Biology:TRNA pseudouridine32 synthase

From HandWiki
tRNA pseudouridine32 synthase
Identifiers
EC number5.4.99.28
CAS number430429-15-5
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

tRNA pseudouridine32 synthase (EC 5.4.99.28, RluA, pseudouridine synthase RluA, Pus9p, Rib2/Pus8p) is an enzyme with systematic name tRNA-uridine32 uracil mutase.[1][2][3][4][5][6] This enzyme catalyses the following chemical reaction

tRNA uridine32 tRNA pseudouridine32

The dual enzyme from Escherichia coli also catalyses the formation of pseudouridine746 in 23S rRNA.

References

  1. "Crystal structure of pseudouridine synthase RluA: indirect sequence readout through protein-induced RNA structure". Molecular Cell 24 (4): 535–45. November 2006. doi:10.1016/j.molcel.2006.09.017. PMID 17188032. 
  2. "Functional importance of motif I of pseudouridine synthases: mutagenesis of aligned lysine and proline residues". Biochemistry 39 (31): 9459–65. August 2000. doi:10.1021/bi001079n. PMID 10924141. 
  3. "Functional effect of deletion and mutation of the Escherichia coli ribosomal RNA and tRNA pseudouridine synthase RluA". The Journal of Biological Chemistry 274 (27): 18880–6. July 1999. doi:10.1074/jbc.274.27.18880. PMID 10383384. 
  4. "Role of cysteine residues in pseudouridine synthases of different families". Biochemistry 38 (40): 13106–11. October 1999. doi:10.1021/bi9913911. PMID 10529181. 
  5. "A dual-specificity pseudouridine synthase: an Escherichia coli synthase purified and cloned on the basis of its specificity for psi 746 in 23S RNA is also specific for psi 32 in tRNA(phe)". RNA 1 (4): 437–48. June 1995. PMID 7493321. 
  6. "Pseudouridylation at position 32 of mitochondrial and cytoplasmic tRNAs requires two distinct enzymes in Saccharomyces cerevisiae". The Journal of Biological Chemistry 279 (51): 52998–3006. December 2004. doi:10.1074/jbc.m409581200. PMID 15466869. https://hal.univ-lorraine.fr/hal-01738505/file/Behm-Ansmant%20et%20al.%2C%202004%2C%20JBC%2C%20Pus8_9.pdf.