In enzymology, a diphthine—ammonia ligase (EC 6.3.1.14, diphthamide synthase, diphthamide synthetase) is an enzyme that catalyzes the chemical reaction
| Diphthine—ammonia ligase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 6.3.1.14 | ||||||||
| CAS no. | 114514-33-9 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
- ATP + diphthine + NH3 ADP + phosphate + diphthamide
The 3 substrates of this enzyme are ATP, diphthine, and NH3, whereas its 3 products are ADP, phosphate, and diphthamide.
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases). The systematic name of this enzyme class is diphthine:ammonia ligase (ADP-forming). Other names in common use include diphthamide synthase, and diphthamide synthetase.
References
edit- Moehring JM, Moehring TJ (1988). "The post-translational trimethylation of diphthamide studied in vitro". J. Biol. Chem. 263 (8): 3840–4. PMID 3346227.
- Moehring TJ, Moehring JM (1987). "Mutant cultured cells used to study the synthesis of diphthamide". UCLA Symp. Mol. Cell. Biol. New Series. 45: 53–63.
