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Literature summary for 5.4.99.27 extracted from

  • Muller, S.; Urban, A.; Hecker, A.; Leclerc, F.; Branlant, C.; Motorin, Y.
    Deficiency of the tRNATyr:Psi35-synthase aPus7 in Archaea of the Sulfolobales order might be rescued by the H/ACA sRNA-guided machinery (2009), Nucleic Acids Res., 37, 1308-1322.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.4.99.27

Cloned(Commentary)

Cloned (Comment) Organism
wild-type and mutant enzymes are produced in Escherichia coli as His6-tagged protein fusions Saccharolobus solfataricus
wild-type and mutant enzymes are produced in Escherichia coli as His6-tagged protein fusions Pyrococcus abyssi

Protein Variants

Protein Variants Comment Organism
A78R/N79H mutation has no positive effect on activity at 80°C on Pyrococcus abyssi tRNAAsp(GUA) Saccharolobus solfataricus
I27K mutation increases activity at 80°C on Pyrococcus abyssi tRNAAsp(GUA) 1.6fold Saccharolobus solfataricus
K19I mutation decreases the activity at position 13 in the Pyrococcus abyssi tRNAAsp at 55°C. At 80°C the mutation has almost no negative effect on its activity towards the Pyrococcus abyssi tRNATyr(GUA) Pyrococcus abyssi
K19I/R78A/H79N mutation completely abolishes the activity at position 13 in the Pyrococcus abyssi tRNAAsp at 55°C. At 80°C the mutation nearly abolishes activity towards the Pyrococcus abyssi tRNATyr(GUA) Pyrococcus abyssi
N79H mutation has no positive effect on activity at 80°C on Pyrococcus abyssi tRNAAsp(GUA) Saccharolobus solfataricus
R78A/H79N mutation decreases the activity at position 13 in the Pyrococcus abyssi tRNAAsp at 55°C. At 80°C the mutation has almost no negative effect on its activity towards the Pyrococcus abyssitRNATyr(GUA) Pyrococcus abyssi

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Pyrococcus abyssi tRNATyr(GUA) uridine35 Pyrococcus abyssi residue 35 reinforces the stability of the anticodon stem–loop by interaction with residue U33 (13). This structural stabilization may increase the aminoacylation efficiency of tRNATyr(GUA) by its cognate aminoacyl-tRNA synthetase Pyrococcus abyssi tRNATyr(GUA) pseudouridine35
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 ?

Organism

Organism UniProt Comment Textmining
Pyrococcus abyssi
-
-
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Saccharolobus solfataricus
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-
-

Purification (Commentary)

Purification (Comment) Organism
wild-type and mutant enzymes produced in Escherichia coli as His6-tagged protein fusions Saccharolobus solfataricus
wild-type and mutant enzymes produced in Escherichia coli as His6-tagged protein fusions Pyrococcus abyssi

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Pyrococcus abyssi tRNAAsp(GUA) uridine13
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 Pyrococcus abyssi Pyrococcus abyssi tRNAAsp(GUA) pseudouridine13
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 ?
Pyrococcus abyssi tRNATyr(GUA) uridine13 some activity at high temperature on tRNAs that contain a U residue at position 13. No activity of is detected at position 35 in the Sulfolobus solfataricus pre-tRNATyr(GUA), even at 80°C Saccharolobus solfataricus Pyrococcus abyssi tRNATyr(GUA) pseudouridine13
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 ?
Pyrococcus abyssi tRNATyr(GUA) uridine13 the enzyme modifies tRNAs at position 13 and at other positions as well as intron-less and intron-containing tRNAsTyr(GUA) at position 35 Pyrococcus abyssi Pyrococcus abyssi tRNATyr(GUA) pseudouridine13
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 ?
Pyrococcus abyssi tRNATyr(GUA) uridine35 residue 35 reinforces the stability of the anticodon stem–loop by interaction with residue U33 (13). This structural stabilization may increase the aminoacylation efficiency of tRNATyr(GUA) by its cognate aminoacyl-tRNA synthetase Pyrococcus abyssi Pyrococcus abyssi tRNATyr(GUA) pseudouridine35
-
 ?
Pyrococcus abyssi tRNATyr(GUA) uridine35 the enzyme modifies tRNAs at position 13 and at other positions as well as intron-less and intron-containing tRNAsTyr(GUA) at position 35 Pyrococcus abyssi Pyrococcus abyssi tRNATyr(GUA) pseudouridine35
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 ?

Synonyms

Synonyms Comment Organism
Pab aPus7
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 Pyrococcus abyssi
Sso aPus7
-
 Saccharolobus solfataricus