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2.3.1.1: amino-acid N-acetyltransferase

This is an abbreviated version!
For detailed information about amino-acid N-acetyltransferase, go to the full flat file.

Word Map on EC 2.3.1.1

Reaction

acetyl-CoA
+
L-glutamate
=
CoA
 +
N-acetyl-L-glutamate

Synonyms

acetylglutamate synthase, acetylglutamate synthetase, acetylglutamic synthetase, acetyltransferase, amino acid, AGAS, amino acid acetyltransferase, ARG2, ArgA, ArgH(A), argJ, Cg3035, More, N-acetyl-glutamate synthase, N-acetyl-L-glutamate synthase, N-acetyl-L-glutamate synthase/kinase, N-acetyl-L-glutamate synthetase, N-acetylglutamate synthase, N-acetylglutamate synthase/kinase, N-acetylglutamate synthetase, NAGS, NAGS-K, NAGS/K, NAT, ngNAGS, PaNAGS, pitax, Rv2747, SINAGS1, XcNAGS

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.1 Transferring groups other than aminoacyl groups
                2.3.1.1 amino-acid N-acetyltransferase

Inhibitors

Inhibitors on EC 2.3.1.1 - amino-acid N-acetyltransferase

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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,3-diaminopropane
-
10 mM, 88% inhibition in the presence of 0.5 mM N-acetyl-L-glutamate
3-methylcrotonyl-CoA
-
about 45% residual activity at 2.5 mM
5,5'-dithiobis(2-nitrobenzoate)
-
strong inhibition
acetyl-CoA
AgNO3
-
0.1 mM, 70-90% inhibition
arginine
BaCl2
-
1 mM, 30-50% inhibition
butyryl-CoA
-
about 30% residual activity at 2.5 mM
CaCl2
-
1 mM, 30-50% inhibition
cadaverine
-
10 mM, 80% inhibition in the presence of 0.5 mM N-acetyl-L-glutamate
Cd2+
-
0.1 mM, 94% inhibition
CoA
-
50% activity reduction at 2.5 mM
CoCl2
-
0.1 mM, 30-50% inhibition
coenzyme A
EDTA
-
weak inhibition
FeCl3
-
0.1 mM, 30-50% inhibition
FeSO4
-
0.1 mM, 30-50% inhibition
glutaryl-CoA
-
about 50% residual activity at 2.5 mM
high ionic strength
-
isobutylmethylxanthine
-
and other oxypurines containing a 2,6-dione group interfere with the binding of glutamate to the active site of N-acetylglutamate synthetase, thereby decreasing synthesis of N-acetylglutamate, resulting in reduction of citrulline and urea synthesis. Isobutylmethylxanthine significantly increases the apparent Km for glutamate and decreases velocity of N-acetylglutamate synthetase, with little effect on carbamoylphosphate synthase-1. Inhibition is reversed by supplementation with N-carbamylglutamate
isobutyryl-CoA
-
about 45% residual activity at 2.5 mM
isovaleryl-CoA
-
about 50% residual activity at 2.5 mM
L-alpha-Acetoxylglutamate
-
2 mM, 17% inhibition
L-arginine
L-citrulline
-
10 mM, 75% inhibition
L-glutamate
-
-
L-glutamine
-
substrate inhibition
L-Indospicine
-
0.2 mM; 50% inhibition
methylmalonyl-CoA
-
about 40% residual activity at 2.5 mM
MgCl2
-
1 mM, 30-50% inhibition
MnCl2
-
0.1 mM, 30-50% inhibition
N-acetyl-D-glutamate
-
2 mM, 30% inhibition
N-acetyl-DL-alpha-aminoadipate
-
2 mM, 78% inhibition
N-acetyl-L-aspartate
-
2 mM, 25% inhibition
N-acetyl-L-glutamate
N-acetyl-L-glutamine
-
2 mM, 46% inhibition
N-acetylglutamate
N-benzoyl-L-glutamate
-
2 mM, 29% inhibition
N-Butyryl-L-glutamate
-
2 mM, 19% inhibition
N-carbamoyl-L-glutamate
-
2 mM, 31% inhibition
N-ethylmaleimide
-
-
N-propionyl-L-glutamate
-
2 mM, 63% inhibition
NaCl
-
200 mM NaCl inhibits the activity by about 22%
Ni(NO3)2
-
0.1 mM, 30-50% inhibition
O-(L-Norvalyl-5)-isourea
-
0.02 mM, 50% inhibition
oxaloacetate
-
1 mM, 68% inhibition
p-chloromercuribenzoate
-
-
p-hydroxymercuribenzoate
Pb(NO3)2
-
0.1 mM, 70-90% inhibition
polyamines
-
-
-
potassium phosphate
-
-
propionyl-CoA
putrescine
-
10 mM, 74% inhibition in the presence of 0.5 mM N-acetyl-L-glutamate
Sodium acetate
-
100 mM NaCl inhibits the activity by about 22%
spermidine
-
1 mM, 78% inhibition in the presence of 0.5 mM N-acetyl-L-glutamate
spermine
-
1 mM, 88% inhibition in the presence of 0.5 mM N-acetyl-L-glutamate
succinate
-
2 mM, 21% inhibition
succinyl-CoA
-
about 60% residual activity at 2.5 mM
uric acid
-
significantly increases the apparent Km for glutamate and decreases velocity of N-acetylglutamate synthetase, with little effect on carbamoylphosphate synthase-1. Inhibition is reversed by supplementation with N-carbamylglutamate
xanthine
-
significantly increases the apparent Km for glutamate and decreases velocity of N-acetylglutamate synthetase, with little effect on carbamoylphosphate synthase-1. Inhibition is reversed by supplementation with N-carbamylglutamate
additional information
-