Acetylglutamate kinase () is an enzyme that catalyzes the chemical reaction:
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.
This enzyme is a transferase, specifically one transferring phosphorus-containing groups (phosphotransferases) with a carboxy group as acceptor.
Nomenclature The systematic name of this enzyme class is ATP:N-acetyl-L-glutamate 5-phosphotransferase. Other names in common use include: N-acetylglutamate 5-phosphotransferase, acetylglutamate phosphokinase, N-acetylglutamate phosphokinase, N-acetylglutamate kinase, and N-acetylglutamic 5-phosphotransferase.
Structural studies
As of late 2007, 9 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , and .
References