| TRNA (pseudouridine54-N1)-methyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.1.1.257 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
TRNA (pseudouridine54-N1)-methyltransferase ( EC 2.1.1.257, TrmY, m1Psi methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:tRNA (pseudouridine54-N1)-methyltransferase. [1] [2] [3] This enzyme catalyses the following chemical reaction
- S-adenosyl-L-methionine + pseudouridine54 in tRNA S-adenosyl-L-homocysteine + N1- methylpseudouridine54 in tRNA
This archaeal enzyme is specific for the 54 position.
References
- ^ Chen HY, Yuan YA (December 2010). "Crystal structure of Mj1640/DUF358 protein reveals a putative SPOUT-class RNA methyltransferase". Journal of Molecular Cell Biology. 2 (6): 366–74. doi: 10.1093/jmcb/mjq034. PMID 21098051.
- ^ Wurm JP, Griese M, Bahr U, Held M, Heckel A, Karas M, Soppa J, Wöhnert J (March 2012). "Identification of the enzyme responsible for N1-methylation of pseudouridine 54 in archaeal tRNAs". RNA. 18 (3): 412–20. doi: 10.1261/rna.028498.111. PMC 3285930. PMID 22274954.
- ^ Chatterjee K, Blaby IK, Thiaville PC, Majumder M, Grosjean H, Yuan YA, Gupta R, de Crécy-Lagard V (March 2012). "The archaeal COG1901/DUF358 SPOUT-methyltransferase members, together with pseudouridine synthase Pus10, catalyze the formation of 1-methylpseudouridine at position 54 of tRNA". RNA. 18 (3): 421–33. doi: 10.1261/rna.030841.111. PMC 3285931. PMID 22274953.
External links
- TRNA+(pseudouridine54-N1)-methyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
| TRNA (pseudouridine54-N1)-methyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.1.1.257 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
TRNA (pseudouridine54-N1)-methyltransferase ( EC 2.1.1.257, TrmY, m1Psi methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:tRNA (pseudouridine54-N1)-methyltransferase. [1] [2] [3] This enzyme catalyses the following chemical reaction
- S-adenosyl-L-methionine + pseudouridine54 in tRNA S-adenosyl-L-homocysteine + N1- methylpseudouridine54 in tRNA
This archaeal enzyme is specific for the 54 position.
References
- ^ Chen HY, Yuan YA (December 2010). "Crystal structure of Mj1640/DUF358 protein reveals a putative SPOUT-class RNA methyltransferase". Journal of Molecular Cell Biology. 2 (6): 366–74. doi: 10.1093/jmcb/mjq034. PMID 21098051.
- ^ Wurm JP, Griese M, Bahr U, Held M, Heckel A, Karas M, Soppa J, Wöhnert J (March 2012). "Identification of the enzyme responsible for N1-methylation of pseudouridine 54 in archaeal tRNAs". RNA. 18 (3): 412–20. doi: 10.1261/rna.028498.111. PMC 3285930. PMID 22274954.
- ^ Chatterjee K, Blaby IK, Thiaville PC, Majumder M, Grosjean H, Yuan YA, Gupta R, de Crécy-Lagard V (March 2012). "The archaeal COG1901/DUF358 SPOUT-methyltransferase members, together with pseudouridine synthase Pus10, catalyze the formation of 1-methylpseudouridine at position 54 of tRNA". RNA. 18 (3): 421–33. doi: 10.1261/rna.030841.111. PMC 3285931. PMID 22274953.
External links
- TRNA+(pseudouridine54-N1)-methyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)