Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.5.1.13 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

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

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
serum
-
Homo sapiens
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
aryl acylamidase
-
Homo sapiens