Biology:TRNA pseudouridine13 synthase

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tRNA pseudouridine13 synthase
Identifiers
EC number5.4.99.27
CAS number430429-15-5
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

tRNA pseudouridine13 synthase (EC 5.4.99.27, TruD, YgbO, tRNA PSI13 synthase, RNA:PSI-synthase Pus7p, Pus7p, RNA:pseudouridine-synthase Pus7p, Pus7 protein) is an enzyme with systematic name tRNA-uridine13 uracil mutase.[1][2][3][4][5] This enzyme catalyses the following chemical reaction

tRNA uridine13 [math]\displaystyle{ \rightleftharpoons }[/math] tRNA pseudouridine13

Pseudouridine synthase TruD from Escherichia coli specifically acts on uridine13 in tRNA.

References

  1. "X-ray structure of tRNA pseudouridine synthase TruD reveals an inserted domain with a novel fold". FEBS Letters 565 (1–3): 59–64. May 2004. doi:10.1016/j.febslet.2004.03.085. PMID 15135053. 
  2. "Enzymatic characterization and mutational studies of TruD--the fifth family of pseudouridine synthases". Archives of Biochemistry and Biophysics 489 (1–2): 15–9. September 2009. doi:10.1016/j.abb.2009.07.023. PMID 19664587. 
  3. "A novel unanticipated type of pseudouridine synthase with homologs in bacteria, archaea, and eukarya". RNA 9 (6): 711–21. June 2003. doi:10.1261/rna.5230603. PMID 12756329. 
  4. "The Saccharomyces cerevisiae U2 snRNA:pseudouridine-synthase Pus7p is a novel multisite-multisubstrate RNA:Psi-synthase also acting on tRNAs". RNA 9 (11): 1371–82. November 2003. doi:10.1261/rna.5520403. PMID 14561887. 
  5. "RNA sequence and two-dimensional structure features required for efficient substrate modification by the Saccharomyces cerevisiae RNA:{Psi}-synthase Pus7p". The Journal of Biological Chemistry 284 (9): 5845–58. February 2009. doi:10.1074/jbc.m807986200. PMID 19114708. https://hal.archives-ouvertes.fr/hal-01738433/file/Urban%20et%20al.%2C%20JBC%2C%202009.pdf. 

External links