Information on EC 2.1.1.219 - tRNA (adenine57-N1/adenine58-N1)-methyltransferase

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The expected taxonomic range for this enzyme is: Pyrococcus abyssi

EC NUMBER
COMMENTARY hide
2.1.1.219
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RECOMMENDED NAME
GeneOntology No.
tRNA (adenine57-N1/adenine58-N1)-methyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 S-adenosyl-L-methionine + adenine57/adenine58 in tRNA = 2 S-adenosyl-L-homocysteine + N1-methyladenine57/N1-methyladenine58 in tRNA
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:tRNA (adenine57/adenine58-N1)-methyltransferase
The enzyme catalyses the formation of N1-methyladenine at two adjacent positions (57 and 58) in the T-loop of certain tRNAs (e.g. tRNAAsp). Methyladenosine at position 57 is an obligatory intermediate for the synthesis of methylinosine, which is commonly found at position 57 of archaeal tRNAs.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
PabTrmI methylates efficiently the first adenine of the A57A58A59 sequence. m1A58 formation triggers RNA release. A model of the protein-tRNA complex shows both target adenines in proximity of S-adenosyl-L-methionine and emphasizes no major tRNA conformational change except base flipping during the reaction. The solvent accessibility of the S-adenosyl-L-methionine pocket is not affected by the tRNA, thereby enabling S-adenosyl-L-homocysteine to be replaced by S-adenosyl-L-methionine without prior release of monomethylated tRNA. Dynamics of RNA binding by PabTrmI in the presence and absence of S-adenosyl-L-methionine, structural model of PabTrmI in complex with tRNA, overview
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 S-adenosyl-L-methionine + adenine57/adenine58 in tRNA
2 S-adenosyl-L-homocysteine + N1-methyladenine57/N1-methyladenine58 in tRNA
show the reaction diagram
2 S-adenosyl-L-methionine + adenine57/adenine58 in tRNAArg
2 S-adenosyl-L-homocysteine + adenine57/N1-methyladenine58 in tRNAArg
show the reaction diagram
modified mini-tRNAAsp substrate, PabTrmI recognizes and methylates only A58 in mini-tRNAArgTCT containing the G57A58A59U60 sequence
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2 S-adenosyl-L-methionine + adenine57/adenine58 in tRNAAsp
2 S-adenosyl-L-homocysteine + N1-methyladenine57/N1-methyladenine58 in tRNAAsp
show the reaction diagram
additional information
?
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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
2 S-adenosyl-L-methionine + adenine57/adenine58 in tRNA
2 S-adenosyl-L-homocysteine + N1-methyladenine57/N1-methyladenine58 in tRNA
show the reaction diagram
additional information
?
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Q9V1J7
in most organisms, the widely conserved 1-methyladenosine58 (m1A58) tRNA modification is catalyzed by S-adenosyl-L-methionine-dependent site-specific enzyme TrmI. In archaea, TrmI also methylates the adjacent adenine 57, m1A57 being an obligatory intermediate of 1-methyl-inosine57 formation, multi-site specificity mechanism, overview
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
dynamics of RNA binding by PabTrmI in the presence and absence of S-adenosyl-L-methionine
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
steady-state fluorescent assay and stopped-flow kinetics with 2-aminopurine-modifed tRNA substrates, , overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Pyrococcus abyssi (strain GE5 / Orsay)
Pyrococcus abyssi (strain GE5 / Orsay)
Pyrococcus abyssi (strain GE5 / Orsay)
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
concentrated by ultrafiltration, crystallisation at 20°C by the sitting-drop vapour diffusion method
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crystal structure TrmI in complex with SAH is determined in two different space groups at 2.6 and 2.05 A resolution, and in complex with S-adenosyl-L-methionine (SAM) at 1.6 A resolution
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
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1 h, wild-type enzyme and mutant enzyme C196S/C233S are stable
85
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mutant enzyme C196S/C233S is inactivated after 20 min, wild-type enzyme is stable for more than 1 h
additional information
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the stabilisation of Pyrococcus abyssi TrmI at extreme temperatures involves intersubunit disulfide bridges formed between Cys196 and Cys233 that reinforce the tetrameric oligomerisation
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; recombinant C-terminally His6-tagged enzyme by nickel affiniyt chromatography and gel filtration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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recombinant expression of C-terminally His6-tagged enzyme
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C196S/C233S