| EC |
2.3.1.193 |
| Accepted name: |
tRNAMet cytidine acetyltransferase |
| Reaction: |
[elongator tRNAMet]-cytidine34 + ATP + acetyl-CoA + H2O = CoA + [elongator tRNAMet]-N4-acetylcytidine34 + ADP + phosphate |
| Other name(s): |
YpfI; TmcA |
| Systematic name: |
acetyl-CoA:[elongator tRNAMet]-cytidine34 N4-acetyltransferase (ATP-hydrolysing) |
| Comments: |
The enzyme acetylates the wobble base cytidine34 of the CAU anticodon of elongation-specific tRNAMet. Escherichia coli TmcA strictly discriminates elongator tRNAMet from tRNAIle, which is structurally similar and has the same anticodon loop, mainly by recognizing the C27-G43 pair in the anticodon stem. The enzyme can use GTP in place of ATP for formation of N4-acetylcytidine [1]. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
| References: |
| 1. |
Ikeuchi, Y., Kitahara, K. and Suzuki, T. The RNA acetyltransferase driven by ATP hydrolysis synthesizes N4-acetylcytidine of tRNA anticodon. EMBO J. 27 (2008) 2194–2203. [DOI] [PMID: 18668122] |
| 2. |
Chimnaronk, S., Suzuki, T., Manita, T., Ikeuchi, Y., Yao, M., Suzuki, T. and Tanaka, I. RNA helicase module in an acetyltransferase that modifies a specific tRNA anticodon. EMBO J. 28 (2009) 1362–1373. [DOI] [PMID: 19322199] |
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| [EC 2.3.1.193 created 2011] |
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