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TRNA pseudouridine13 synthase

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(Redirected from Pus7 protein)
tRNA pseudouridine13 synthase
Identifiers
EC no.5.4.99.27
CAS no.430429-15-5
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
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PMCarticles
PubMedarticles
NCBIproteins

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 tRNA pseudouridine13

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

References

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  1. ^ Ericsson UB, Nordlund P, Hallberg BM (May 2004). "X-ray structure of tRNA pseudouridine synthase TruD reveals an inserted domain with a novel fold". FEBS Letters. 565 (1–3): 59–64. doi:10.1016/j.febslet.2004.03.085. PMID 15135053. S2CID 31602560.
  2. ^ Chan CM, Huang RH (September 2009). "Enzymatic characterization and mutational studies of TruD--the fifth family of pseudouridine synthases". Archives of Biochemistry and Biophysics. 489 (1–2): 15–9. doi:10.1016/j.abb.2009.07.023. PMID 19664587.
  3. ^ Kaya Y, Ofengand J (June 2003). "A novel unanticipated type of pseudouridine synthase with homologs in bacteria, archaea, and eukarya". RNA. 9 (6): 711–21. doi:10.1261/rna.5230603. PMC 1370438. PMID 12756329.
  4. ^ Behm-Ansmant I, Urban A, Ma X, Yu YT, Motorin Y, Branlant C (November 2003). "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. doi:10.1261/rna.5520403. PMC 1287059. PMID 14561887.
  5. ^ Urban A, Behm-Ansmant I, Branlant C, Motorin Y (February 2009). "RNA sequence and two-dimensional structure features required for efficient substrate modification by the Saccharomyces cerevisiae RNA:{Psi}-synthase Pus7p" (PDF). The Journal of Biological Chemistry. 284 (9): 5845–58. doi:10.1074/jbc.m807986200. PMID 19114708. S2CID 19586610.
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