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Information on EC 2.5.1.75 - tRNA dimethylallyltransferase
for references in articles please use BRENDA:EC2.5.1.75
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EC Tree 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
IUBMB Comments
Formerly known as tRNA isopentenyltransferase, but it is now known that prenyl diphosphate, rather than isopentenyl diphosphate, is the substrate.
The enzyme appears in viruses and cellular organisms
- 2.5.1.75
-
prenylation
-
farnesylation
-
geranylgeranylated
-
isopentenylation
-
isoprenoids
-
geranyl
-
farnesyltransferase
-
ubiad1
-
geranylgeranyltransferase
-
isoprenylation
- isoprene
-
meroterpenoids
-
schnyder
-
neosartorya
-
polyprenyl
-
aspartate-rich
- ftase
- menaquinone-4
- undecaprenyl
- dimethylallyltryptophan
-
tryptophan-containing
- agriculture
- glyceollins
- medicine
- dmats
-
nonsterol
- biotechnology
Reaction Schemes
show+
adenosine37 in tRNA
=
+
N6-(3-methylbut-2-en-1-yl)-adenosine37 in tRNA
Synonyms
prenyltransferase, trit1, trna isopentenyltransferase, trna-ipt, dmatase, trna ipt, mhipt3, noipt2, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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-diphosphate:adenine37 in tRNA dimethylallyltransferase
-
-
-
-
EC 2.5.1.8
-
-
formerly
-
IPT
isopentenyltransferase
isopentenyltransferase, transfer ribonucleate
-
-
-
-
MiaA
Mod5
transfer ribonucleate isopentenyltransferase
-
-
-
-
TRIT1
dimethylallyl (DELTA2-isopentenyl)diphosphate-tRNA transferase
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
prenyl diphosphate + adenosine37 in tRNA = diphosphate + N6-(3-methylbut-2-en-1-yl)-adenosine37 in tRNA
prenyl diphosphate + adenosine37 in tRNA = diphosphate + N6-(3-methylbut-2-en-1-yl)-adenosine37 in tRNA
mechanism
-
prenyl diphosphate + adenosine37 in tRNA = diphosphate + N6-(3-methylbut-2-en-1-yl)-adenosine37 in tRNA
ordered substrate binding
prenyl diphosphate + adenosine37 in tRNA = diphosphate + N6-(3-methylbut-2-en-1-yl)-adenosine37 in tRNA
ordered sequential mechanism for substrate binding
-
prenyl diphosphate + adenosine37 in tRNA = diphosphate + N6-(3-methylbut-2-en-1-yl)-adenosine37 in tRNA
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
alkenyl group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
cis-zeatin biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
prenyl-diphosphate:adenine37 in tRNA prenyltransferase
Formerly known as tRNA isopentenyltransferase, but it is now known that prenyl diphosphate, rather than isopentenyl diphosphate, is the substrate.
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CAS REGISTRY NUMBER
COMMENTARY
37277-78-4
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
dimethylallyl diphosphate + A37 nucleoside
N6-(D2-isopentenyl)adenine + diphosphate
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + adenine37 in tRNA
diphosphate + N6-dimethylallyladenine37 in tRNA
dimethylallyl diphosphate + adenine37 in tRNA([Ser]Sec)
diphosphate + N6-dimethylallyladenine37 in tRNA([Ser]Sec)
dimethylallyl diphosphate + adenine37 in tRNAPhe
diphosphate + N6-dimethylallyladenine37 in tRNAPhe
-
Substrates: -
Products: enzyme transfers the dimethylallyl moiety of dimethylallyl diphosphate to A37, located adjacent to the anticodon in undermodified tRNAPhe
Products: 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
dimethylallyl diphosphate + adenosine 37 in tRNA
N6-(dimethylallyl)adenosine37 in tRNA + diphosphate
-
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + adenosine 37 in tRNA-Phe
N6-(dimethylallyl)adenosine37 in tRNAPhe + diphosphate
-
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + adenosine 37 in tRNACys
N6-(dimethylallyl)adenosine37 in tRNACys + diphosphate
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + adenosine 37 in tRNASer
N6-(dimethylallyl)adenosine37 in tRNASer + diphosphate
dimethylallyl diphosphate + adenosine 37 in tRNATrpCCA
N6-(dimethylallyl)adenosine37 in tRNATrpCCA + diphosphate
dimethylallyl diphosphate + adenosine 37 in tRNATyr
N6-(dimethylallyl)adenosine37 in tRNATyr + diphosphate
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + adenosine 37 in tRNATyrGUA
N6-(dimethylallyl)adenosine37 in tRNATyrGUA + diphosphate
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + adenosine37 in tRNATrpCCA
N6-(dimethylallyl)adenosine37 in tRNATrpCCA + diphosphate
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + GCGGACUCAAAAUCCGC
diphosphate + GCGGACUCAAAAUCCGC containing 6-dimethylallyladenosine
-
Substrates: chemically synthesized 17-base RNA oligoribonucleotide minihelix based on variations in the anticodon stem-loop of unmodified Escherichia coli tRNAPhe
Products: -
Products: -
?
dimethylallyl diphosphate + GGCCAUUGAAAAUGGCC
diphosphate + GGCCAUUGAAAAUGGCC containing 6-dimethylallyladenosine
-
Substrates: chemically synthesized 17-base RNA oligoribonucleotide minihelix based on variations in the anticodon stem-loop of unmodified Escherichia coli tRNAPhe
Products: -
Products: -
?
dimethylallyl diphosphate + GGGAAUUGAAAAUUCCC
diphosphate + GGCCAUUGAAAAUGGCC containing 6-dimethylallyladenosine
-
Substrates: chemically synthesized 17-base RNA oligoribonucleotide minihelix based on variations in the anticodon stem-loop of unmodified Escherichia coli tRNAPhe
Products: -
Products: -
?
dimethylallyl diphosphate + GGGCAUUGAAAAUGCCC
diphosphate + GGGCAUUGAAAAUGCCC containing 6-dimethylallyladenosine
-
Substrates: chemically synthesized 17-base RNA oligoribonucleotide minihelix based on variations in the anticodon stem-loop of unmodified Escherichia coli tRNAPhe
Products: -
Products: -
?
dimethylallyl diphosphate + GGGGAUUGAAAAAGGGG
diphosphate + GGGGAUUGAAAAAGGGG containing 6-dimethylallyladenosine
-
Substrates: chemically synthesized 17-base RNA random coil oligoribonucleotide based on variations in the anticodon stem-loop of unmodified Escherichia coli tRNAPhe
Products: -
Products: -
?
dimethylallyl diphosphate + GGGGAUUGAAAAUCCCC
diphosphate + GGGGAUUGAAAAAGGGG containing 6-dimethylallyladenosine
-
Substrates: chemically synthesized 17-base RNA oligoribonucleotide minihelix based on variations in the anticodon stem-loop of unmodified Escherichia coli tRNAPhe
Products: -
Products: -
?
dimethylallyl diphosphate + GGGGAUUGAAAGUCCCC
diphosphate + GGGGAUUGAAAGUCCCC containing 6-dimethylallyladenosine
-
Substrates: chemically synthesized 17-base RNA oligoribonucleotide minihelix based on variations in the anticodon stem-loop of unmodified Escherichia coli tRNAPhe
Products: -
Products: -
?
dimethylallyl diphosphate + GGGGAUUGAGAAUCCCC
diphosphate + GGGGAUUGAGAAUCCCC containing 6-dimethylallyladenosine
-
Substrates: chemically synthesized 17-base RNA oligoribonucleotide minihelix based on variations in the anticodon stem-loop of unmodified Escherichia coli tRNAPhe
Products: -
Products: -
?
dimethylallyl diphosphate + GGGGGUUGAAAACCCCC
diphosphate + GGGGGUUGAAAACCCCC containing 6-dimethylallyladenosine
-
Substrates: chemically synthesized 17-base RNA oligoribonucleotide minihelix based on variations in the anticodon stem-loop of unmodified Escherichia coli tRNAPhe
Products: -
Products: -
?
dimethylallyl diphosphate + oligo-RNA
oligo-RNA containing N6-(dimethylallyl)adenosine + diphosphate
Substrates: 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
Products: -
Products: -
?
dimethylallyl diphosphate + seventeen-base RNA oligonucleotide
diphosphate + seventeen-base RNA oligonucleotide containing 6-dimethylallyladenosine
-
Substrates: sequence 5'GCGGACUCAAAAUCCGC3', RNA oligonucleotide based on the unmodified stem-loop region of tRNAPhe
Products: -
Products: -
?
dimethylallyl diphosphate + tRNATrpCCA
tRNATrpCCA containing N6-(dimethylallyl)adenosine + diphosphate
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + adenine37 in tRNA
diphosphate + N6-dimethylallyladenine37 in tRNA
-
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + adenine37 in tRNA
diphosphate + N6-dimethylallyladenine37 in tRNA
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + adenine37 in tRNA
diphosphate + N6-dimethylallyladenine37 in tRNA
-
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + adenine37 in tRNA
diphosphate + N6-dimethylallyladenine37 in tRNA
-
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + adenine37 in tRNA
diphosphate + N6-dimethylallyladenine37 in tRNA
-
Substrates: regulates global physiology by unknown mechanisms
Products: -
Products: -
?
dimethylallyl diphosphate + adenine37 in tRNA
diphosphate + N6-dimethylallyladenine37 in tRNA
-
Substrates: tRNA lacking the isopentenyl modification normally present in vivo
Products: -
Products: -
?
dimethylallyl diphosphate + adenine37 in tRNA
diphosphate + N6-dimethylallyladenine37 in tRNA
-
Substrates: specific for DELTA2-isopentenyl phosphate
Products: -
Products: -
?
dimethylallyl diphosphate + adenine37 in tRNA
diphosphate + N6-dimethylallyladenine37 in tRNA
-
Substrates: mycoplasma species (kid) tRNA
Products: -
Products: -
?
dimethylallyl diphosphate + adenine37 in tRNA
diphosphate + N6-dimethylallyladenine37 in tRNA
-
Substrates: no reaction with DELTA3-isopentenyl diphosphate
Products: -
Products: -
?
dimethylallyl diphosphate + adenine37 in tRNA
diphosphate + N6-dimethylallyladenine37 in tRNA
-
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + adenine37 in tRNA
diphosphate + N6-dimethylallyladenine37 in tRNA
-
Substrates: recognition mode of substrate, structural features of substrate tRNA
Products: -
Products: -
?
dimethylallyl diphosphate + adenine37 in tRNA
diphosphate + N6-dimethylallyladenine37 in tRNA
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + adenine37 in tRNA
diphosphate + N6-dimethylallyladenine37 in tRNA
Substrates: -
Products: -
Products: -
ir
dimethylallyl diphosphate + adenine37 in tRNA
diphosphate + N6-dimethylallyladenine37 in tRNA
-
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + adenine37 in tRNA
diphosphate + N6-dimethylallyladenine37 in tRNA
Substrates: -
Products: -
Products: -
ir
dimethylallyl diphosphate + adenine37 in tRNA
diphosphate + N6-dimethylallyladenine37 in tRNA
-
Substrates: specific for DELTA2-isopentenyl phosphate
Products: -
Products: -
?
dimethylallyl diphosphate + adenine37 in tRNA
diphosphate + N6-dimethylallyladenine37 in tRNA
-
Substrates: no reaction with DELTA3-isopentenyl diphosphate
Products: -
Products: -
?
dimethylallyl diphosphate + adenine37 in tRNA
diphosphate + N6-dimethylallyladenine37 in tRNA
-
Substrates: no reaction with homologous native tRNA or homologous, permanganate-treated tRNA (permanganate specifically cleaves the DELTA2-isopentenyl groups of tRNA leaving adenosine residues)
Products: -
Products: -
?
dimethylallyl diphosphate + adenine37 in tRNA
diphosphate + N6-dimethylallyladenine37 in tRNA
-
Substrates: the enzyme from both yeast and rat liver catalyzes a significant incorporation of DELTA2-isopentenyl groups into untreated E. coli B tRNA
Products: -
Products: -
?
dimethylallyl diphosphate + adenine37 in tRNA
diphosphate + N6-dimethylallyladenine37 in tRNA
-
Substrates: biosynthesis of N6-(DELTA2-isopentenyl)adenosine which several species of tRNA contain adjacent to the 3'-end of the anticodon
Products: -
Products: -
?
dimethylallyl diphosphate + adenine37 in tRNA
diphosphate + N6-dimethylallyladenine37 in tRNA
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + adenine37 in tRNA
diphosphate + N6-dimethylallyladenine37 in tRNA
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + adenine37 in tRNA
diphosphate + N6-dimethylallyladenine37 in tRNA
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + adenine37 in tRNA
diphosphate + N6-dimethylallyladenine37 in tRNA
-
Substrates: no reaction with DELTA3-isopentenyl diphosphate
Products: -
Products: -
?
dimethylallyl diphosphate + adenine37 in tRNA([Ser]Sec)
diphosphate + N6-dimethylallyladenine37 in tRNA([Ser]Sec)
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + adenine37 in tRNA([Ser]Sec)
diphosphate + N6-dimethylallyladenine37 in tRNA([Ser]Sec)
Substrates: tRNA[Ser]Sec modification assay with [14C]DMAPP and in vitro transcribed tRNA[Ser]Sec. Incubation of in vitro transcribed tRNA[Ser]Sec with recombinant Trit1 transfers [14C]dimethylallyl diphosphate to tRNA[Ser]Sec reveals that 37A>G tRNA[Ser]Sec is resistant to isopentenylation by Trit1
Products: -
Products: -
?
dimethylallyl diphosphate + adenine37 in tRNATrp
diphosphate + N6-dimethylallyladenine37 in tRNATrp
Substrates: isopentenylaion of the A37 within the ACSLTrp sequence, detailed spectrometrical reaction analysis, overview
Products: -
Products: -
?
dimethylallyl diphosphate + adenine37 in tRNATrp
diphosphate + N6-dimethylallyladenine37 in tRNATrp
Substrates: isopentenylaion of the A37 within the ACSLTrp sequence, detailed spectrometrical reaction analysis, overview
Products: -
Products: -
?
dimethylallyl diphosphate + adenosine 37 in tRNASer
N6-(dimethylallyl)adenosine37 in tRNASer + diphosphate
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + adenosine 37 in tRNASer
N6-(dimethylallyl)adenosine37 in tRNASer + diphosphate
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + adenosine 37 in tRNATrpCCA
N6-(dimethylallyl)adenosine37 in tRNATrpCCA + diphosphate
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + adenosine 37 in tRNATrpCCA
N6-(dimethylallyl)adenosine37 in tRNATrpCCA + diphosphate
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: The A36-A37-A38 motif, which is completely conserved in tRNAs modified by the enzyme, is important for modification. A helix-loop structure is essential for recognition
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme does not bind dimethylallyl diphosphate in absence of tRNA
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme recognizes the tRNA substrate through indirect sequence readout. The targeted nucleotide A37 flips out from the anticodon loop of tRNA and flips into a channel in DMATase, where it meets its reaction partner dimethylallyl diphosphate, which enters the channel from the opposite end. Structural changes accompanying the transfer reaction result in disengagement of DMATase-tRNA interaction near the reaction center
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme recognizes the tRNA substrate through indirect sequence readout. The targeted nucleotide A37 flips out from the anticodon loop of tRNA and flips into a channel in DMATase, where it meets its reaction partner dimethylallyl diphosphate, which enters the channel from the opposite end. Structural changes accompanying the transfer reaction result in disengagement of DMATase-tRNA interaction near the reaction center
Products: -
Products: -
?
additional information
?
-
Substrates: the minimal substrate for bacterial MiaA is the anticodon stem loop (ACSL) of targeted tRNA molecules
Products: -
Products: -
?
additional information
?
-
Substrates: the minimal substrate for bacterial MiaA is the anticodon stem loop (ACSL) of targeted tRNA molecules
Products: -
Products: -
?
additional information
?
-
Substrates: anticondon stem-loops with substitutions as in Ser-G36, Ser-G37, and Ser-G36,G38 greatly diminish activity, and Ser-C38 and Ser-U38 are not modified, while Ser-G38 is a substrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: anticondon stem-loops with substitutions as in Ser-G36, Ser-G37, and Ser-G36,G38 greatly diminish activity, and Ser-C38 and Ser-U38 are not modified, while Ser-G38 is a substrate
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
dimethylallyl diphosphate + adenine37 in tRNA
diphosphate + N6-dimethylallyladenine37 in tRNA
dimethylallyl diphosphate + adenine37 in tRNA([Ser]Sec)
diphosphate + N6-dimethylallyladenine37 in tRNA([Ser]Sec)
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + tRNATrpCCA
tRNATrpCCA containing N6-(dimethylallyl)adenosine + diphosphate
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + adenine37 in tRNA
diphosphate + N6-dimethylallyladenine37 in tRNA
-
Substrates: regulates global physiology by unknown mechanisms
Products: -
Products: -
?
dimethylallyl diphosphate + adenine37 in tRNA
diphosphate + N6-dimethylallyladenine37 in tRNA
Substrates: -
Products: -
Products: -
ir
dimethylallyl diphosphate + adenine37 in tRNA
diphosphate + N6-dimethylallyladenine37 in tRNA
-
Substrates: biosynthesis of N6-(DELTA2-isopentenyl)adenosine which several species of tRNA contain adjacent to the 3'-end of the anticodon
Products: -
Products: -
?
dimethylallyl diphosphate + adenine37 in tRNA
diphosphate + N6-dimethylallyladenine37 in tRNA
Substrates: -
Products: -
Products: -
?
dimethylallyl diphosphate + adenine37 in tRNA
diphosphate + N6-dimethylallyladenine37 in tRNA
Substrates: -
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Adenocarcinoma of Lung
Ethnic differences in frequencies of gene polymorphisms in the MYCL1 region and modulation of lung cancer patients' survival.
African Swine Fever
The African swine fever virus prenyltransferase is an integral membrane trans-geranylgeranyl-diphosphate synthase.
Arthritis, Rheumatoid
Protein isoprenylation regulates secretion of matrix metalloproteinase 1 from rheumatoid synovial fibroblasts: effects of statins and farnesyl and geranylgeranyl transferase inhibitors.
Cardiomegaly
UBIAD1 expression is associated with cardiac hypertrophy in spontaneously hypertensive rats.
Cardiovascular Diseases
Depletion of ubiA prenyltransferase domain containing 1 expression promotes angiotensin II?induced hypertrophic response in AC16 human myocardial cells via modulating the expression levels of coenzyme Q10 and endothelial nitric oxide synthase.
Choroideremia
Dual chemical probes enable quantitative system-wide analysis of protein prenylation and prenylation dynamics.
Corneal Dystrophies, Hereditary
A Mouse Model of Schnyder Corneal Dystrophy with the N100S Point Mutation.
Corneal Dystrophies, Hereditary
A mutation in the UBIAD1 gene in a Han Chinese family with Schnyder corneal dystrophy.
Corneal Dystrophies, Hereditary
In Vivo Laser Confocal Microscopy Findings and Mutational Analysis for Schnyder's Crystalline Corneal Dystrophy.
Corneal Dystrophies, Hereditary
Long-Term Outcome After Penetrating Keratoplasty in a Pedigree With the G177E Mutation in the UBIAD1 Gene for Schnyder Corneal Dystrophy.
Corneal Dystrophies, Hereditary
Mutations in the UBIAD1 gene, encoding a potential prenyltransferase, are causal for Schnyder crystalline corneal dystrophy.
Corneal Dystrophies, Hereditary
Phenotype-genotype correlation in patients with schnyder corneal dystrophy.
Corneal Dystrophies, Hereditary
Schnyder Corneal Dystrophy-Associated UBIAD1 is Defective in MK-4 Synthesis and Resists Autophagy-Mediated Degradation.
Corneal Dystrophies, Hereditary
Structure of a membrane-embedded prenyltransferase homologous to UBIAD1.
Corneal Dystrophies, Hereditary
UBIAD1 mutation alters a mitochondrial prenyltransferase to cause Schnyder corneal dystrophy.
creatine kinase deficiency
Manipulation of cytokinin level in the ergot fungus Claviceps purpurea emphasizes its contribution to virulence.
Epilepsies, Myoclonic
Noninvasive diagnosis of TRIT1-related mitochondrial disorder by measuring i6 A37 and ms2 i6 A37 modifications in tRNAs from blood and urine samples.
Epilepsy
Matchmaking facilitates the diagnosis of an autosomal-recessive mitochondrial disease caused by biallelic mutation of the tRNA isopentenyltransferase (TRIT1) gene.
Genetic Diseases, Inborn
Structure of a membrane-embedded prenyltransferase homologous to UBIAD1.
Hepatitis C
Prenyltransferase Inhibitors: Treating Human Ailments from Cancer to Parasitic Infections.
Hypercholesterolemia
The tumor suppressor TERE1 (UBIAD1) prenyltransferase regulates the elevated cholesterol phenotype in castration resistant prostate cancer by controlling a program of ligand dependent SXR target genes.
Infections
Further investigations of race:cultivar-specific induction of enzymes related to phytoalexin biosynthesis in soybean roots following infection with Phytophthora megasperma f.sp. glycinea.
Ischemic Stroke
Effect of Coenzyme Q10 on Expression of UbiAd1 Gene in Rat Model of Local Cerebral Ischemia.
Leukemia, Myeloid, Acute
Is there a future for prenyltransferase inhibitors in cancer therapy?
Lung Neoplasms
Ethnic differences in frequencies of gene polymorphisms in the MYCL1 region and modulation of lung cancer patients' survival.
Lung Neoplasms
Gene Amplification-Associated Overexpression of the Selenoprotein tRNA Enzyme TRIT1 Confers Sensitivity to Arsenic Trioxide in Small-Cell Lung Cancer.
Lung Neoplasms
Identification and functional characterization of the candidate tumor suppressor gene TRIT1 in human lung cancer.
Lymphatic Metastasis
Association of polymorphisms and haplotype in the region of TRIT1, MYCL1 and MFSD2A with the risk and clinicopathological features of gastric cancer in a southeast Chinese population.
Malaria
Global proteomic analysis of prenylated proteins in Plasmodium falciparum using an alkyne-modified isoprenoid analogue.
Melanoma
Antimelanoma CTL recognizes peptides derived from an ORF transcribed from the antisense strand of the 3' untranslated region of TRIT1.
Microcephaly
Matchmaking facilitates the diagnosis of an autosomal-recessive mitochondrial disease caused by biallelic mutation of the tRNA isopentenyltransferase (TRIT1) gene.
Mitochondrial Diseases
Matchmaking facilitates the diagnosis of an autosomal-recessive mitochondrial disease caused by biallelic mutation of the tRNA isopentenyltransferase (TRIT1) gene.
Mitochondrial Diseases
Noninvasive diagnosis of TRIT1-related mitochondrial disorder by measuring i6 A37 and ms2 i6 A37 modifications in tRNAs from blood and urine samples.
Mitochondrial Diseases
The first Korean cases of combined oxidative phosphorylation deficiency 35 with two novel TRIT1 mutations in two siblings confirmed by clinical and molecular investigation.
Neoplasm Metastasis
Association of polymorphisms and haplotype in the region of TRIT1, MYCL1 and MFSD2A with the risk and clinicopathological features of gastric cancer in a southeast Chinese population.
Neoplasms
Antimelanoma CTL recognizes peptides derived from an ORF transcribed from the antisense strand of the 3' untranslated region of TRIT1.
Neoplasms
Association of polymorphisms and haplotype in the region of TRIT1, MYCL1 and MFSD2A with the risk and clinicopathological features of gastric cancer in a southeast Chinese population.
Neoplasms
Breast cancer cell targeting by prenylation inhibitors elucidated in living animals with a bioluminescence reporter.
Neoplasms
Circulating essential metals and lung cancer: Risk assessment and potential molecular effects.
Neoplasms
Direct evidence for the contribution of activated N-ras and K-ras oncogenes to increased intrinsic radiation resistance in human tumor cell lines.
Neoplasms
Evaluation of prenylated peptides for use in cellular imaging and biochemical analysis.
Neoplasms
Gene Amplification-Associated Overexpression of the Selenoprotein tRNA Enzyme TRIT1 Confers Sensitivity to Arsenic Trioxide in Small-Cell Lung Cancer.
Neoplasms
Human cells have a limited set of tRNA anticodon loop substrates of the tRNA isopentenyltransferase TRIT1 tumor suppressor.
Neoplasms
Identification and functional characterization of the candidate tumor suppressor gene TRIT1 in human lung cancer.
Neoplasms
Inhibiting Ras prenylation increases the radiosensitivity of human tumor cell lines with activating mutations of ras oncogenes.
Neoplasms
Inhibitors of farnesyltransferase and geranylgeranyltransferase-I for antitumor therapy: substrate-based design, conformational constraint and biological activity.
Neoplasms
Molecular targets for altering radiosensitivity: lessons from Ras as a pre-clinical and clinical model.
Neoplasms
Pancreatic cancer cell radiation survival and prenyltransferase inhibition: the role of K-Ras.
Neoplasms
Plasticity and diversity of tRNA anticodon determinants of substrate recognition by eukaryotic A37 isopentenyltransferases.
Neoplasms
Prenyltransferase Inhibitors: Treating Human Ailments from Cancer to Parasitic Infections.
Neoplasms
The cytoplasmic and nuclear populations of the eukaryote tRNA-isopentenyl transferase have distinct functions with implications in human cancer.
Neoplasms
The Role of Geranylgeranyltransferase I-Mediated Protein Prenylation in the Brain.
Neoplasms
The tumor suppressor TERE1 (UBIAD1) prenyltransferase regulates the elevated cholesterol phenotype in castration resistant prostate cancer by controlling a program of ligand dependent SXR target genes.
Pancreatic Neoplasms
Pancreatic cancer cell radiation survival and prenyltransferase inhibition: the role of K-Ras.
Parasitic Diseases
Prenyltransferase Inhibitors: Treating Human Ailments from Cancer to Parasitic Infections.
Parasitic Diseases
Protein prenylation: enzymes, therapeutics, and biotechnology applications.
Progeria
Prenyltransferase Inhibitors: Treating Human Ailments from Cancer to Parasitic Infections.
Prostatic Neoplasms
The tumor suppressor TERE1 (UBIAD1) prenyltransferase regulates the elevated cholesterol phenotype in castration resistant prostate cancer by controlling a program of ligand dependent SXR target genes.
Seizures
Noninvasive diagnosis of TRIT1-related mitochondrial disorder by measuring i6 A37 and ms2 i6 A37 modifications in tRNAs from blood and urine samples.
Stomach Neoplasms
Association of polymorphisms and haplotype in the region of TRIT1, MYCL1 and MFSD2A with the risk and clinicopathological features of gastric cancer in a southeast Chinese population.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
KM of substrates and tRNA from various species
-
additional information
additional information
-
KM for tRNA substrates is around 3 nM
-
additional information
additional information
Michaelis-Menten steady-state kinetics
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
7.5 - 8
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
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
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
ubiquitous expression, highest in proliferating tissue
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Trit1 encodes an amino-terminal mitochondrial targeting sequence that directs mitochondrial import and modification of mitochondrial-tRNAs
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
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
evolution
while absent in eukaryotes, some facultative bacteria use a non-heme diiron enzyme [MiaE, 2-methylthio-N6-isopentenyladenosine(37)-tRNA monooxygenase] to catalyze the O2-dependent hydroxylation of ms2i6A37 to produce 2-methylthio-N6-(4-hydroxyisopentenyl)-adenosine (ms2io6A37), comparison of MiaA and MiaE catalytic reactions, overview
evolution
-
while absent in eukaryotes, some facultative bacteria use a non-heme diiron enzyme [MiaE, 2-methylthio-N6-isopentenyladenosine(37)-tRNA monooxygenase] to catalyze the O2-dependent hydroxylation of ms2i6A37 to produce 2-methylthio-N6-(4-hydroxyisopentenyl)-adenosine (ms2io6A37), comparison of MiaA and MiaE catalytic reactions, overview
-
metabolism
the enzyme is involved in the hypermodification enzyme pathway for 2-methylthio-N6-(4-hydroxyisopentenyl)-adenosine (ms2io6A37) synthesis. within the anticodon stem loop of tRNA, nucleotide modifications are frequently observed at position 34 (the wobble position) or position 37 (3' adjacent to the anticodon), nearly all eukaryotic and bacterial tRNAs that read codons starting with U are modified by the enzymes MiaA and MiaB and contain the ms2i6A modification
metabolism
-
the enzyme is involved in the hypermodification enzyme pathway for 2-methylthio-N6-(4-hydroxyisopentenyl)-adenosine (ms2io6A37) synthesis. within the anticodon stem loop of tRNA, nucleotide modifications are frequently observed at position 34 (the wobble position) or position 37 (3' adjacent to the anticodon), nearly all eukaryotic and bacterial tRNAs that read codons starting with U are modified by the enzymes MiaA and MiaB and contain the ms2i6A modification
-
physiological function
mammalian Trit1 is a tRNA([Ser]Sec)-isopentenyl transferase required for full selenoprotein expression, full expression of selenoproteins requires modification of tRNA[Ser]Sec, including N6-isopentenylation of base A37
physiological function
enzyme MiaA catalyzes the nucleophilic substitution of the dimethylallyl group from dimethylallyl diphosphate (DMAPP) to the exocyclic 6-amino nitrogen of A37 (N6) to yield N6-isopentenyladenosine (i6A37) with release of inorganic diphosphate
physiological function
Trit1 exhibits substrate-specific restriction against Schizosaccharomyces pombe cytosolic tRNATrpCCA-A37-A38. Position 32 of tRNATrpCCA may be a conditional determinant for substrate-specific i6A37 modification by Trit1
physiological function
-
enzyme MiaA catalyzes the nucleophilic substitution of the dimethylallyl group from dimethylallyl diphosphate (DMAPP) to the exocyclic 6-amino nitrogen of A37 (N6) to yield N6-isopentenyladenosine (i6A37) with release of inorganic diphosphate
-
Show AA Sequence and Transmembrane Helices (24326 entries)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E229A
-
substantial increase in Km for RNA, dimethylallyl diphosphate becomes inhibitory at higher concentrations
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
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
K181H
selective disproportionate decrease in activity toward several substrates
additional information
additional information
-
deletion mutant: no enzyme activity, no release of isopentenyladenine into extracellular medium
additional information
an N-terminal deletion construct 57-467 is inactive on both the mitochondrial and cytosolic tRNA substrates
additional information
-
an N-terminal deletion construct 57-467 is inactive on both the mitochondrial and cytosolic tRNA substrates
additional information
knockdown of enzyme TRIT1 in NIH-3T3 cells by stable expression of shRNA. GPx1 expression is highly sensitive to tRNA[Ser]Sec modification in mouse liver expressing only tRNA[Ser]Sec carrying a 37A>G substitution, GPx1 levels in murine NIH-3T3 cells expressing the Trit1-knockdown construct are significantly reduced compared with control cells
additional information
mutation of the enzyme in its G34 recognition loop region debilitates it differentially for its G34 substrates
additional information
-
mutation of the enzyme in its G34 recognition loop region debilitates it differentially for its G34 substrates
additional information
deletion of 55 amino acids from the C terminus or mutation of both cysteines of the C2H2 Zn finger to alanine leads to inactivity with all of the anticodon stem-loop minihelices tested and with tRNAs
additional information
-
deletion of 55 amino acids from the C terminus or mutation of both cysteines of the C2H2 Zn finger to alanine leads to inactivity with all of the anticodon stem-loop minihelices tested and with tRNAs
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-18°C, 0.59 mg bovine serum albumin/ml, 50% glycerol, purified enzyme loses 80% of activity after 14 days
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partial
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
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Petunia hybrida under control of the flowerspecific Arabidopsis AP3 promoter
-
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
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
nitrate treatment of roots and leaves enhances amount of mRNA significantly
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
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
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
medicine
identification of compound heterozygous missense mutations, i.e. c.244A>G p.(Met82Val) in exon 2 in the maternally derived allele, and c.1034A>G p.(Tyr345Cys) in exon 9 in the paternally derived allele, in Trit1 in a girl with a developmental delay, frequent episodes of seizures induced by febrile illness, and myoclonic epilepsy. In peripheral blood and urine, a marked decrease in both i6A and ms2i6A modifications is observed. The mitochondrial disorder is caused by defective tRNA isopentenylation arising from a loss-of-function mutation in Trit1
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kline, L.K.; Fittler, F.; Hall, R.H.
N6-(delta-2-isopentenyl) adenosine. Biosynthesis in transfer ribonucleic acid in vitro
Biochemistry
8
4361-4371
1969
Saccharomyces cerevisiae
brenda
Rosenbaum, N.; Gefter, M.L.
DELTA 2 -isopentenylpyrophosphate: transfer ribonucleic acid 2 -isopentenyltransferase from Escherichia coli. Purification and properties of the enzyme
J. Biol. Chem.
247
5675-5680
1972
Escherichia coli
brenda
Bartz, J.K.; Soell, D.
N6-(2-isopentenyl) adenosine: biosynthesis in vitro in transfer RNA by an enzyme purified from Escherichia coli
Biochimie
54
31-39
1972
Escherichia coli
brenda
Holtz, J.; Klmbt, D.
tRNA isopentenyltransferase from Lactobacillus acidophilus ATCC 4963
Hoppe-Seyler's Z. Physiol. Chem.
356
1459-1464
1975
Lactobacillus acidophilus
brenda
Holtz, J.; Klmbt, D.
tRNA isopentenyltransferase from Zea mays L. Characterization of the isopentenylation reaction of tRNA, oligo (A) and other nucleic acids
Hoppe-Seyler's Z. Physiol. Chem.
359
89-101
1978
Zea mays
brenda
Golovko, A.; Sitbon, F.; Tillberg, E.; Nicander, B.
Identification of a tRNA isopentenyltransferase gene from Arabidopsis thaliana
Plant Mol. Biol.
49
161-169
2002
Arabidopsis thaliana (Q9ZUX7), Arabidopsis thaliana
brenda
Gray, J.; Gelvin, S.B.; Meilan, R.; Morris, R.O.
Transfer RNA is the source of extracellular isopentenyladenine in a Ti-plasmidless strain of Agrobacterium tumefaciens
Plant Physiol.
110
431-438
1996
Agrobacterium tumefaciens
brenda
Leung, H.C.E.; Chen, Y.; Winkler, M.E.
Regulation of substrate recognition by the MiaA tRNA prenyltransferase modification enzyme of Escherichia coli K-12
J. Biol. Chem.
272
13073-13083
1997
Escherichia coli
brenda
Lemieux, J.; Lakowski, B.; Webb, A.; Meng, Y.; Ubach, A.; Bussiere, F.; Barnes, T.; Hekimi, S.
Regulation of physiological rates in Caenorhabditis elegans by a tRNA-modifying enzyme in the mitochondria
Genetics
159
147-157
2001
Caenorhabditis elegans
brenda
Golovko, A.; Hjalm, G.; Sitbon, F.; Nicander, B.
Cloning of a human tRNA isopentenyl transferase
Gene
258
85-93
2000
Homo sapiens (Q9H3H1)
brenda
Motorin, Y.; Bec, G.; Tewari, R.; Grosjean, H.
Transfer RNA recognition by the Escherichia coli D2-isopentenyl-pyrophosphate:tRNA D2-isopentenyl transferase: dependence on the anticodon arm structure
RNA
3
721-733
1997
Escherichia coli
brenda
Spinola, M.; Galvan, A.; Pignatiello, C.; Conti, B.; Pastorino, U.; Nicander, B.; Paroni, R.; Dragani, T.A.
Identification and functional characterization of the candidate tumor suppressor gene TRIT1 in human lung cancer
Oncogene
24
5502-5509
2005
Homo sapiens (Q3T7C6), Homo sapiens
brenda
Miyawaki, K.; Matsumoto-Kitano, M.; Kakimoto, T.
Expression of cytokinin biosynthetic isopentenyltransferase genes in Arabidopsis: tissue specificity and regulation by auxin, cytokinin, and nitrate
Plant J.
37
128-138
2004
Arabidopsis thaliana
brenda
Yevdakova, N.A.; von Schwartzenberg, K.
Characterisation of a prokaryote-type tRNA-isopentenyltransferase gene from the moss Physcomitrella patens
Planta
226
683-695
2007
Physcomitrium patens (A4ZZA3), Physcomitrium patens
brenda
Miyawaki, K.; Tarkowski, P.; Matsumoto-Kitano, M.; Kato, T.; Sato, S.; Tarkowska, D.; Tabata, S.; Sandberg, G.; Kakimoto, T.
Roles of Arabidopsis ATP/ADP isopentenyltransferases and tRNA isopentenyltransferases in cytokinin biosynthesis
Proc. Natl. Acad. Sci. USA
103
16598-16603
2006
Arabidopsis thaliana
brenda
Golovko, A.; Sitbon, F.; Tillberg, E.; Nicander, B.
Expression of a human tRNA isopentenyltransferase in tobacco reveals a developmental role for tRNA isopentenyladenosine
Funct. Plant Biol.
34
654-661
2007
Homo sapiens (Q9H3H1)
-
brenda
Kaminska, K.H.; Baraniak, U.; Boniecki, M.; Nowaczyk, K.; Czerwoniec, A.; Bujnicki, J.M.
Structural bioinformatics analysis of enzymes involved in the biosynthesis pathway of the hypermodified nucleoside ms2io6A37 in tRNA
Proteins Struct. Funct. Bioinform.
70
1-18
2007
Salmonella enterica subsp. enterica serovar Typhimurium (P37724)
brenda
Moore, J.A.; Poulter, C.D.
Escherichia coli dimethylallyl diphosphate:tRNA dimethylallyltransferase: a binding mechanism for recombinant enzyme
Biochemistry
36
604-614
1997
Escherichia coli
brenda
Soderberg, T.; Poulter, C.D.
Escherichia coli dimethylallyl diphosphate:tRNA dimethylallyltransferase: essential elements for recognition of tRNA substrates within the anticodon stem-loop
Biochemistry
39
6546-6553
2000
Escherichia coli
brenda
Soderberg, T.; Poulter, C.D.
Escherichia coli dimethylallyl diphosphate:tRNA dimethylallyltransferase: site-directed mutagenesis of highly conserved residues
Biochemistry
40
1734-1740
2001
Escherichia coli
brenda
Zhou, C.; Huang, R.H.
Crystallographic snapshots of eukaryotic dimethylallyltransferase acting on tRNA: insight into tRNA recognition and reaction mechanism
Proc. Natl. Acad. Sci. USA
105
16142-16147
2008
Saccharomyces cerevisiae (P07884), Saccharomyces cerevisiae
brenda
Chu, H.M.; Ko, T.P.; Wang, A.H.
Crystal structure and substrate specificity of plant adenylate isopentenyltransferase from Humulus lupulus: distinctive binding affinity for purine and pyrimidine nucleotides
Nucleic Acids Res.
38
1738-1748
2010
Humulus lupulus (Q5GHF7), Humulus lupulus
brenda
Verdonk, J.C.; Shibuya, K.; Loucas, H.M.; Colquhoun, T.A.; Underwood, B.A.; Clark, D.G.
Flower-specific expression of the Agrobacterium tumefaciens isopentenyltransferase gene results in radial expansion of floral organs in Petunia hybrida
Plant Biotechnol. J.
6
694-701
2008
Agrobacterium tumefaciens
brenda
Ma, Q.; Liu, Y.
Expression of isopentenyl transferase gene (ipt) in leaf and stem delayed leaf senescence without affecting root growth
Plant Cell Rep.
28
1759-1765
2009
Agrobacterium tumefaciens
brenda
Peng, J.; Peng, F.; Zhu, C.; Wei, S.
Molecular cloning of a putative gene encoding isopentenyltransferase from pingyitiancha (Malus hupehensis) and characterization of its response to nitrate
Tree Physiol.
28
899-904
2008
Malus hupehensis
brenda
Lamichhane, T.N.; Blewett, N.H.; Maraia, R.J.
Plasticity and diversity of tRNA anticodon determinants of substrate recognition by eukaryotic A37 isopentenyltransferases
RNA
17
1846-1857
2011
Schizosaccharomyces pombe (Q9UT75), Schizosaccharomyces pombe, Saccharomyces cerevisiae (P07884), Saccharomyces cerevisiae, Homo sapiens (Q9H3H1), Homo sapiens
brenda
Fradejas, N.; Carlson, B.A.; Rijntjes, E.; Becker, N.P.; Tobe, R.; Schweizer, U.
Mammalian Trit1 is a tRNA([Ser]Sec)-isopentenyl transferase required for full selenoprotein expression
Biochem. J.
450
427-432
2013
Mus musculus (Q80UN9)
brenda
Subedi, B.P.; Corder, A.L.; Zhang, S.; Foss, F.W.; Pierce, B.S.
Steady-state kinetics and spectroscopic characterization of enzyme-tRNA interactions for the non-heme diiron tRNA-monooxygenase, MiaE
Biochemistry
54
363-376
2015
Salmonella enterica (P37724), Salmonella enterica ATCC 700720 (P37724)
brenda
Takenouchi, T.; Wei, F.Y.; Suzuki, H.; Uehara, T.; Takahashi, T.; Okazaki, Y.; Kosaki, K.; Tomizawa, K.
Noninvasive diagnosis of TRIT1-related mitochondrial disorder by measuring i6 A37 and ms2 i6 A37 modifications in tRNAs from blood and urine samples
Am. J. Med. Genet. A
179
1609-1614
2019
Homo sapiens (Q9H3H1), Homo sapiens
brenda
Frebortova, J.; Plihal, O.; Florova, V.; Kokas, F.; Kubiasova, K.; Greplova, M.; Simura, J.; Novak, O.; Frebort, I.
Light influences cytokinin biosynthesis and sensing in Nostoc (cyanobacteria)
J. Phycol.
53
703-714
2017
Nostoc sp. PCC 7120 = FACHB-418 (Q8YLN2)
brenda
Khalique, A.; Mattijssen, S.; Haddad, A.F.; Chaudhry, S.; Maraia, R.J.
Targeting mitochondrial and cytosolic substrates of TRIT1 isopentenyltransferase Specificity determinants and tRNA-i6A37 profiles
PLoS Genet.
16
e1008330
2020
Homo sapiens (Q9H3H1), Homo sapiens
brenda
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