The Enzyme Database

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EC 3.5.4.33     
Accepted name: tRNA(adenine34) deaminase
Reaction: adenine34 in tRNA + H2O = hypoxanthine34 in tRNA + NH3
Other name(s): tRNA:A34 deaminase; tadA protein; ADAT2-ADAT3 complex; TADA; tRNA adenosine deaminase arginine; AtTadA; tadA/ecADAT2; tRNA A:34 deaminase
Systematic name: tRNA(adenine34) aminohydrolase
Comments: The enzyme is involved in editing of tRNA. The active site contains Zn2+ [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Spears, J.L., Rubio, M.A., Gaston, K.W., Wywial, E., Strikoudis, A., Bujnicki, J.M., Papavasiliou, F.N. and Alfonzo, J.D. A single zinc ion is sufficient for an active Trypanosoma brucei tRNA editing deaminase. J. Biol. Chem. 286 (2011) 20366–20374. [DOI] [PMID: 21507956]
2.  Delannoy, E., Le Ret, M., Faivre-Nitschke, E., Estavillo, G.M., Bergdoll, M., Taylor, N.L., Pogson, B.J., Small, I., Imbault, P. and Gualberto, J.M. Arabidopsis tRNA adenosine deaminase arginine edits the wobble nucleotide of chloroplast tRNAArg(ACG) and is essential for efficient chloroplast translation. Plant Cell 21 (2009) 2058–2071. [DOI] [PMID: 19602623]
3.  Kuratani, M., Ishii, R., Bessho, Y., Fukunaga, R., Sengoku, T., Shirouzu, M., Sekine, S. and Yokoyama, S. Crystal structure of tRNA adenosine deaminase (TadA) from Aquifex aeolicus. J. Biol. Chem. 280 (2005) 16002–16008. [DOI] [PMID: 15677468]
4.  Wolf, J., Gerber, A.P. and Keller, W. tadA, an essential tRNA-specific adenosine deaminase from Escherichia coli. EMBO J. 21 (2002) 3841–3851. [DOI] [PMID: 12110595]
5.  Lee, W.H., Kim, Y.K., Nam, K.H., Priyadarshi, A., Lee, E.H., Kim, E.E., Jeon, Y.H., Cheong, C. and Hwang, K.Y. Crystal structure of the tRNA-specific adenosine deaminase from Streptococcus pyogenes. Proteins 68 (2007) 1016–1019. [DOI] [PMID: 17554781]
6.  Ragone, F.L., Spears, J.L., Wohlgamuth-Benedum, J.M., Kreel, N., Papavasiliou, F.N. and Alfonzo, J.D. The C-terminal end of the Trypanosoma brucei editing deaminase plays a critical role in tRNA binding. RNA 17 (2011) 1296–1306. [DOI] [PMID: 21602302]
[EC 3.5.4.33 created 2013]
 
 


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