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Literature summary for 2.3.1.1 extracted from

  • Bachmann, C.; Krahenbuhl, S.; Colombo, J.P.
    Purification and properties of acetyl-CoA:L-glutamate N-acetyltransferase from human liver (1982), Biochem. J., 205, 123-127.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.3.1.1

Inhibitors

Inhibitors Comment Organism Structure
N-acetyl-L-glutamate
-
 Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.4
-
 acetyl-CoA
-
 Homo sapiens
8.1
-
 glutamate
-
 Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
190000
-
 gel filtration Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
ammonium sulfate, hydroxyapatite, DEAE-cellulose, Sephacryl-300 Homo sapiens

Reaction

Reaction Comment Organism Reaction ID
acetyl-CoA + L-glutamate = CoA + N-acetyl-L-glutamate rapid-equilibrium random bi bi mechanism Homo sapiens
a

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Homo sapiens
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.00286
-
-
 Homo sapiens

Storage Stability

Storage Stability Organism
-20°C, stable for 2 months Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + L-glutamate
-
 Homo sapiens CoA + N-acetyl-L-glutamate
-
 ?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
 liver enzyme, in the presence of arginine Homo sapiens

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.49
-
 N-acetyl-L-glutamate
-
 Homo sapiens