| EC |
6.1.1.11 |
| Accepted name: |
serine—tRNA ligase |
| Reaction: |
ATP + L-serine + tRNASer = AMP + diphosphate + L-seryl-tRNASer |
| Other name(s): |
seryl-tRNA synthetase; SerRS; seryl-transfer ribonucleate synthetase; seryl-transfer RNA synthetase; seryl-transfer ribonucleic acid synthetase; serine translase |
| Systematic name: |
L-serine:tRNASer ligase (AMP-forming) |
| Comments: |
This enzyme also recognizes tRNASec, the special tRNA for selenocysteine, and catalyses the formation of L-seryl-tRNASec, the substrate for EC 2.9.1.1, L-seryl-tRNASec selenium transferase. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9023-48-7 |
| References: |
| 1. |
Katze, J.R. and Konigsberg, W. Purification and properties of seryl transfer ribonucleic acid synthetase from Escherichia coli. J. Biol. Chem. 245 (1970) 923–930. [PMID: 4906848] |
| 2. |
Makman, M.H. and Cantoni, G.L. Isolation of seryl and phenylalanyl ribonucleic acid synthetases from baker's yeast. Biochemistry 4 (1965) 1434–1442. |
| 3. |
Webster, L.T. and Davie, E.W. Purification and properties of serine-activating enzyme from beef pancreas. J. Biol. Chem. 236 (1961) 479–484. [PMID: 13783661] |
| 4. |
Ohama, T., Yang, D.C. and Hatfield, D.L. Selenocysteine tRNA and serine tRNA are aminoacylated by the same synthetase, but may manifest different identities with respect to the long extra arm. Arch. Biochem. Biophys. 315 (1994) 293–301. [DOI] [PMID: 7986071] |
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| [EC 6.1.1.11 created 1961, modified 2002] |
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