| TRNAIle-lysidine synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 6.3.4.19 | ||||||||
| CAS no. | 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 (July 2005). "molecular mechanism of lysidine synthesis that determines tRNA identity and codon recognition". Molecular Cell. 19 (2): 235–46. doi: 10.1016/j.molcel.2005.06.007. PMID 16039592.
- ^ Salowe SP, Wiltsie J, Hawkins JC, Sonatore LM (April 2009). "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. doi: 10.1074/jbc.M809013200. PMC 2665086. PMID 19233850.
- ^ Nakanishi K, Fukai S, Ikeuchi Y, Soma A, Sekine Y, Suzuki T, Nureki O (May 2005). "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. 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 (September 2003). "An RNA-modifying enzyme that governs both the codon and amino acid specificities of isoleucine tRNA". Molecular Cell. 12 (3): 689–98. doi: 10.1016/s1097-2765(03)00346-0. PMID 14527414.
- ^ Nakanishi K, Bonnefond L, Kimura S, Suzuki T, Ishitani R, Nureki O (October 2009). "Structural basis for translational fidelity ensured by transfer RNA lysidine synthetase". Nature. 461 (7267): 1144–8. doi: 10.1038/nature08474. PMID 19847269. S2CID 4426738.
External links
- TRNAIle-lysidine+synthase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
| TRNAIle-lysidine synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 6.3.4.19 | ||||||||
| CAS no. | 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 (July 2005). "molecular mechanism of lysidine synthesis that determines tRNA identity and codon recognition". Molecular Cell. 19 (2): 235–46. doi: 10.1016/j.molcel.2005.06.007. PMID 16039592.
- ^ Salowe SP, Wiltsie J, Hawkins JC, Sonatore LM (April 2009). "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. doi: 10.1074/jbc.M809013200. PMC 2665086. PMID 19233850.
- ^ Nakanishi K, Fukai S, Ikeuchi Y, Soma A, Sekine Y, Suzuki T, Nureki O (May 2005). "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. 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 (September 2003). "An RNA-modifying enzyme that governs both the codon and amino acid specificities of isoleucine tRNA". Molecular Cell. 12 (3): 689–98. doi: 10.1016/s1097-2765(03)00346-0. PMID 14527414.
- ^ Nakanishi K, Bonnefond L, Kimura S, Suzuki T, Ishitani R, Nureki O (October 2009). "Structural basis for translational fidelity ensured by transfer RNA lysidine synthetase". Nature. 461 (7267): 1144–8. doi: 10.1038/nature08474. PMID 19847269. S2CID 4426738.
External links
- TRNAIle-lysidine+synthase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)