Biology:TRNAIle-lysidine synthase

From HandWiki
TRNAIle-lysidine synthase
Identifiers
EC number6.3.4.19
CAS number635304-92-6
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

TRNAIle-lysidine synthase (EC 6.3.4.19, TilS, mesJ (gene), yacA (gene), isoleucine-specific transfer ribonucleate lysidine synthetase, tRNAIle-lysidine synthetase) is an enzyme with systematic name L-lysine:(tRNAIle2)-cytidine34 ligase (AMP-forming).[1][2][3][4][5] This enzyme catalyses the following chemical reaction

[tRNAIle2]-cytidine34 + L-lysine + ATP [math]\displaystyle{ \rightleftharpoons }[/math] [tRNAIle2]-lysidine34 + AMP + diphosphate + H2O

The bacterial enzyme modifies the wobble base of the CAU anticodon of tRNAIle at the oxo group in position 2 of cytidine34.

References

  1. "molecular mechanism of lysidine synthesis that determines tRNA identity and codon recognition". Molecular Cell 19 (2): 235–46. July 2005. doi:10.1016/j.molcel.2005.06.007. PMID 16039592. 
  2. "The catalytic flexibility of tRNAIle-lysidine synthetase can generate alternative tRNA substrates for isoleucyl-tRNA synthetase". The Journal of Biological Chemistry 284 (15): 9656–62. April 2009. doi:10.1074/jbc.M809013200. PMID 19233850. 
  3. "Structural basis for lysidine formation by ATP pyrophosphatase accompanied by a lysine-specific loop and a tRNA-recognition domain". Proceedings of the National Academy of Sciences of the United States of America 102 (21): 7487–92. May 2005. doi:10.1073/pnas.0501003102. PMID 15894617. 
  4. "An RNA-modifying enzyme that governs both the codon and amino acid specificities of isoleucine tRNA". Molecular Cell 12 (3): 689–98. September 2003. doi:10.1016/s1097-2765(03)00346-0. PMID 14527414. 
  5. "Structural basis for translational fidelity ensured by transfer RNA lysidine synthetase". Nature 461 (7267): 1144–8. October 2009. doi:10.1038/nature08474. PMID 19847269. 

External links