomethionine substituted enzyme, site directed mutagenesis
-
gene argB, cloning in Escherichia coli strain JM109 and recombinant expression of wild-type and mutant enzymes in Corynebacterium crenatum strain SYPA5-5
recombinant His-tagged wild-type and mutant enzymes expression in Escherichia coli BL21(DE3)
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
threefold repression of enzyme formation by arginine
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A26V
site-directed mutagenesis, the mutation deregulates the feedback inhibition of the enzyme
G287D
site-directed mutagenesis, the mutation increases the 50% inhibitoryL--arginine concentration significantly in vitro, which deregulates the feedback inhibition of CcNAGK by L-arginine in SYPA5-5 during the fermentation
H268N/H26E
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Km and kcat (N-acetyl-L-glutamate) similar to wild-type, IC50 (L-arginine) 875fold increased compared to wild-type
H268N/H26E/E19R
-
Km and kcat (N-acetyl-L-glutamate) similar to wild-type, IC50 (L-arginine) 1960fold increased compared to wild-type
M31V
site-directed mutagenesis, the mutation deregulates the feedback inhibition of the enzyme
R209A
site-directed mutagenesis, the mutant strain shows accumulation of large amounts of pathway intermediates L-citrulline and L-ornithine and decreased production of L-arginine. Transcription levels of argGH decrease accompanied with the reduction of argininosuccinase activity, which leads to the metabolic obstacle from L-citrulline to L-arginine; site-directed mutagenesis, the mutation increases the 50% inhibitoryL--arginine concentration significantly in vitro, which deregulates the feedback inhibition of CcNAGK by L-arginine in SYPA5-5 during the fermentation
H268N
-
site-directed mutagenesis, the mutant strain shows accumulation of large amounts of pathway intermediates L-citrulline and L-ornithine and decreased production of L-arginine. Transcription levels of argGH decrease accompanied with the reduction of argininosuccinate synthase activity, which leads to the metabolic obstacle from L-citrulline to L-arginine; site-directed mutagenesis, the mutation increases the 50% inhibitoryL--arginine concentration significantly in vitro, which deregulates the feedback inhibition of CcNAGK by L-arginine in SYPA5-5 during the fermentation
-
R209A
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site-directed mutagenesis, the mutant strain shows accumulation of large amounts of pathway intermediates L-citrulline and L-ornithine and decreased production of L-arginine. Transcription levels of argGH decrease accompanied with the reduction of argininosuccinase activity, which leads to the metabolic obstacle from L-citrulline to L-arginine; site-directed mutagenesis, the mutation increases the 50% inhibitoryL--arginine concentration significantly in vitro, which deregulates the feedback inhibition of CcNAGK by L-arginine in SYPA5-5 during the fermentation
-
DELTA2-15
-
Km (N-acetyl-L-glutamate) increased compared to wild-type, kcat decreased compared to wild-type, IC50 (L-arginine) 71fold increased compared to wild-type
DELTA2-19
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Km (N-acetyl-L-glutamate) increased compared to wild-type, kcat decreased compared to wild-type, IC50 (L-arginine) 148fold increased compared to wild-type
DELTA2-29
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Km (N-acetyl-L-glutamate) increased compared to wild-type, kcat decreased compared to wild-type, IC50 (L-arginine) 163fold increased compared to wild-type
DELTA25
-
Km (N-acetyl-L-glutamate) highly increased compared to wild-type, kcat highly decreased compared to wild-type, IC50 (L-arginine) 17fold increased compared to wild-type
DELTA8
-
Km (N-acetyl-L-glutamate) increased compared to wild-type, kcat highly decreased compared to wild-type, IC50 (L-arginine) 16fold increased compared to wild-type
E19A
-
Km (N-acetyl-L-glutamate) similar to wild-type, kcat similar to wild-type, IC50 (L-arginine) 40fold increased compared to wild-type
E19R
-
Km (N-acetyl-L-glutamate) similar to wild-type, kcat similar to wild-type, IC50 (L-arginine) 61fold increased compared to wild-type
E281A
-
Km (N-acetyl-L-glutamate) highly increased compared to wild-type, kcat similar to wild-type, IC50 (L-arginine) 21fold increased compared to wild-type
G287A
-
Km (N-acetyl-L-glutamate) similar to wild-type, kcat decreased compared to wild-type, IC50 (L-arginine) 37fold increased compared to wild-type
G287D
-
Km (N-acetyl-L-glutamate) similar to wild-type, kcat similar to wild-type, IC50 (L-arginine) 40fold increased compared to wild-type
H268A
-
Km (N-acetyl-L-glutamate) similar to wild-type, kcat similar to wild-type, IC50 (L-arginine) 39fold increased compared to wild-type
H268N
-
Km (N-acetyl-L-glutamate) similar to wild-type, kcat similar to wild-type, IC50 (L-arginine) 58fold increased compared to wild-type
H26A
-
Km (N-acetyl-L-glutamate) similar to wild-type, kcat similar to wild-type, IC50 (L-arginine) 54fold increased compared to wild-type
R209A
-
Km (N-acetyl-L-glutamate) similar to wild-type, kcat similar to wild-type, IC50 (L-arginine) 46fold increased compared to wild-type
R209K
-
Km (N-acetyl-L-glutamate) similar to wild-type, kcat similar to wild-type, IC50 (L-arginine) 37fold increased compared to wild-type
W23A
-
Km (N-acetyl-L-glutamate) similar to wild-type, kcat similar to wild-type, IC50 (L-arginine) 4.5fold increased compared to wild-type
D162E
-
about 0.1% of wild-type activity
G11A
C6EE50
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
K8R
-
substantial although diminished activity
N158K
-
substantial although diminished activity
R66K
-
substantial although diminished activity
I106M
-
to increase phasing power, three additional amino acids codons are mutated to methionine (I106M, I294M and L367M). Crystals from this mutant protein are diffracted to 2.7 A
I294M
-
to increase phasing power, three additional amino acids codons are mutated to methionine (I106M, I294M and L367M). Crystals from this mutant protein are diffracted to 2.7 A
K356H
site-directed mutagenesis, inactive mutant
L367M
-
to increase phasing power, three additional amino acids codons are mutated to methionine (I106M, I294M and L367M). Crystals from this mutant protein are diffracted to 2.7 A
N391Q
site-directed mutagenesis, inactive mutant
R386K
site-directed mutagenesis, inactive mutant
S387A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y397F
site-directed mutagenesis, inactive mutant
E17A
-
site-directed mutagenesis, the mutant shows reduced Vmax, the mutation results in decreased affinity of NAGK for arginine
E17D
-
site-directed mutagenesis, the mutant shows reduced Vmax, the mutation results in decreased affinity of NAGK for arginine
E17Q
-
site-directed mutagenesis, the mutant shows reduced Vmax, the mutation results in decreased affinity of NAGK for arginine
E284D
-
site-directed mutagenesis, the mutant shows reduced Vmax and altered Km for the substrates
G290A
-
site-directed mutagenesis, the mutant shows reduced Vmax and altered Km for the substrates
H271N
-
site-directed mutagenesis, the mutant shows reduced Vmax and altered Km for the substrates
K213
-
site-directed mutagenesis, the mutant shows reduced Vmax and altered Km for the substrates
Q10A
-
site-directed mutagenesis, the mutant shows reduced Vmax and altered Km for the substrates
R24E
-
site-directed mutagenesis, the mutant shows reduced Vmax , the mutation results in increased affinity of NAGK for arginine
Y21A
-
site-directed mutagenesis, the mutant shows reduced Vmax and altered Km for the substrates
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
R233A
-
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
E186A/E387A
-
to improve resolution in crystallization
E416A/K417A
-
to improve resolution in crystallization
E94A/K95A
-
to improve resolution in crystallization
K26A/E27A
-
to improve resolution in crystallization
K279A/E280A
-
to improve resolution in crystallization
K364H
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
K419A
-
to improve resolution in crystallization
N399Q
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
R394K
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
S395A
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
Y405F
site-directed mutagenesis, inactive mutant
K364H
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
-
N399Q
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
-
R394K
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
-
S395A
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
-
Y405F
-
site-directed mutagenesis, inactive mutant
-
additional information
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