| EC |
2.3.1.311 |
| Accepted name: |
tRNA carboxymethyluridine synthase |
| Reaction: |
acetyl-CoA + uridine34 in tRNA + S-adenosyl-L-methionine + H2O = CoA + 5-(carboxymethyl)uridine34 in tRNA + L-methionine + 5′-deoxyadenosine |
| Other name(s): |
elongator complex; ELP3 |
| Systematic name: |
acetyl-CoA:tRNA uridine carboxymethyltransferase |
| Comments: |
The enzyme, found in eukaryotes, most archaea, and some bacteria, catalyses the first step in modification of the wobble uridine base of certain tRNAs. In eukaryotes the enzyme is a complex of six conserved subunits, with ELP3 being the catalytic subunit. In archaea and bacteria the enzyme consists of a single subunit, homologous to ELP3. The enzyme contains an [4Fe-4S] cluster and uses radical chemistry. A 5′-deoxyadenosyl radical generated in the radical AdoMet (SAM) domain attacks the acetyl-CoA donor, activating its methyl group, which forms a C-C bond with C5 of the uridine moiety. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
| References: |
| 1. |
Paraskevopoulou, C., Fairhurst, S.A., Lowe, D.J., Brick, P. and Onesti, S. The Elongator subunit Elp3 contains a Fe4S4 cluster and binds S-adenosylmethionine. Mol. Microbiol. 59 (2006) 795–806. [DOI] [PMID: 16420352] |
| 2. |
Selvadurai, K., Wang, P., Seimetz, J. and Huang, R.H. Archaeal Elp3 catalyzes tRNA wobble uridine modification at C5 via a radical mechanism. Nat. Chem. Biol. 10 (2014) 810–812. [DOI] [PMID: 25151136] |
| 3. |
Lin, T.Y., Abbassi, N.EH., Zakrzewski, K., Chramiec-Glabik, A., Jemiola-Rzeminska, M., Rozycki, J. and Glatt, S. The Elongator subunit Elp3 is a non-canonical tRNA acetyltransferase. Nat. Commun. 10:625 (2019). [DOI] [PMID: 30733442] |
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| [EC 2.3.1.311 created 2022] |
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