|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Macromolecule Reactions → Polynucleotide-Reactions → RNA-Reactions → tRNA-Reactions|
EC Number: 220.127.116.11
The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the Enzyme Commission system.
Mass balance status: Balanced.
Enzyme Commission Primary Name: tRNA pseudouridine38-40 synthase
Enzyme Commission Synonyms: TruA, tRNA pseudouridine synthase I, PSUI, hisT (gene name)
Enzyme Commission Summary:
The uridylate residues at positions 38, 39 and 40 of nearly all tRNAs are isomerized to pseudouridine. The bacterial enzyme TruA specifically modifies uridines at positions 38, 39, and/or 40 in the anticodon stem loop of tRNAs with highly divergent sequences and structures [Hur07]. The yeast enzyme Pus3 is active only towards uridine38 and uridine39, and shows no activity with uridine40 [Zhao97]. The enzyme from mouse is active only towards uridine39 [Foster00].
Dong06: Dong X, Bessho Y, Shibata R, Nishimoto M, Shirouzu M, Kuramitsu S, Yokoyama S (2006). "Crystal structure of tRNA pseudouridine synthase TruA from Thermus thermophilus HB8." RNA Biol 3(3);115-22. PMID: 17114947
Foster00: Foster PG, Huang L, Santi DV, Stroud RM (2000). "The structural basis for tRNA recognition and pseudouridine formation by pseudouridine synthase I." Nat Struct Biol 7(1);23-7. PMID: 10625422
Huang98a: Huang L, Pookanjanatavip M, Gu X, Santi DV (1998). "A conserved aspartate of tRNA pseudouridine synthase is essential for activity and a probable nucleophilic catalyst." Biochemistry 37(1);344-51. PMID: 9425056
Lecointe98: Lecointe F, Simos G, Sauer A, Hurt EC, Motorin Y, Grosjean H (1998). "Characterization of yeast protein Deg1 as pseudouridine synthase (Pus3) catalyzing the formation of psi 38 and psi 39 in tRNA anticodon loop." J Biol Chem 273(3);1316-23. PMID: 9430663
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