5.4.99.25: tRNA pseudouridine55 synthase
This is an abbreviated version!
For detailed information about tRNA pseudouridine55 synthase, go to the full flat file.
Word Map on EC 5.4.99.25
-
5.4.99.25
-
synthases
-
pseudouridylation
-
anticodon
-
rna-guided
-
5-fluorouridine
-
srnps
-
thumb
-
snornas
-
eukaryal
- 5.4.99.25
- synthases
-
pseudouridylation
-
anticodon
-
rna-guided
- 5-fluorouridine
-
srnps
-
thumb
- snornas
-
eukaryal
Reaction
Synonyms
aCBF5, Cbf5, Mj-Pus10, MjPus10, More, pfuCbf5, pseudouridine 55 synthase, pseudouridine synthase, pseudouridine synthase Pus10, pseudouridine synthase TruB, pseuduridine-55 synthase, PSI synthase, PSI synthase TruB, PSI55 synthase, PSI55 synthaseuB, psi55 tRNA pseudouridine synthase, psi55S, Pus10, Pus4, RNA pseudouridine synthase TruB, TR, tRNA pseudouridine 55 synthase, tRNA pseudouridine synthase, tRNA PSI 55 synthase, tRNA:pseudouridine-55 synthase, tRNA:PSI55 synthase, tRNA:PSI55-synthase, TruB, YNL292w
ECTree
Advanced search results
Engineering
Engineering on EC 5.4.99.25 - tRNA pseudouridine55 synthase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
C174A
kcat is 1.3fold higher than wild-type value, KM is 1.1fold lower than wild-type value
C193V
kcat is 1.5fold higher than wild-type value, KM is 1.5fold higher than wild-type value
C58A
kcat is 2.2fold higher than wild-type value, KM is 1.2fold higher than wild-type value
C58A/C174A/C193A
kcat is 1.1fold lower than wild-type value, KM is 1.2fold lower than wild-type value
D90A
-
dissociation constant: 0.4 microM (wild-type: 0.7 microM), rate of pseudouridine formation compared to wild-type: 500fold decreased, rate of tRNA binding (kapp2): 2/sec (wild-type: 4.2/sec)
D90E
-
dissociation constant: 0.4 microM (wild-type: 0.7 microM), rate of pseudouridine formation compared to wild-type: 30fold decreased, rate of tRNA binding (kapp2): 1.5/sec (wild-type: 4.2/sec)
D90N
-
dissociation constant: 0.4 microM (wild-type: 0.7 microM), rate of pseudouridine formation compared to wild-type: 50fold decreased, rate of tRNA binding (kapp2): 1.9/sec (wild-type: 4.2/sec)
K19M
kcat is 8fold lower than wild-type value. KM-value is 11fold higher than wild-type value
K19R
kcat is 10fold lower than wild-type value. KM-value is 6fold higher than wild-type value
P20G
kcat is 4.8fold lower than wild-type value. KM-value is 2.2fold higher than wild-type value
P20L
kcat is 2.1fold lower than wild-type value. KM-value is 3.5fold higher than wild-type value
R181A
-
dissociation constant: 2 microM (wild-type: 0.7 microM), rate of pseudouridine formation compared to wild-type: more than 20000fold decreased, rate of tRNA binding (kapp2): 4/sec (wild-type: 4.2/sec)
R181K
-
dissociation constant: 0.7 microM (wild-type: 0.7 microM), rate of pseudouridine formation compared to wild-type: 2500fold decreased, rate of tRNA binding (kapp2): 1.9/sec (wild-type: 4.2/sec)
R181M
-
dissociation constant: 0.5 microM (wild-type: 0.7 microM), rate of pseudouridine formation compared to wild-type: more than 20000fold decreased, rate of tRNA binding (kapp2): 3/sec (wild-type: 4.2/sec)
C106A/C109A
decrease in tRNA pseudouridine54 synthase activity, no decrease in tRNA pseudouridine55 synthase activity
D275A
the mutant shows no tRNA pseudouridine54 synthase activity and no tRNA pseudouridine55 synthase activity
D277A
decrease in tRNA pseudouridine54 synthase activity and low decrease in tRNA pseudouridine55 synthase activity
H376A/R377A
decrease in tRNA pseudouridine54 synthase activity and in tRNA pseudouridine55 synthase activity
I412A
decrease in tRNA pseudouridine54 synthase activity and in tRNA pseudouridine55 synthase activity
K413A
decrease in tRNA pseudouridine54 synthase activity and in tRNA pseudouridine55 synthase activity
L440A
the mutant shows no tRNA pseudouridine54 synthase activity and no tRNA pseudouridine55 synthase activity
R273A
decrease in tRNA pseudouridine54 synthase activity and in tRNA pseudouridine55 synthase activity
Y339A
the mutant shows no tRNA pseudouridine54 synthase activity and no tRNA pseudouridine55 synthase activity
D275A
-
the mutant shows no tRNA pseudouridine54 synthase activity and no tRNA pseudouridine55 synthase activity
-
D277A
-
decrease in tRNA pseudouridine54 synthase activity and low decrease in tRNA pseudouridine55 synthase activity
-
I412A
-
decrease in tRNA pseudouridine54 synthase activity and in tRNA pseudouridine55 synthase activity
-
R273A
-
decrease in tRNA pseudouridine54 synthase activity and in tRNA pseudouridine55 synthase activity
-
Y339A
-
the mutant shows no tRNA pseudouridine54 synthase activity and no tRNA pseudouridine55 synthase activity
-
K53A
substitution K53A or R202A in aCBF5 impairs both the tRNA:pseudouridine55-synthase and the RNA-guided RNA:pseudouridine-synthase activities
R202A
substitution K53A or R202A in aCBF5 impairs both the tRNA:pseudouridine55-synthase and the RNA-guided RNA:pseudouridine-synthase activities
Y67F
no activity with the natural RNA substrate, efficient formation of 5-fluoro-6-hydroxypseudouridine55 from 5-fluorouridine55
Y67L
no activity with the natural RNA substrate, efficient formation of 5-fluoro-6-hydroxypseudouridine55 from 5-fluorouridine55
additional information
mutant enzymes with substitution of the nearly invariant lysine and proline residues in motif I of RluA display only very mild kinetic impairment. Substitution of the aligned lysine and proline residues reduces structural stability
additional information
substitution of cysteine for amino acids with nonnucleophilic side chains does not significantly alter the catalytic activity