| Glutaminyl-tRNA synthase (glutamine-hydrolyzing) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 6.3.5.7 | ||||||||
| CAS no. | 52232-48-1 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a glutaminyl-tRNA synthase (glutamine-hydrolysing) (EC 6.3.5.7) is an enzyme that catalyzes the chemical reaction
- ATP + glutamyl-tRNAGln + L-glutamine ADP + phosphate + glutaminyl-tRNAGln + L-glutamate
The 3 substrates of this enzyme are ATP, glutamyl-tRNA(Gln), and L-glutamine, whereas its 4 products are ADP, phosphate, glutaminyl-tRNA(Gln), and L-glutamate.
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds carbon-nitrogen ligases with glutamine as amido-N-donor. The systematic name of this enzyme class is glutamyl-tRNAGln:L-glutamine amido-ligase (ADP-forming). This enzyme participates in glutamate metabolism and alanine and aspartate metabolism.
References
- Horiuchi KY, Harpel MR, Shen L, Luo Y, Rogers KC, Copeland RA (2001). "Mechanistic studies of reaction coupling in Glu-tRNAGln amidotransferase". Biochemistry. 40 (21): 6450–7. doi:10.1021/bi002599l. PMID 11371208.
- Curnow AW, Tumbula DL, Pelaschier JT, Min B, Soll D (1998). "Glutamyl-tRNA(Gln) amidotransferase in Deinococcus radiodurans may be confined to asparagine biosynthesis". Proc. Natl. Acad. Sci. U.S.A. 95 (22): 12838–43. Bibcode:1998PNAS...9512838C. doi:10.1073/pnas.95.22.12838. PMC 23620. PMID 9789001.
- Ibba M, Soll D (2000). "Aminoacyl-tRNA synthesis". Annu. Rev. Biochem. 69: 617–50. doi:10.1146/annurev.biochem.69.1.617. PMID 10966471.
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