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Arginine activation of N ‐acetylglutamate synthetase in mouse liver
Author(s) -
Kawamoto Susumu,
Tatibana Masamiti
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80355-x
Subject(s) - cycloheximide , arginine , puromycin , biochemistry , enzyme , biology , allosteric regulation , protein biosynthesis , amino acid , activator (genetics) , aurintricarboxylic acid , dactinomycin , chemistry , microbiology and biotechnology , apoptosis , programmed cell death , gene
N ‐Acetyl‐L‐glutamate sythetase catalyzes the synthesis of N ‐acetyl‐L‐glutamate, an allosteric and esential activator of carbamoyl‐phosphate synthetase I in the liver of ureotelic animals. The enzyme is activated specifically by arginine. We report here that the sensitivity of the synthetase to activation by arginine increases markedly after intraperitoneal administration to mice of inhibitors of nucleic acid and protein synthesis, including actinomycin D, aurintricarboxylic acid, cycloheximide, emetine and puromycin. The effects of cycloheximide were investigated in detail and an amino acid analysis was made of the homogenate of freeze‐clamped livers of control or cycloheximide‐treated mice.