Structure-function relationships of glutamine synthetases

D Eisenberg; H S Gill; G M Pfluegl; S H Rotstein

doi:10.1016/s0167-4838(99)00270-8

Structure-function relationships of glutamine synthetases

Biochim Biophys Acta. 2000 Mar 7;1477(1-2):122-45. doi: 10.1016/s0167-4838(99)00270-8.

Authors

D Eisenberg¹, H S Gill, G M Pfluegl, S H Rotstein

Affiliation

¹ 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

PMID: 10708854
DOI: 10.1016/s0167-4838(99)00270-8

Abstract

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.

Publication types

Comparative Study
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review

MeSH terms

Amino Acid Sequence
Animals
Bacteria
Binding Sites
Catalysis
Enzyme Inhibitors / chemistry*
Eukaryotic Cells
Gene Expression Regulation
Glutamate-Ammonia Ligase / antagonists & inhibitors
Glutamate-Ammonia Ligase / chemistry*
Glutamate-Ammonia Ligase / metabolism
Humans
Molecular Sequence Data
Plants
Sequence Alignment
Structure-Activity Relationship
Substrate Specificity

Substances

Enzyme Inhibitors
Glutamate-Ammonia Ligase