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2.7.2.8: acetylglutamate kinase

This is an abbreviated version!
For detailed information about acetylglutamate kinase, go to the full flat file.

Word Map on EC 2.7.2.8

Reaction

ATP
+
N-acetyl-L-glutamate
=
ADP
+
N-acetyl-L-glutamyl 5-phosphate

Synonyms

acetylglutamate kinase, acetylglutamate phosphokinase, amino-acid acetyltransferase, argB, CcNAGK, EcNAGK, GRMZM2G132777, kinase, acetylglutamate (phosphorylating), mmNAGS/K, N-acetyl glutamate kinase, N-acetyl-glutamate 5-phosphotransferase, N-acetyl-L-glutamate 5-phosphotransferase, N-acetyl-L-glutamate kinase, N-acetyl-L-glutamate synthase/kinase, N-acetylglutamate 5-phosphotransferase, N-acetylglutamate kinase, N-acetylglutamate phosphokinase, N-acetylglutamate-5-phosphotransferase, N-acetylglutamic 5-phosphotransferase, NagK, NAGK1, NAGS-K, SYPA5-5 N-acetylglutamate kinase, xcNAGS/K, yNAGK

ECTree

     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.2 Phosphotransferases with a carboxy group as acceptor
                2.7.2.8 acetylglutamate kinase

Engineering

Engineering on EC 2.7.2.8 - acetylglutamate kinase

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PROTEIN VARIANTS
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
H268N/H26E
-
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
H268N
R209A
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
-
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
-
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
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