CATH Classification

Domain Context

CATH Clusters

Superfamily Glutamine synthetase, N-terminal domain
Functional Family Glutamine synthetase

Enzyme Information

2.3.1.225
Protein S-acyltransferase.
based on mapping to UniProt P15104
Palmitoyl-CoA + [protein]-L-cysteine = [protein]-S-palmitoyl-L-cysteine + CoA.
-!- The enzyme catalyzes the posttranslational protein palmitoylation that plays a role in protein-membrane interactions, protein trafficking, and enzyme activity. -!- Palmitoylation increases the hydrophobicity of proteins or protein domains and contributes to their membrane association.
6.3.1.2
Glutamine synthetase.
based on mapping to UniProt P15104
ATP + L-glutamate + NH(3) = ADP + phosphate + L-glutamine.
-!- Glutamine synthetase, which catalyzes the incorporation of ammonium into glutamate, is a key enzyme of nitrogen metabolism found in all domains of life. -!- Several types have been described, differing in their oligomeric structures and cofactor requirements.

UniProtKB Entries (1)

P15104
GLNA_HUMAN
Homo sapiens
Glutamine synthetase

PDB Structure

PDB 2OJW
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Crystal structures of mammalian glutamine synthetases illustrate substrate-induced conformational changes and provide opportunities for drug and herbicide design.
Krajewski, W.W., Collins, R., Holmberg-Schiavone, L., Jones, T.A., Karlberg, T., Mowbray, S.L.
J.Mol.Biol.