Information on EC 2.5.1.75 - tRNA dimethylallyltransferase

Word Map on EC 2.5.1.75
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
2.5.1.75
-
RECOMMENDED NAME
GeneOntology No.
tRNA dimethylallyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
dimethylallyl diphosphate + adenine37 in tRNA = diphosphate + N6-dimethylallyladenine37 in tRNA
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alkenyl group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
-
cis-zeatin biosynthesis
-
-
Metabolic pathways
-
-
Zeatin biosynthesis
-
-
SYSTEMATIC NAME
IUBMB Comments
dimethylallyl-diphosphate: tRNA dimethylallyltransferase
Formerly known as tRNA isopentenyltransferase (EC 2.5.1.8), but it is now known that dimethylallyl diphosphate, rather than isopentenyl diphosphate, is the substrate.
CAS REGISTRY NUMBER
COMMENTARY hide
37277-78-4
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
knockdown of Trit1 reduces expression of selenoproteins. Trit1 proteins carrying the D55G or T32A mutations exhibit significantly reduced specific activity of 50% and 10%of wild-type respectively. Overexpression of TRIT1 does not increase selenoprotein expression in HepG2 cells
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
dimethylallyl diphosphate + A37 nucleoside
N6-(D2-isopentenyl)adenine + diphosphate
show the reaction diagram
-
-
-
?
dimethylallyl diphosphate + adenine37 in tRNA
diphosphate + N6-dimethylallyladenine37 in tRNA
show the reaction diagram
dimethylallyl diphosphate + adenine37 in tRNA([Ser]Sec)
diphosphate + N6-dimethylallyladenine37 in tRNA([Ser]Sec)
show the reaction diagram
dimethylallyl diphosphate + adenine37 in tRNAPhe
diphosphate + N6-dimethylallyladenine37 in tRNAPhe
show the reaction diagram
-
-
enzyme transfers the dimethylallyl moiety of dimethylallyl diphosphate to A37, located adjacent to the anticodon in undermodified tRNAPhe
-
?
dimethylallyl diphosphate + adenine37 in tRNATrp
diphosphate + N6-dimethylallyladenine37 in tRNATrp
show the reaction diagram
dimethylallyl diphosphate + adenosine 37 in tRNACys
N6-(dimethylallyl)adenosine37 in tRNACys + diphosphate
show the reaction diagram
-
-
-
-
?
dimethylallyl diphosphate + adenosine 37 in tRNASer
N6-(dimethylallyl)adenosine37 in tRNASer + diphosphate
show the reaction diagram
dimethylallyl diphosphate + adenosine 37 in tRNATrpCCA
N6-(dimethylallyl)adenosine37 in tRNATrpCCA + diphosphate
show the reaction diagram
dimethylallyl diphosphate + adenosine 37 in tRNATyr
N6-(dimethylallyl)adenosine37 in tRNATyr + diphosphate
show the reaction diagram
-
-
-
-
?
dimethylallyl diphosphate + adenosine 37 in tRNATyrGUA
N6-(dimethylallyl)adenosine37 in tRNATyrGUA + diphosphate
show the reaction diagram
-
-
-
?
dimethylallyl diphosphate + adenosine37 in tRNATrpCCA
N6-(dimethylallyl)adenosine37 in tRNATrpCCA + diphosphate
show the reaction diagram
-
-
-
-
?
dimethylallyl diphosphate + GCGGACUCAAAAUCCGC
diphosphate + GCGGACUCAAAAUCCGC containing 6-dimethylallyladenosine
show the reaction diagram
-
chemically synthesized 17-base RNA oligoribonucleotide minihelix based on variations in the anticodon stem-loop of unmodified Escherichia coli tRNAPhe
-
-
?
dimethylallyl diphosphate + GGCCAUUGAAAAUGGCC
diphosphate + GGCCAUUGAAAAUGGCC containing 6-dimethylallyladenosine
show the reaction diagram
-
chemically synthesized 17-base RNA oligoribonucleotide minihelix based on variations in the anticodon stem-loop of unmodified Escherichia coli tRNAPhe
-
-
?
dimethylallyl diphosphate + GGGAAUUGAAAAUUCCC
diphosphate + GGCCAUUGAAAAUGGCC containing 6-dimethylallyladenosine
show the reaction diagram
-
chemically synthesized 17-base RNA oligoribonucleotide minihelix based on variations in the anticodon stem-loop of unmodified Escherichia coli tRNAPhe
-
-
?
dimethylallyl diphosphate + GGGCAUUGAAAAUGCCC
diphosphate + GGGCAUUGAAAAUGCCC containing 6-dimethylallyladenosine
show the reaction diagram
-
chemically synthesized 17-base RNA oligoribonucleotide minihelix based on variations in the anticodon stem-loop of unmodified Escherichia coli tRNAPhe
-
-
?
dimethylallyl diphosphate + GGGGAUUGAAAAAGGGG
diphosphate + GGGGAUUGAAAAAGGGG containing 6-dimethylallyladenosine
show the reaction diagram
-
chemically synthesized 17-base RNA random coil oligoribonucleotide based on variations in the anticodon stem-loop of unmodified Escherichia coli tRNAPhe
-
-
?
dimethylallyl diphosphate + GGGGAUUGAAAAUCCCC
diphosphate + GGGGAUUGAAAAAGGGG containing 6-dimethylallyladenosine
show the reaction diagram
-
chemically synthesized 17-base RNA oligoribonucleotide minihelix based on variations in the anticodon stem-loop of unmodified Escherichia coli tRNAPhe
-
-
?
dimethylallyl diphosphate + GGGGAUUGAAAGUCCCC
diphosphate + GGGGAUUGAAAGUCCCC containing 6-dimethylallyladenosine
show the reaction diagram
-
chemically synthesized 17-base RNA oligoribonucleotide minihelix based on variations in the anticodon stem-loop of unmodified Escherichia coli tRNAPhe
-
-
?
dimethylallyl diphosphate + GGGGAUUGAGAAUCCCC
diphosphate + GGGGAUUGAGAAUCCCC containing 6-dimethylallyladenosine
show the reaction diagram
-
chemically synthesized 17-base RNA oligoribonucleotide minihelix based on variations in the anticodon stem-loop of unmodified Escherichia coli tRNAPhe
-
-
?
dimethylallyl diphosphate + GGGGGUUGAAAACCCCC
diphosphate + GGGGGUUGAAAACCCCC containing 6-dimethylallyladenosine
show the reaction diagram
-
chemically synthesized 17-base RNA oligoribonucleotide minihelix based on variations in the anticodon stem-loop of unmodified Escherichia coli tRNAPhe
-
-
?
dimethylallyl diphosphate + oligo-RNA
oligo-RNA containing N6-(dimethylallyl)adenosine + diphosphate
show the reaction diagram
substrates are 17-nt or 19-nt synthetic oligo-RNAs representing anticondon stem-loops as minihelix analogs of tRNAs. Only the anticodon stem-loops with a predicted stem of 6 bp are efficiently modified
-
-
?
dimethylallyl diphosphate + seventeen-base RNA oligonucleotide
diphosphate + seventeen-base RNA oligonucleotide containing 6-dimethylallyladenosine
show the reaction diagram
-
sequence 5'GCGGACUCAAAAUCCGC3', RNA oligonucleotide based on the unmodified stem-loop region of tRNAPhe
-
-
?
dimethylallyl diphosphate + tRNATrpCCA
tRNATrpCCA containing N6-(dimethylallyl)adenosine + diphosphate
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
dimethylallyl diphosphate + adenine37 in tRNA
diphosphate + N6-dimethylallyladenine37 in tRNA
show the reaction diagram
dimethylallyl diphosphate + adenine37 in tRNA([Ser]Sec)
diphosphate + N6-dimethylallyladenine37 in tRNA([Ser]Sec)
show the reaction diagram
Q80UN9
-
-
-
?
dimethylallyl diphosphate + tRNATrpCCA
tRNATrpCCA containing N6-(dimethylallyl)adenosine + diphosphate
show the reaction diagram
Q9UT75
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Divalent cation
-
required for full activity
Zn2+
-
sequence contains a C2H2 Zn-finger-like motif
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ADP
-
competitive to DELTA2-isopentenyl diphosphate
ATP
-
competitive to DELTA2-isopentenyl diphosphate
diphosphate
High ionic strength
-
-
-
iodoacetamide
-
-
p-mercuribenzoate
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000632 - 0.003
DELTA2-isopentenyl diphosphate
0.0032 - 114
dimethylallyl diphosphate
0.0065
GCGGACUCAAAAUCCGC
-
pH 7.5, 37C
-
0.0045
GGCCAUUGAAAAUGGCC
-
pH 7.5, 37C
-
0.022
GGGAAUUGAAAAUUCCC
-
pH 7.5, 37C
-
0.012
GGGCAUUGAAAAUGCCC
-
pH 7.5, 37C
-
0.019
GGGGAUUGAAAAAGGGG
-
pH 7.5, 37C
-
0.0047
GGGGAUUGAAAAUCCCC
-
pH 7.5, 37C
-
0.0033
GGGGAUUGAAAGUCCCC
-
pH 7.5, 37C
-
0.0031
GGGGAUUGAGAAUCCCC
-
pH 7.5, 37C
-
0.059
GGGGGUUGAAAACCCCC
-
pH 7.5, 37C
-
1.5 - 75
seventeen-base RNA oligonucleotide
-
0.013
tRNA
-
from Lactobacillus
0.000096
tRNAPhe
-
pH 7.5, 37C
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.26
GCGGACUCAAAAUCCGC
Escherichia coli
-
pH 7.5, 37C
-
0.67
GGCCAUUGAAAAUGGCC, GGGAAUUGAAAAUUCCC
Escherichia coli
-
pH 7.5, 37C
-
0.79
GGGCAUUGAAAAUGCCC
Escherichia coli
-
pH 7.5, 37C
-
0.001
GGGGAUUGAAAAAGGGG
Escherichia coli
-
pH 7.5, 37C
-
1
GGGGAUUGAAAAUCCCC
Escherichia coli
-
pH 7.5, 37C
-
0.0039
GGGGAUUGAAAGUCCCC
Escherichia coli
-
pH 7.5, 37C
-
0.75
GGGGAUUGAGAAUCCCC
Escherichia coli
-
pH 7.5, 37C
-
0.111
GGGGGUUGAAAACCCCC
Escherichia coli
-
pH 7.5, 37C
-
0.002 - 0.3
seventeen-base RNA oligonucleotide
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.15
-
pH 7.5, 37C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 9
-
broad
7.5
assay at
7.8
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
-
about 50% of maximum activity at pH 6 and pH 9, below pH 5 activity is totally abolished
7 - 9.5
-
pH 7: about 95% of maximum activity, pH 9.5: about 45% of maximum activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
normal and tumor tissue
Manually annotated by BRENDA team
-
only a tenth compared with leaves
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
only a fifth compared with leaves
Manually annotated by BRENDA team
additional information
-
ubiquitous expression, highest in proliferating tissue
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Staphylococcus epidermidis (strain ATCC 12228)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
34700
-
1 * 34700, SDS-PAGE
37300
-
calculated
37800
-
gel fitlration
60000
-
gel filtration, SDS-PAGE
62000
calculated from amino acid sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
The crystal structure of the AIPT-ATP complex from Humulus lupulus is similar to the previous structures of Agrobacterium AIPT and yeast tRNA-IPT. The enzyme is structurally homologous to the NTP-binding kinase family of proteins but forms a solvent-accessible channel that binds to the donor substrate dimethylallyl diphosphate, which is directed toward the acceptor substrate ATP/ADP.
DMATase-tRNACys complex in four distinct forms, which provide snapshots of the RNA modification reaction catalyzed by DMATase
-
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
not stable to ammonium sulfate precipitation
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-18C, 0.59 mg bovine serum albumin/ml, 50% glycerol, purified enzyme loses 80% of activity after 14 days
-
-18C, 50% glycerol, partially purified enzyme stable for 3 months
-
-78C, stable for several months
-
0C, stable for 1 month
-
0C, stable for at least one week
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DEAE-cellulose chromatography
partial
recombinant enzyme
-
recombinant expression of His-tagged enzyme from Escherichia coli by nickel affinity chromatography
recombinant MBP-tagged enzyme from Escherichia coli strain BL21(DE3) by amylose affinity chromatography, tag cleavage by TEV protease, and
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Nicotiana tabacum cultivar Wisconsin 38
-
expressed in Petunia hybrida under control of the flowerspecific Arabidopsis AP3 promoter
-
expressed in Saccharomyces cerevisiae strain MT-8
expressed in transgenic Nicotiana tabacum cv. Wisconsin 38, transcripts are found in leaves and stem but not in root
-
gene miaA, DNA and amino acid sequence determination and analysis, recombinant expression of the enzyme as maltose-binding-protein fusion protein in Escherichia coli strain BL21(DE3)
overexpressed as a N-terminal hexahistidine tag protein in Escherichia coli BL21 (DE3)
recombinant expression of His-tagged enzyme in Escherichia coli, recombinant overexpression of enzyme TRIT1 NIH 3T3 cells, recombinant overexpression of TRIT1 in HepG2 cells
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
nitrate treatment of roots and leaves enhances amount of mRNA significantly
-
ENGINEERING
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
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
-
production of ornamental crops with large flowers and crop species with larger fruit
biotechnology
-
production of ornamental crops with large flowers and crop species with larger fruit
medicine
expression of full-length transcript is downregulated 6-14fold in lung adenocarcinomas compared to normal tissue. A549-cells transfected to express the functional enzyme form significantly smaller colonies with reduced scattering on the edges and have only limited ability to induce tumors in nude mice
Show AA Sequence (15298 entries)
Longer loading times are possible. Please use the Sequence Search for a specific query.