Multiple control of N-acetylglutamate synthetase from Pseudomonas aeruginosa: synergistic inhibition by acetylglutamate and polyamines.

Details

Serval ID
serval:BIB_E8A613BC0217
Type
Article: article from journal or magazin.
Collection
Publications
Title
Multiple control of N-acetylglutamate synthetase from Pseudomonas aeruginosa: synergistic inhibition by acetylglutamate and polyamines.
Journal
Biochemical and Biophysical Research Communications
Author(s)
Haas D., Leisinger T.
ISSN
0006-291X (Print)
ISSN-L
0006-291X
Publication state
Published
Issued date
1974
Volume
60
Number
1
Pages
42-47
Language
english
Abstract
N-Acetylglutamate synthetase (EC 2.3.1.1), the first enzyme of arginine synthesis was shown to be under multiple control by the reaction products and the endproducts of the pathway in tenfold purified extracts from . Synergistic inhibition of the enzyme was exerted by N-acetyl-L-glutamate and polyamines. At 0.5 mM N-acetyl-L-glutamate spermine was the most potent inhibitor, whereas spermidine, cadaverine and putrescine inhibited the enzyme to a lesser extent. Furthermore, feedback-inhibition by L-arginine was enhanced synergistically by N-acetyl-L-glutamate and CoA.
Keywords
Acetyl Coenzyme A, Acetyltransferases/antagonists & inhibitors, Arginine/pharmacology, Cadaverine/pharmacology, Carbon Radioisotopes, Coenzyme A, Diamines/pharmacology, Drug Synergism, Glutamates/pharmacology, Kinetics, Polyamines/pharmacology, Propane/analogs & derivatives, Propane/pharmacology, Pseudomonas aeruginosa/drug effects, Pseudomonas aeruginosa/enzymology, Putrescine/pharmacology, Spermidine/pharmacology, Spermine/pharmacology
Pubmed
Web of science
Create date
25/01/2008 17:01
Last modification date
20/08/2019 16:11
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