| EC |
6.3.5.7 |
| Accepted name: |
glutaminyl-tRNA synthase (glutamine-hydrolysing) |
| Reaction: |
ATP + L-glutamyl-tRNAGln + L-glutamine = ADP + phosphate + L-glutaminyl-tRNAGln + L-glutamate |
| Other name(s): |
Glu-AdT; Glu-tRNAGln amidotransferase; glutamyl-tRNAGln amidotransferase; Glu-tRNAGln:L-glutamine amido-ligase (ADP-forming) |
| Systematic name: |
L-glutamyl-tRNAGln:L-glutamine amido-ligase (ADP-forming) |
| Comments: |
In systems lacking discernible glutamine—tRNA ligase (EC 6.1.1.18), glutaminyl-tRNAGln is formed by a two-enzyme system. In the first step, a nondiscriminating ligase (EC 6.1.1.24, glutamate—tRNAGln ligase) mischarges tRNAGln with glutamate, forming glutamyl-tRNAGln. The glutamyl-tRNAGln is not used in protein synthesis until the present enzyme converts it into glutaminyl-tRNAGln (glutamyl-tRNAGlu is not a substrate for this reaction). Ammonia or asparagine can substitute for the preferred substrate glutamine. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 52232-48-1 |
| References: |
| 1. |
Horiuchi, K.Y., Harpel, M.R., Shen, L., Luo, Y., Rogers, K.C. and Copeland, R.A. Mechanistic studies of reaction coupling in Glu-tRNAGln amidotransferase. Biochemistry 40 (2001) 6450–6457. [DOI] [PMID: 11371208] |
| 2. |
Curnow, A.W., Tumbula, D.L., Pelaschier, J.T., Min, B. and Söll, D. Glutamyl-tRNAGln amidotransferase in Deinococcus radiodurans may be confined to asparagine biosynthesis. Proc. Natl. Acad. Sci. USA 95 (1998) 12838–12843. [DOI] [PMID: 9789001] |
| 3. |
Ibba, M. and Söll, D. Aminoacyl-tRNA synthesis. Annu. Rev. Biochem. 69 (2000) 617–650. [DOI] [PMID: 10966471] |
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| [EC 6.3.5.7 created 2002] |
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