Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
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Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
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Enzyme
Compound
Query: EC:3.1.1.7 (
acetylcholinesterase
)
28,390
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
The effect of chemical modification on the
acetylcholinesterase
and the aryl acylamidase activities of purified
acetylcholinesterase
from electric eel and basal ganglia was investigated in the presence and absence of acetylcholine, the substrate of
acetylcholinesterase
, and 1,5-bis[4-(allyldimethylammonium)phenyl]pentan-3-one dibromide (BW284C51), a reversible competitive inhibitor of
acetylcholinesterase
. Trinitrobenzenesulfonic acid,
pyridoxal phosphate
, acetic anhydride, diethyl pyrocarbonate, and 2-hydroxy-5-nitrobenzyl bromide under specified conditions inactivated both
acetylcholinesterase
and aryl acylamidase in the absence of acetylcholine and BW284C51. Chemical modifications in the presence of acetylcholine and BW284C51 by all the above except diethyl pyrocarbonate selectively prevented the loss of
acetylcholinesterase
but not aryl acylamidase activity; modification by diethyl pyrocarbonate in the presence of acetylcholine and BW284C51 prevented the loss of both
acetylcholinesterase
and aryl acylamidase activities. Treatment with N-acetylimidazole resulted in the inactivation of
acetylcholinesterase
and the activation of aryl acylamidase. These changes in both the activities could be prevented by acetylcholine and BW284C51. Modification by phenylglyoxal, 2,4-pentanedione, or N-ethylmaleimide did not affect the enzyme activities. Indophenylacetate hydrolase activity followed a pattern similar to that of
acetylcholinesterase
in all the above modification studies. The results suggested essential lysine, tyrosine, tryptophan, and histidine residues for the active center of
acetylcholinesterase
and essential lysine, histidine, and tryptophan residues for the active center of aryl acylamidase.(ABSTRACT TRUNCATED AT 250 WORDS)
...
PMID:Chemical modification of acetylcholinesterase from eel and basal ganglia: effect on the acetylcholinesterase and aryl acylamidase activities. 638 42
