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Literature summary for 5.4.99.B22 extracted from

  • Sibert, B.S.; Fischel-Ghodsian, N.; Patton, J.R.
    Partial activity is seen with many substitutions of highly conserved active site residues in human Pseudouridine synthase 1 (2008), RNA, 14, 1895-1906.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
R116A the mutant exhibits some activity with the yeast pre-tRNAIle substrate. Low activity with the mouse tRNAMet substrate Homo sapiens
R116C the activity of the mutant enzyme with the yeast pre-tRNAIle substrate is approximately one-third that of the wild-type levels. No activity with the mouse tRNAMet substrate Homo sapiens
R116E the mutant is inactive with with the yeast pre-tRNAIle substrate. No activity with the mouse tRNAMet substrate Homo sapiens
R116G the mutant exhibits some activity with the yeast pre-tRNAIle substrate. No activity with the mouse tRNAMet substrate Homo sapiens
R116H the mutant is inactive with with the yeast pre-tRNAIle substrate. Low activity with the mouse tRNAMet substrate Homo sapiens
R116K the activity of the mutant enzyme with the yeast pre-tRNAIle substrate is approximately one-third that of the wild-type levels Homo sapiens
R116N the mutant exhibits some activity with the yeast pre-tRNAIle substrate. No activity with the mouse tRNAMet substrate Homo sapiens
R116Q the mutant exhibits some activity with the yeast pre-tRNAIle substrate. No activity with the mouse tRNAMet substrate Homo sapiens
R116S the mutant exhibits some activity with the yeast pre-tRNAIle substrate. No activity with the mouse tRNAMet substrate Homo sapiens
R116W the mutant is inactive with with the yeast pre-tRNAIle substrate. Low activity with the mouse tRNAMet substrate Homo sapiens
Y173C mutant enzyme retains some activity with yeast pre-tRNAIle. The activity is relatively low Homo sapiens
Y173F mutant enzyme is minimally activity with yeast pre-tRNAIle Homo sapiens
Y173F mutant enzyme retains some activity with yeast pre-tRNAIle. The activity is relatively low Homo sapiens
Y173G mutant enzyme retains some activity with yeast pre-tRNAIle. The activity is relatively low Homo sapiens
Y173S mutant enzyme is minimally activity with yeast pre-tRNAIle Homo sapiens
Y173T mutant enzyme is minimally activity with yeast pre-tRNAIle Homo sapiens
Y173T mutant enzyme retains some activity with yeast pre-tRNAIle. The activity is relatively low Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.000032
-
yeast pre-tRNAIle uridine possible modification sites are uridine 27, uridine30, uridine34 or uridine36, wild-type enzyme, pH and temperature not specified in the publication Homo sapiens
0.000168
-
yeast pre-tRNAIle uridine possible modification sites are uridine 27, uridine30, uridine34 or uridine36, mutant enzyme R116K, pH and temperature not specified in the publication Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q9Y606
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
human tRNAMet uridine27
-
Homo sapiens human tRNAMet pseudouridine27
-
?
additional information Pus1p modifies uridines at positions 1, 26, 27, 28, 30, 34, 36, 65, and 67 depending on the source of the enzyme (Saccharomyces cerevisiae or mouse), the substrates (intron-containing or not), or whether the activity is monitored in vivo or in vitro. Out of all the positions that Pus1p modifies, the modification of uridines at positions 27 and 28 is by far the most common in tRNAs, with pseudouridine infrequently found at the other positions that the Pus1p enzymes recognize Homo sapiens ?
-
?
mouse tRNAIle(UAU) uridine30
-
Homo sapiens mouse tRNAIle(UAU) pseudouridine30
-
?
mouse tRNAMet uridine27
-
Homo sapiens mouse tRNAMet pseudouridine27
-
?
yeast pre-tRNAIle uridine possible modification sites are uridine 27, uridine30, uridine34 or uridine36 Homo sapiens yeast pre-tRNAIle pseudouridine
-
?

Synonyms

Synonyms Comment Organism
hPus1p
-
Homo sapiens
pseudouridine synthase 1
-
Homo sapiens