TRNAIle-lysidine synthase
TRNAIle-lysidine synthase | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||
EC number | 6.3.4.19 | ||||||||
CAS number | 635304-92-6 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB 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 [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
- ↑ Ikeuchi, Y.; Soma, A.; Ote, T.; Kato, J.; Sekine, Y.; Suzuki, T. (2005). "molecular mechanism of lysidine synthesis that determines tRNA identity and codon recognition". Mol. Cell. 19 (2): 235–246. doi:10.1016/j.molcel.2005.06.007. PMID 16039592.
- ↑ Salowe, S.P.; Wiltsie, J.; Hawkins, J.C.; Sonatore, L.M. (2009). "The catalytic flexibility of tRNAIle-lysidine synthetase can generate alternative tRNA substrates for isoleucyl-tRNA synthetase". J. Biol. Chem. 284: 9656–9662. doi:10.1074/jbc.M809013200. PMC 2665086. PMID 19233850.
- ↑ Nakanishi, K.; Fukai, S.; Ikeuchi, Y.; Soma, A.; Sekine, Y.; Suzuki, T.; Nureki, O. (2005). "Structural basis for lysidine formation by ATP pyrophosphatase accompanied by a lysine-specific loop and a tRNA-recognition domain". Proc. Natl. Acad. Sci. USA. 102: 7487–7492. doi:10.1073/pnas.0501003102. PMC 1140429. PMID 15894617.
- ↑ Soma, A.; Ikeuchi, Y.; Kanemasa, S.; Kobayashi, K.; Ogasawara, N.; Ote, T.; Kato, J.; Watanabe, K.; Sekine, Y.; Suzuki, T. (2003). "An RNA-modifying enzyme that governs both the codon and amino acid specificities of isoleucine tRNA". Mol. Cell. 12 (3): 689–698. doi:10.1016/s1097-2765(03)00346-0. PMID 14527414.
- ↑ Nakanishi, K.; Bonnefond, L.; Kimura, S.; Suzuki, T.; Ishitani, R.; Nureki, O. (2009). "Structural basis for translational fidelity ensured by transfer RNA lysidine synthetase". Nature. 461 (7267): 1144–1148. doi:10.1038/nature08474. PMID 19847269.
External links
- TRNAIle-lysidine synthase at the US National Library of Medicine Medical Subject Headings (MeSH)
This article is issued from Wikipedia - version of the 5/23/2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.