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2.5.1.75: tRNA dimethylallyltransferase

This is an abbreviated version!
For detailed information about tRNA dimethylallyltransferase, go to the full flat file.

Word Map on EC 2.5.1.75

Reaction

dimethylallyl diphosphate
+
adenine37 in tRNA
=
diphosphate
+
N6-dimethylallyladenine37 in tRNA

Synonyms

A37 isopentenyltransferase, alr5266, DELTA2-isopentenyl pyrophosphate:transfer ribonucleic acid DELTA2-isopentenyltransferase, DELTA2-isopentenyl pyrophosphate:tRNA-DELTA2-isopentenyl transferase, dimethylallyl (DELTA2-isopentenyl)diphosphate-tRNA transferase, dimethylallyl(D2-isopentenyl) diphosphate:tRNA transferase, dimethylallyl:tRNA[Ser]Sec transferase, DMAPP:tRNA[Ser]Sec transferase, DMATase, EC 2.5.1.8, IPT, IPT2, IPT9, isopentenyl transferase, isopentenyltransferase, isopentenyltransferase, transfer ribonucleate, MhIPT3, MiaA, Mod5, NoIPT2, prenyltransferase, Tit1, transfer ribonucleate isopentenyltransferase, TRIT1, tRNA IPT, tRNA isopentenyltransferase, tRNA([Ser]Sec)-isopentenyl transferase, tRNA-IPT, tRNA-IPT1

ECTree

     2 Transferases
         2.5 Transferring alkyl or aryl groups, other than methyl groups
             2.5.1 Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date)
                2.5.1.75 tRNA dimethylallyltransferase

Engineering

Engineering on EC 2.5.1.75 - tRNA dimethylallyltransferase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D153A
-
at least 25% of wild-type activity
D164A
-
increase in Km for both substrates
D42A
-
20fold decrease in kcat
E173A
-
at least 25% of wild-type activity
E229A
-
substantial increase in Km for RNA, dimethylallyl diphosphate becomes inhibitory at higher concentrations
F84A
-
at least 25% of wild-type activity
H67F
-
25fold increase in Km for dimethylallyl diphosphate
K23A
-
increase in Km for both substrates
K280A
-
increase in Km for both substrates
K56A
-
15fold increase in Km for RNA, dimethylallyl diphosphate becomes inhibitory at higher concentrations
Q253A
-
18fold increase in Km for RNA, dimethylallyl diphosphate becomes inhibitory at higher concentrations
Q282A
-
increase in both Km and kcat value
R167A
-
increase in Km for both substrates
R170A
-
increase in Km for both substrates
R213A
-
at least 25% of wild-type activity
R217A
-
increase in Km and decrease in kcat for dimethylallyl diphosphate
R281A
-
at least 25% of wild-type activity
S178A
-
at least 25% of wild-type activity
S43A
-
at least 25% of wild-type activity
T108A
-
increase in Km for both substrates
T19A
-
about 600fold decrease in kcat
T24A
-
increase in Km for both substrates
T275A
-
at least 25% of wild-type activity
T54A
-
increase in Km for both substrates
W285A
-
at least 25% of wild-type activity
Y111F
-
at least 25% of wild-type activity
Y111S
-
at least 25% of wild-type activity
Y47F
-
at least 25% of wild-type activity
Y47S
-
100fold decrease in kcat
R17E
mutation in the basic amphipathic helix component of the predicted mitochondrial targeting sequence, mutant accumulates mostly in nuclei and is not found to localize to mitochondria. Mutation decreases modification of mitochondrial but not cytosolic tRNAs upon expression in both Saccharomyces cerevisiae and Schizosaccharomyces pombe
R21E
mutation in the basic amphipathic helix component of the predicted mitochondrial targeting sequence, mutant accumulates mostly in nuclei and is not found to localize to mitochondria. Mutation decreases modification of mitochondrial but not cytosolic tRNAs upon expression in both Saccharomyces cerevisiae and Schizosaccharomyces pombe
T32A
mutant is inactive on both the mitochondrial and cytosolic tRNA substrates
D55G
site-directed mutagenesis, the mutant shows 50% reduced specific activity compared to the wild-type enzyme
T32A
site-directed mutagenesis, the mutant shows 90% reduced specific activity compared to the wild-type enzyme
K127D
activity similar to wild-type
K181H
selective disproportionate decrease in activity toward several substrates
Y84S
activity similar to wild-type
additional information