Description
In enzymology, an aminoacylase (EC 3.5.1.14) is an enzyme that catalyzes the chemical reaction:N-acyl-L-amino acid + H2O↔ carboxylate + L-amino acid. Thus, the two substRates of this enzyme are N-acyl-L-amino acid and H2O, whereas its two products are carboxylate and L-amino acid. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. This enzyme participates in urea cycle and metabolism of amino groups.
Abbr
ACY1, Native (Aspergillus melleus)
Source
Aspergillus melleus
Product Overview
Enzyme activity: the optimum temperature is 40-45 oc, the optimum pH is 8.0 (stable form pH 6-10). The enzyme is activated by CoCl2 in the range of 10-4 to 10-3 M.
Enzyme Commission Number
EC 3.5.1.14
Unit Definition
1 U corresponds to the amount of enzyme which hydrolyzes 1 μmol N-acetyl-L-methionine per minute at pH 8.0 and 37°C
Synonyms
aminoacylase 1; aminoacylase I; dehydropeptidase II; histozyme; hippuricase; benzamidase; acylase I; hippurase; amido acid deacylase; L-aminoacylase; acylase; aminoacylase; L-amino-acid acylase; α-N-acylaminoacid hydrolase; long acyl amidoacylase; short acyl amidoacylase; ACY1 (gene name); N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14; 9012-37-7
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