Biology:Glutaminyl-tRNA synthase (glutamine-hydrolysing)
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Glutaminyl-tRNA synthase (glutamine-hydrolyzing) | |||||||||
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Identifiers | |||||||||
EC number | 6.3.5.7 | ||||||||
CAS number | 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 | ||||||||
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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 [math]\displaystyle{ \rightleftharpoons }[/math] 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
- "Mechanistic studies of reaction coupling in Glu-tRNAGln amidotransferase". Biochemistry 40 (21): 6450–7. 2001. doi:10.1021/bi002599l. PMID 11371208.
- "Glutamyl-tRNA(Gln) amidotransferase in Deinococcus radiodurans may be confined to asparagine biosynthesis". Proc. Natl. Acad. Sci. U.S.A. 95 (22): 12838–43. 1998. doi:10.1073/pnas.95.22.12838. PMID 9789001. Bibcode: 1998PNAS...9512838C.
- "Aminoacyl-tRNA synthesis". Annu. Rev. Biochem. 69: 617–50. 2000. doi:10.1146/annurev.biochem.69.1.617. PMID 10966471.
![]() | Original source: https://en.wikipedia.org/wiki/Glutaminyl-tRNA synthase (glutamine-hydrolysing).
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