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Literature summary extracted from

  • Masson, P.; Froment, M.T.; Darvesh, S.; Schopfer, L.M.; Lockridge, O.
    Aryl acylamidase activity of human serum albumin with o-nitrotrifluoroacetanilide as the substrate (2007), J. Enzyme Inhib. Med. Chem., 22, 463-469.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.5.1.13 fatty acid fatty acids block aryl acylamidase activity competing with amides for binding in the catalytic domain Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.1.13 0.67
-
o-nitrotrifluoroacetanilide assays performed at high albumin concentrations, spectrophotometric assay Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.13 Homo sapiens
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.5.1.13 serum
-
Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.13 o-nitrotrifluoroacetanilide + H2O reaction is performed by human serum albumin, substrate is more reactive than o-nitroacetanilide Homo sapiens o-nitroaniline + trifluoroacetic acid
-
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Synonyms

EC Number Synonyms Comment Organism
3.5.1.13 aryl acylamidase
-
Homo sapiens