Studies of the ammonia-dependent reaction of beef pancreatic asparagine synthetase

Autor:	Sheldon M. Schuster, Craig A. Luehr, Paige M. Mehlhaff
Rok vydání:	1985
Předmět:	chemistry.chemical_classification Asparagine synthetase Kinetics Substrate (chemistry) Aspartate-Ammonia Ligase Hydroxylamine Hydroxylamines Biochemistry Ligases Ammonia chemistry.chemical_compound Enzyme chemistry Animals Cattle Asparagine Pancreas Mathematics
Zdroj:	Biochemistry. 24:1104-1110
ISSN:	1520-4995 0006-2960
Popis:	We have studied the asparagine synthetase reaction with regard to the ammonia-dependent production of asparagine. Hydroxylamine was shown to be an alternate substrate for the asparagine synthetase reaction, and some of its kinetic properties were examined. The ammonia-dependent reaction was examined with regard to inhibition by asparagine. It was found that asparagine inhibition was partial competitive with respect to ammonia, regardless of the concentration of aspartate. However, when MgATP was not saturating, the inhibition by asparagine became linear competitive. These results were interpreted to be consistent with a kinetic mechanism for asparagine synthetase where ammonia is bound to the enzyme followed by MgATP causing asparagine release.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::16114c95d31708eff7e457bab6664ee0 https://doi.org/10.1021/bi00326a006 Zobrazit plný text záznamu