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Literature summary for 2.3.1.192 extracted from

  • Kelley, M.; Vessey, D.A.
    Characterization of the acyl-CoA:amino acid N-acyltransferases from primate liver mitochondria (1994), J. Biochem. Toxicol., 9, 153-158.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
KCl 80 mM KC1, ca. 30% inhibition, inhibition is seen at all concentrations of glutamine up to 150 mM Homo sapiens
additional information human enzyme is insensitive to salts Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
120
-
L-glutamine pH 8.0, 30°C Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
Homo sapiens 5739
-

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
partial Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1-naphtylacetyl-CoA + L-glutamine 3-5% of the rate with phenacetyl-CoA Homo sapiens ? + CoA
-
?
indoleacetyl-CoA + L-glutamine 3-5% of the rate with phenacetyl-CoA Homo sapiens ? + CoA
-
?
additional information glycination of phenylacetyl-CoA by human phenacetyltransferase can only be detected at a concentration of glycine above 50 mM, and the rates are below 2% of the rate of glutamination Homo sapiens ?
-
?
phenylacetyl-CoA + L-glutamine may substitue for glycine, but at lower rate Homo sapiens phenylacetyl-L-glutamine + CoA
-
?

Synonyms

Synonyms Comment Organism
AAC
-
Homo sapiens