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amidase

   Also found in: Encyclopedia 0.01 sec.
amidase /am·i·dase/ (am´ĭ-dās)
1. any of a group of enzymes that catalyze the cleavage of carbon–nitrogen bonds in amides.
2. an enzyme that catalyzes the cleavage of the carbon–nitrogen bond of a monocarboxylic acid amide to form a monocarboxylic acid and ammonia.

am·i·dase (m-ds, -dz)
n.
An enzyme that catalyzes the hydrolysis of monocarboxylic amides, thus freeing ammonia. Also called acylamidase, acylase.

amidase
[am′i·dās]
1 an enzyme that catalyzes the formation of a monocarboxylic acid and ammonia by hydrolytic cleavage of the C─N bond of a monocarboxylic acid amide.
2 a term used in the recommended and trivial names of some hydrolases acting on amides, particularly those acting on linear amides.


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Also, they found that PEA - also present in foods like eggs and peanuts - is deactivated by a protein called N-acylethanolamine-hydrolyzing acid amidase, which is an enzyme that breaks down molecules controlling cell inflammation.
Amidase activity The procedure measures the enzymatic hydrolysis of BAPNA substrate following incubation with enzyme between 5 and 60 min at 37[degree]C, as described by Gravina de Moraes et al.
This suggests that any CDEPA or CMEPA produced in this time was either not being metabolized to the corresponding aniline by the aryl amidase or metabolized so slowly as to preclude detection.
 
 
 
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