Glutamate—putrescine ligase
| Glutamate-putrescine ligase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 6.3.1.11 | ||||||||
| CAS number | 914090-78-1 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
In enzymology, a glutamate-putrescine ligase (EC 6.3.1.11) is an enzyme that catalyzes the chemical reaction
- ATP + L-glutamate + putrescine ADP + phosphate + gamma-L-glutamylputrescine
The 3 substrates of this enzyme are ATP, L-glutamate, and putrescine, whereas its 3 products are ADP, phosphate, and gamma-L-glutamylputrescine.
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-ammonia (or amine) ligases (amide synthases). The systematic name of this enzyme class is L-glutamate:putrescine ligase (ADP-forming). Other names in common use include gamma-glutamylputrescine synthetase, and YcjK. This enzyme participates in urea cycle and metabolism of amino groups.
References
- Kurihara S, Oda S, Kato K, Kim HG, Koyanagi T, Kumagai H, Suzuki H (2005). "A novel putrescine utilization pathway involves gamma-glutamylated intermediates of Escherichia coli K-12". J. Biol. Chem. 280 (6): 4602&ndash, 8. doi:10.1074/jbc.M411114200. PMID 15590624.
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