N-Acetylglutamate synthase of Escherichia coli regulation of synthesis and activity by arginine.

Details

Serval ID
serval:BIB_E9D5561DEF89
Type
Article: article from journal or magazin.
Collection
Publications
Title
N-Acetylglutamate synthase of Escherichia coli regulation of synthesis and activity by arginine.
Journal
Journal of Biological Chemistry
Author(s)
Leisinger T., Haas D.
ISSN
0021-9258
Publication state
Published
Issued date
1975
Peer-reviewed
Oui
Volume
250
Number
5
Pages
1690-1693
Language
english
Abstract
N-Acetylglutamate synthase, the first enzyme of arginine biosynthesis, was stabilized in crude extracts from Escherichia coli. At 4 degrees the enzyme lost less than 5% of activity per day. L-Arginine repressed the formation of N-acetylglutamate synthase. Under conditions of genetic or physiological derepression, a specific activity of approximately 50 nmol per min per mg of protein was measured. No activity (i.e. less than 0.2 nmol per min per mg of protein) could be detected in extracts from cells grown under conditions of repression, whereas an intermediate level was found in cell cultivated on minimal medium. In a 6-fold purified preparation L-arginine inhibited the enzyme. Of 11 precursors and analogues of arginine tested only O-[L-norvalyl-5]-isourea inhibited N-acetylglutamate synthase as strongly as L-agrinine.
Keywords
Acetyl Coenzyme A, Acetyltransferases/antagonists & inhibitors, Acetyltransferases/isolation & purification, Arginine/pharmacology, Culture Media, Enzyme Repression, Escherichia coli/enzymology, Glutamates, Kinetics, Ornithine/pharmacology, Urea/analogs & derivatives, Urea/pharmacology
Pubmed
Web of science
Create date
25/01/2008 17:01
Last modification date
20/08/2019 16:12
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