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Information on EC 2.1.1.34 - tRNA (guanosine18-2'-O)-methyltransferase and Organism(s) Aquifex aeolicus and UniProt Accession O67577

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EC Tree
     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.1 Methyltransferases
                2.1.1.34 tRNA (guanosine18-2'-O)-methyltransferase
IUBMB Comments
The enzyme catalyses the methylation of guanosine18 in tRNA.
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This record set is specific for:
Aquifex aeolicus
UNIPROT: O67577
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Word Map
The taxonomic range for the selected organisms is: Aquifex aeolicus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Synonyms
tarbp1, trna (gm18) methyltransferase, transfer rna (gm18) methyltransferase, trna (gm18) 2'-o-methyltransferase, trna gm18 methyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methyltransferase, transfer ribonucleate guanosine 2'-
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S-adenosyl-L-methionine:tRNA (guanosine-2'-O-)-methyltransferase
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transfer ribonucleate guanosine 2'-methyltransferase
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tRNA (guanosine-2'-O-)-methyltransferase
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tRNA guanosine 2'-methyltransferase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methyl group transfer
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:tRNA (guanosine18-2'-O)-methyltransferase
The enzyme catalyses the methylation of guanosine18 in tRNA.
CAS REGISTRY NUMBER
COMMENTARY hide
37257-01-5
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + tRNA
S-adenosyl-L-homocysteine + tRNA containing 2'-O-methylguanine
show the reaction diagram
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additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
54000
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
gel filtration
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by the hanging-drop method, at 1.85 A resolution, diffraction-quality crystals in the pH range 4.0–4.5, enzyme can not be crystallized with S-adenosyl-L-methionine or an analog in the active site
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
gel filtration, more than 99% pure
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
into vector pThioHisB and transformed into Escherichia coli strain DH5alpha, overexpressed in Escherichia coli Rosetta(DE3)/pLysS cells
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
reveals a fold typical of members of the SpoU clan of proteins, a subfamily of the alpha/beta-knot superfamily, with alpha-helical extensions at the N- and C-termini that are likely to be involved in tRNA binding
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hori, H.; Kubota, S.; Watanabe, K.; Kim, J.M.; Ogasawara, T.; Sawasaki, T.; Endo, Y.
Aquifex aeolicus tRNA (Gm18) methyltransferase has unique substrate specificity: tRNA recognition mechanism of the enzyme
J. Biol. Chem.
278
25081-25090
2003
Aquifex aeolicus (O67577), Aquifex aeolicus
Manually annotated by BRENDA team
Pleshe, E.; Truesdell, J.; Batey, R.T.
Structure of a class II TrmH tRNA-modifying enzyme from Aquifex aeolicus
Acta Crystallogr. Sect. F
61
722-728
2005
Aquifex aeolicus (O67577)
Manually annotated by BRENDA team