Acetylglutamate kinase
Class of enzymes
From Wikipedia, the free encyclopedia
Acetylglutamate kinase (EC 2.7.2.8) is an enzyme that catalyzes the chemical reaction:
-N-Acetylglutamic_acid.svg)
The enzyme characterised from the bacterium, Escherichia coli and the green algae, Chlamydomonas reinhardti, converts N-acetyl-L-glutamic acid to N-acetyl-L-γ-glutamyl phosphate by transferring a phosphate group from the cofactor, adenosine triphosphate (ATP), which is converted to adenosine diphosphate (ADP). The reaction is part of the biosynthesis of arginine.[1][2]
This enzyme is a transferase, specifically one transferring phosphorus-containing groups (phosphotransferases) with a carboxy group as acceptor.[3]
Nomenclature
The systematic name of this enzyme class is ATP:N-acetyl-L-glutamate 5-phosphotransferase. Other names in common use include:[4]
- N-acetylglutamate 5-phosphotransferase,
- acetylglutamate phosphokinase,
- N-acetylglutamate phosphokinase,
- N-acetylglutamate kinase, and
- N-acetylglutamic 5-phosphotransferase.
