Structure-function relationships of glutamine synthetases.
As a highly regulated enzyme at the core of nitrogen metabolism, glutamine synthetase has been studied intensively. We review structural and functional studies of both bacterial and eukaryotic glutamine synthetases, with emphasis on enzymatic inhibitors.
Eisenberg
D
D
UCLA-DOE Laboratory of Structural Biology and Molecular Medicine, Departments of Chemistry, Biochemistry and Biological Chemistry, University of California, Los Angeles, 201 MBI, Box 951570, Los Angeles, CA 90095-1570, USA. david@mbi.ucla.edu
Gill
H S
HS
Pfluegl
G M
GM
Rotstein
S H
SH
D000595:Amino Acid Sequence; D000818:Animals; D001419:Bacteria; D001665:Binding Sites; D002384:Catalysis; D004791:Enzyme Inhibitors / Q000737:chemistry*; D005057:Eukaryotic Cells; D005786:Gene Expression Regulation; D005974:Glutamate-Ammonia Ligase / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D008969:Molecular Sequence Data; D010944:Plants; D016415:Sequence Alignment; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
D004791:Enzyme Inhibitors; D005974:Glutamate-Ammonia Ligase