5.4.99.12: tRNA pseudouridine38-40 synthase
This is an abbreviated version!
For detailed information about tRNA pseudouridine38-40 synthase, go to the full flat file.
Reaction
Synonyms
Deg1, Deg1p, hisT, mPus3p, pseudouridine synthase, pseudouridine synthase 3, pseudouridine synthase I, PSUI, PUS3, Pus3p, tRNA pseudouridine synthase 3, tRNA pseudouridine synthase I, TruA
ECTree
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Substrates Products
Substrates Products on EC 5.4.99.12 - tRNA pseudouridine38-40 synthase
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REACTION DIAGRAM
Escherichia coli tRNAPhe uridine39
Escherichia coli tRNAPhe pseudouridine39
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human tRNALeu uridine 38 uridine39
human tRNALeu pseudouridine 38 pseudouridine39
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psuedouridine formation in position 39 is clearly preferred over position 38
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Salmonella typhimurium HisT- tRNALeu
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tRNAPhe2 from mutant HisT- strain defective for tRNA pseudouridine synthase I that forms pseudouridine in the 3'-side of the anticodon region of approximately half of the cellular tRNAs
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Salmonella typhimurium HisT- tRNAPhe2 uridine39
Salmonella typhimurium HisT- tRNAPhe2 pseudouridine39
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tRNAPhe2 from mutant HisT- strain defective for tRNA pseudouridine synthase I that forms pseudouridine in the 3 side of the anticodon region of approximately half of the cellular tRNAs
specific modification of uridine39
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Salmonelly typhimurium HisT- tRNATyr
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tRNAPhe2 from mutant HisT- strain defective for tRNA pseudouridine synthase I that forms pseudouridine in the 3'-side of the anticodon region of approximately half of the cellular tRNAs
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tRNA uridine40
tRNA pseudouridine40
modified tRNALeu3 with uridine at position 40 instead of position 38. Wild-typeTruA pseudouridylates uridines at all three positions (38, 39 and 40) with efficiencies (kcat/KM) differing by less than 10fold, while R58A is inactive toward all three uridines
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tRNAHis guanidine36 uridine38 cytidine39
RNAHis guanidine36 pseudouridine38 cytidine39
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tRNAHis uridine38 uridine39
tRNAHis pseudouridine38 pseudouridine39
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tRNALeu3 carrying uridine at position 38
tRNALeu3 carrying pseudouridine at position 38
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tRNALeu3 carrying uridine at position 39
tRNALeu3 carrying pseudouridine at position 39
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tRNALeu3 carrying uridine at position 40
tRNALeu3 carrying pseudouridine at position 40
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tRNAVal2a cytidine36 uridine38
tRNAVal2a cytidine36 pseudouridine38
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poor substrate, tRNAVal2a is not a substrate
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additional information
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presence of a G36 residue modulates modification at position 38. In addition to local sequence effects, steady-state kinetic analyses suggest the existence of other recognition elements distinct from the immediate vicinity of modification
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tRNA pseudouridine38
tRNALeu3 contains uridine at position 38. Wild-typeTruA pseudouridylates uridines at all three positions (38, 39 and 40) with efficiencies (kcat/KM) differing by less than 10fold, while R58A is inactive toward all three uridines. When flexibility of the anticodon stem loop is increased by mutating the two G:C base pairs in the stem of the anticodon stem loop of tRNALeu3 into A:U pairs, the kcat/KM increased 2fold. When flexibility is decreased by base-pairing the target U38 of tRNALeu3 with A32 instead of with U32, the kcat/KM decreases 10fold
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tRNA uridine38
tRNA pseudouridine38
the enzyme modifies the anticodon arm of transfer RNA at positions 38 and 39 by catalyzing the conversion of uridine to pseudouridine
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tRNA pseudouridine38-40
TruA specifically modifies uridines at positions 38, 39, and/or 40 of tRNAs with highly divergent sequences and structures
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tRNA uridine38-40
tRNA pseudouridine38-40
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purified tRNA pseudouridine synthase I modifies all of the hisT isoacceptors of tRNAHis, tRNATyr, and tRNALeu to products which are chromatographically indistinguishable from the respective wild-type species. These three groups of isoacceptors contain all the known topological sites for pseudouridine modification of residues 38,39, and 40
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tRNA uridine38-40
tRNA pseudouridine38-40
TruA specifically modifies uridines at positions 38, 39, and/or 40 of tRNAs with highly divergent sequences and structures. The molecular basis for the site and substrate promiscuity is studied by determining the crystal structures of Eschrichia coli TruA in complex with two different leucyl tRNAs in conjunction with functional assays and computer simulation
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tRNA pseudouridine39
modified tRNALeu3 with uridine at position 39 instead of position 38. Wild-typeTruA pseudouridylates uridines at all three positions (38, 39 and 40) with efficiencies (kcat/KM) differing by less than 10fold, while R58A is inactive toward all three uridines
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tRNA uridine39
tRNA pseudouridine39
tRNAPhe from yeast, which contains a single target for tRNA pseudouridine synthase I at U39
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tRNA uridine39
tRNA pseudouridine39
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tRNAPhe with uridine at position 39
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tRNA uridine39
tRNA pseudouridine39
with tRNA substrates from both yeast and humans, uridines at position 39 are modified to pseudouridine. In a tRNA substrate with a uridine at position 38 (human tRNALeu), there is very slight formation of pseudouridine at that position after incubation with mPus3p
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tRNA uridine39
tRNA pseudouridine39
the enzyme modifies the anticodon arm of transfer RNA at positions 38 and 39 by catalyzing the conversion of uridine to pseudouridine
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