N-acetylglutamate synthetase of Pseudomonas aeruginosa. An assay in vitro and feedback inhibition by arginine.

Details

Serval ID
serval:BIB_EB76AA80F727
Type
Article: article from journal or magazin.
Collection
Publications
Title
N-acetylglutamate synthetase of Pseudomonas aeruginosa. An assay in vitro and feedback inhibition by arginine.
Journal
European Journal of Biochemistry
Author(s)
Haas D., Kurer V., Leisinger T.
ISSN
0014-2956 (Print)
ISSN-L
0014-2956
Publication state
Published
Issued date
1972
Volume
31
Number
2
Pages
290-295
Language
english
Abstract
1 N-Acetylglutamate synthetase (acetyl-CoA: l-glutamate N-acetyltransferase), the first enzyme of arginine biosynthesis, has been detected in extracts from Pseudomonas aeruginosa by a specific and sensitive assay in vitro.
2 The enzyme, partially purified by chromatography on hydroxyapatite, was dependent on l-glutamate and acetyl-CoA. l-Aspartate could not replace l-glutamate as a substrate; acetyl phosphate and N2-acetyl-l-ornithine were not utilized as acetyl donors.
3 The enzyme was inhibited by l-arginine (approx. 50% inhibition by 0.1 mM l-arginine). N2-Acetyl-l-ornithine, l-ornithine, and l-citrulline were not effective as inhibitors. Since N-acetylglutamate 5-phosphotransferase of P. aeruginosa is known to be inhibited by arginine, the first and the second enzymes of arginine synthesis in this organism are subject to feedback inhibition by the end-product.
4 Arginine did not repress the formation of N- acetylglutamate synthetase.
Keywords
Acetyltransferases/antagonists & inhibitors, Acetyltransferases/biosynthesis, Arginine/biosynthesis, Carbon Isotopes, Chromatography, Ion Exchange, Coenzyme A, Enzyme Repression, Feedback, Glutamates, Ornithine, Pseudomonas aeruginosa/enzymology
Pubmed
Web of science
Open Access
Yes
Create date
25/01/2008 17:00
Last modification date
20/08/2019 16:13
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