BRENDA - Enzyme Database
show all sequences of 2.7.2.8

Structure of N-acetyl-L-glutamate synthase/kinase from Maricaulis maris with the allosteric inhibitor L-arginine bound

Zhao, G.; Haskins, N.; Jin, Z.; M Allewell, N.; Tuchman, M.; Shi, D.; Biochem. Biophys. Res. Commun. 437, 585-590 (2013)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
recombinant His-tagged wild-type and mutant enzymes expression in Escherichia coli BL21(DE3)
Maricaulis maris
recombinant His-tagged wild-type and mutant enzymes expression in Escherichia coli BL21(DE3)
Xanthomonas campestris
Crystallization (Commentary)
Crystallization
Organism
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
Maricaulis maris
Engineering
Amino acid exchange
Commentary
Organism
K356H
site-directed mutagenesis, inactive mutant
Maricaulis maris
K364H
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
Xanthomonas campestris
N391Q
site-directed mutagenesis, inactive mutant
Maricaulis maris
N399Q
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
Xanthomonas campestris
R386K
site-directed mutagenesis, inactive mutant
Maricaulis maris
R394K
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
Xanthomonas campestris
S387A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Maricaulis maris
S395A
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
Xanthomonas campestris
Y397F
site-directed mutagenesis, inactive mutant
Maricaulis maris
Y405F
site-directed mutagenesis, inactive mutant
Xanthomonas campestris
Inhibitors
Inhibitors
Commentary
Organism
Structure
L-arginine
an allosteric inhibitor of mmNAGS/K, mechanism of allosteric inhibition of mmNAGS/K by L-arginine. L-Arginine is an allosteric inhibitor of NAGS/K but an allosteric activator of mammalian NAGS. 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. In this conformation, the AcCoA binding site in the N-acetyltransferase domain is blocked by a loop from the amino acid kinase domain, as a result of a domain rotation that occurs when L-arginine binds
Maricaulis maris
trichloroacetic acid
complete inactivation at 30%
Maricaulis maris
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mg2+
required
Maricaulis maris
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ATP + N-acetyl-L-glutamate
Maricaulis maris
-
ADP + N-acetyl-L-glutamyl 5-phosphate
-
-
r
ATP + N-acetyl-L-glutamate
Xanthomonas campestris
-
ADP + N-acetyl-L-glutamyl 5-phosphate
-
-
r
ATP + N-acetyl-L-glutamate
Maricaulis maris MCS10
-
ADP + N-acetyl-L-glutamyl 5-phosphate
-
-
r
ATP + N-acetyl-L-glutamate
Xanthomonas campestris 8004
-
ADP + N-acetyl-L-glutamyl 5-phosphate
-
-
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Maricaulis maris
Q0ASS9
-
-
Maricaulis maris MCS10
Q0ASS9
-
-
Xanthomonas campestris
A0A0H2X8L7
pv. campestris
-
Xanthomonas campestris 8004
A0A0H2X8L7
pv. campestris
-
Purification (Commentary)
Commentary
Organism
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli BL21(DE3) by nickel affinity chromatography
Maricaulis maris
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli BL21(DE3) by nickel affinity chromatography
Xanthomonas campestris
Reaction
Reaction
Commentary
Organism
ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate
allosterically regulated mechanism for the enzyme from Maricaulis maris with roles for Lys356, Arg386, Asn391 and Tyr397 in the catalytic mechanism
Maricaulis maris
Specific Activity [micromol/min/mg]
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
0.47
-
purified mutant K364H enzyme, pH 8.5, 30C
Xanthomonas campestris
1.66
-
purified mutant R394K enzyme, pH 8.5, 30C
Xanthomonas campestris
3.11
-
purified mutant N399Q enzyme, pH 8.5, 30C
Xanthomonas campestris
4.97
-
purified mutant S387A enzyme, pH 8.5, 30C
Maricaulis maris
6.81
-
purified recominant wild-type enzyme, pH 8.5, 30C
Maricaulis maris
39.87
-
purified mutant S387A enzyme, pH 8.5, 30C
Xanthomonas campestris
44.05
-
purified recominant wild-type enzyme, pH 8.5, 30C
Xanthomonas campestris
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + N-acetyl-L-glutamate
-
735596
Maricaulis maris
ADP + N-acetyl-L-glutamyl 5-phosphate
-
-
-
r
ATP + N-acetyl-L-glutamate
-
735596
Xanthomonas campestris
ADP + N-acetyl-L-glutamyl 5-phosphate
-
-
-
r
ATP + N-acetyl-L-glutamate
-
735596
Maricaulis maris MCS10
ADP + N-acetyl-L-glutamyl 5-phosphate
-
-
-
r
ATP + N-acetyl-L-glutamate
-
735596
Xanthomonas campestris 8004
ADP + N-acetyl-L-glutamyl 5-phosphate
-
-
-
r
additional information
residues Lys364, Arg394 and Asn399 in xcNAGS/K are involved in binding of L-glutamate
735596
Xanthomonas campestris
?
-
-
-
-
additional information
residues Lys364, Arg394 and Asn399 in xcNAGS/K are involved in binding of L-glutamate
735596
Xanthomonas campestris 8004
?
-
-
-
-
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
-
assay at
Maricaulis maris
30
-
assay at
Xanthomonas campestris
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.5
-
assay at
Maricaulis maris
8.5
-
assay at
Xanthomonas campestris
Cofactor
Cofactor
Commentary
Organism
Structure
ATP
-
Maricaulis maris
ATP
-
Xanthomonas campestris
Cloned(Commentary) (protein specific)
Commentary
Organism
recombinant His-tagged wild-type and mutant enzymes expression in Escherichia coli BL21(DE3)
Maricaulis maris
recombinant His-tagged wild-type and mutant enzymes expression in Escherichia coli BL21(DE3)
Xanthomonas campestris
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
ATP
-
Maricaulis maris
ATP
-
Xanthomonas campestris
Crystallization (Commentary) (protein specific)
Crystallization
Organism
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
Maricaulis maris
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
K356H
site-directed mutagenesis, inactive mutant
Maricaulis maris
K364H
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
Xanthomonas campestris
N391Q
site-directed mutagenesis, inactive mutant
Maricaulis maris
N399Q
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
Xanthomonas campestris
R386K
site-directed mutagenesis, inactive mutant
Maricaulis maris
R394K
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
Xanthomonas campestris
S387A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Maricaulis maris
S395A
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
Xanthomonas campestris
Y397F
site-directed mutagenesis, inactive mutant
Maricaulis maris
Y405F
site-directed mutagenesis, inactive mutant
Xanthomonas campestris
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
L-arginine
an allosteric inhibitor of mmNAGS/K, mechanism of allosteric inhibition of mmNAGS/K by L-arginine. L-Arginine is an allosteric inhibitor of NAGS/K but an allosteric activator of mammalian NAGS. 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. In this conformation, the AcCoA binding site in the N-acetyltransferase domain is blocked by a loop from the amino acid kinase domain, as a result of a domain rotation that occurs when L-arginine binds
Maricaulis maris
trichloroacetic acid
complete inactivation at 30%
Maricaulis maris
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mg2+
required
Maricaulis maris
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ATP + N-acetyl-L-glutamate
Maricaulis maris
-
ADP + N-acetyl-L-glutamyl 5-phosphate
-
-
r
ATP + N-acetyl-L-glutamate
Xanthomonas campestris
-
ADP + N-acetyl-L-glutamyl 5-phosphate
-
-
r
ATP + N-acetyl-L-glutamate
Maricaulis maris MCS10
-
ADP + N-acetyl-L-glutamyl 5-phosphate
-
-
r
ATP + N-acetyl-L-glutamate
Xanthomonas campestris 8004
-
ADP + N-acetyl-L-glutamyl 5-phosphate
-
-
r
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli BL21(DE3) by nickel affinity chromatography
Maricaulis maris
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli BL21(DE3) by nickel affinity chromatography
Xanthomonas campestris
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
0.47
-
purified mutant K364H enzyme, pH 8.5, 30C
Xanthomonas campestris
1.66
-
purified mutant R394K enzyme, pH 8.5, 30C
Xanthomonas campestris
3.11
-
purified mutant N399Q enzyme, pH 8.5, 30C
Xanthomonas campestris
4.97
-
purified mutant S387A enzyme, pH 8.5, 30C
Maricaulis maris
6.81
-
purified recominant wild-type enzyme, pH 8.5, 30C
Maricaulis maris
39.87
-
purified mutant S387A enzyme, pH 8.5, 30C
Xanthomonas campestris
44.05
-
purified recominant wild-type enzyme, pH 8.5, 30C
Xanthomonas campestris
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + N-acetyl-L-glutamate
-
735596
Maricaulis maris
ADP + N-acetyl-L-glutamyl 5-phosphate
-
-
-
r
ATP + N-acetyl-L-glutamate
-
735596
Xanthomonas campestris
ADP + N-acetyl-L-glutamyl 5-phosphate
-
-
-
r
ATP + N-acetyl-L-glutamate
-
735596
Maricaulis maris MCS10
ADP + N-acetyl-L-glutamyl 5-phosphate
-
-
-
r
ATP + N-acetyl-L-glutamate
-
735596
Xanthomonas campestris 8004
ADP + N-acetyl-L-glutamyl 5-phosphate
-
-
-
r
additional information
residues Lys364, Arg394 and Asn399 in xcNAGS/K are involved in binding of L-glutamate
735596
Xanthomonas campestris
?
-
-
-
-
additional information
residues Lys364, Arg394 and Asn399 in xcNAGS/K are involved in binding of L-glutamate
735596
Xanthomonas campestris 8004
?
-
-
-
-
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
-
assay at
Maricaulis maris
30
-
assay at
Xanthomonas campestris
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.5
-
assay at
Maricaulis maris
8.5
-
assay at
Xanthomonas campestris
General Information
General Information
Commentary
Organism
evolution
the allosterically regulated mechanism for mmNAGS/K differs significantly from that for Neisseria gonorrhoeae NAGS. L-Arginine is an allosteric inhibitor of NAGS/K but an allosteric activator of mammalian NAGS
Maricaulis maris
metabolism
N-acetylglutamate synthase/kinase catalyzes the first two steps in L-arginine biosynthesis. The synthase activity of mmNAGS/K is allosterically regulated by L-arginine
Maricaulis maris
metabolism
N-acetylglutamate synthase/kinase catalyzes the first two steps in L-arginine biosynthesis
Xanthomonas campestris
General Information (protein specific)
General Information
Commentary
Organism
evolution
the allosterically regulated mechanism for mmNAGS/K differs significantly from that for Neisseria gonorrhoeae NAGS. L-Arginine is an allosteric inhibitor of NAGS/K but an allosteric activator of mammalian NAGS
Maricaulis maris
metabolism
N-acetylglutamate synthase/kinase catalyzes the first two steps in L-arginine biosynthesis. The synthase activity of mmNAGS/K is allosterically regulated by L-arginine
Maricaulis maris
metabolism
N-acetylglutamate synthase/kinase catalyzes the first two steps in L-arginine biosynthesis
Xanthomonas campestris
Other publictions for EC 2.7.2.8
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
738801
Zhao
Controlling the transcription ...
Corynebacterium crenatum, Corynebacterium crenatum SYPA5-5
J. Ind. Microbiol. Biotechnol.
43
55-66
2016
-
-
1
-
8
-
1
-
-
1
-
2
-
4
-
-
-
-
-
-
-
-
2
-
1
-
-
-
1
-
-
1
-
-
-
-
-
1
1
-
8
-
-
1
-
-
-
1
-
2
-
-
-
-
-
-
-
-
2
-
1
-
-
-
1
-
-
-
-
1
1
-
-
-
735596
Zhao
Structure of N-acetyl-L-glutam ...
Maricaulis maris, Maricaulis maris MCS10, Xanthomonas campestris, Xanthomonas campestris 8004
Biochem. Biophys. Res. Commun.
437
585-590
2013
-
-
2
1
10
-
2
-
-
1
-
4
-
7
-
-
2
1
-
-
7
-
6
-
2
-
-
-
2
-
-
2
-
-
-
-
-
2
2
1
10
-
-
2
-
-
-
1
-
4
-
-
-
2
-
-
7
-
6
-
2
-
-
-
2
-
-
-
-
3
3
-
-
-
721268
Xu
Site-directed mutagenesis and ...
Corynebacterium crenatum
Amino Acids
43
255-266
2012
-
-
1
-
5
-
1
5
-
-
1
-
-
1
-
-
-
-
-
-
-
-
1
-
1
-
-
12
1
-
-
-
-
-
6
-
-
1
-
-
5
-
6
1
-
5
-
-
1
-
-
-
-
-
-
-
-
-
1
-
1
-
-
12
1
-
-
-
-
1
1
-
-
-
722087
Xu
Site-directed mutagenesis stud ...
Corynebacterium glutamicum
Curr. Microbiol.
64
164-172
2012
-
-
1
-
16
-
1
17
-
-
1
-
-
2
-
-
1
-
-
-
-
-
1
-
-
-
-
32
-
-
-
-
-
-
17
-
-
1
-
-
16
-
17
1
-
17
-
-
1
-
-
-
-
1
-
-
-
-
1
-
-
-
-
32
-
-
-
-
-
-
-
-
-
-
723557
de Cima
Insight on an arginine synthes ...
Saccharomyces cerevisiae
PLoS ONE
7
e34734
2012
-
-
1
1
1
-
1
4
-
-
-
-
-
4
-
-
1
-
-
-
-
-
1
1
1
-
-
4
-
-
-
-
1
-
2
-
-
1
-
1
1
-
2
1
1
4
-
-
-
-
-
-
-
1
-
-
-
-
1
1
1
-
-
4
-
-
-
-
-
-
-
-
-
-
720845
Shi
A novel N-acetylglutamate synt ...
Maricaulis maris
PLoS ONE
6
e28825
2011
1
-
1
1
3
-
-
-
-
-
-
-
-
7
-
-
1
-
-
-
1
-
1
1
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
1
3
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
723511
Marcos
Changes in dynamics upon oligo ...
Escherichia coli
PLoS Comput. Biol.
7(9)
e1002201
2011
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
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1
-
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
722963
Fokina
A novel signal transduction pr ...
Synechococcus elongatus
J. Mol. Biol.
399
410-421
2010
-
-
-
-
1
-
-
-
-
-
-
1
-
7
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
722965
Gil-Ortiz
Two crystal structures of Esch ...
Escherichia coli
J. Mol. Biol.
399
476-490
2010
-
-
-
1
1
-
-
4
-
-
-
-
-
2
-
-
-
-
-
-
-
-
1
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
1
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
702066
Feria Bourrellier
Metabolite regulation of the i ...
Arabidopsis thaliana
Biochem. Biophys. Res. Commun.
387
700-704
2009
-
-
1
-
-
-
-
-
1
1
1
1
-
3
-
-
1
-
-
-
-
-
2
1
-
-
-
-
-
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