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Information on EC 2.4.2.48 - tRNA-guanine15 transglycosylase and Organism(s) Methanocaldococcus jannaschii and UniProt Accession Q57878

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EC Tree
     2 Transferases
         2.4 Glycosyltransferases
             2.4.2 Pentosyltransferases
                2.4.2.48 tRNA-guanine15 transglycosylase
IUBMB Comments
Archaeal tRNAs contain the modified nucleoside archaeosine at position 15. This archaeal enzyme catalyses the exchange of guanine at position 15 of tRNA with the base preQ0, which is ultimately modified to form the nucleoside archaeosine (cf. EC 2.6.1.97) .
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This record set is specific for:
Methanocaldococcus jannaschii
UNIPROT: Q57878
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The taxonomic range for the selected organisms is: Methanocaldococcus jannaschii
The expected taxonomic range for this enzyme is: Archaea, Bacteria
Reaction Schemes
hide
guanine15 in tRNA
+
7-cyano-7-carbaguanine
=
7-cyano-7-carbaguanine15 in tRNA
+
guanine
guanine15 in tRNA
+
=
7-cyano-7-carbaguanine15 in tRNA
+
Synonyms
archaeosine trna-guanine transglycosylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tRNA-guanine transglycosylase
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transfer ribonucleic acid guanine15 transglycosylase
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tRNA guanine15 transglycosidase
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PATHWAY SOURCE
PATHWAYS
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-, -
SYSTEMATIC NAME
IUBMB Comments
tRNA-guanine15:7-cyano-7-carbaguanine tRNA-D-ribosyltransferase
Archaeal tRNAs contain the modified nucleoside archaeosine at position 15. This archaeal enzyme catalyses the exchange of guanine at position 15 of tRNA with the base preQ0, which is ultimately modified to form the nucleoside archaeosine (cf. EC 2.6.1.97) [1].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
guanine15 in tRNA + 7-cyano-7-carbaguanine
7-cyano-7-carbaguanine15 in tRNA + guanine
show the reaction diagram
additional information
?
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the enzyme catalyzes a transglycosylation reaction in which guanine is eliminated from position 15 of the tRNA and an archaeosine precursor (preQ0) is inserted. The enzyme is able to utilize both guanine and the 7-deazaguanine base preQ0 as substrates, but not other 7-deazaguanine bases, and is able to modify tRNA from all three phylogenetic domains. The enzyme shows good activity with the tRNASer transcript as well as tRNA from Escherichia coli and yeast
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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
guanine15 in tRNA + 7-cyano-7-carbaguanine
7-cyano-7-carbaguanine15 in tRNA + guanine
show the reaction diagram
i.e. 7-(cyano)-7-deazaguanine = preQ0
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-
?
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
134
purified recombinant TGT, pH 5.5, 80°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
optimal activity at acidic pH
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
optimal activity at high temperatures
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene tgtA, orf MJ0436; gene tgt
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
biogenetic relationship of queuosine and archaeosine, overview. The elements necessary for tRNA recognition by the enzyme are not unique to archaeal tRNA
metabolism
GTP is apparently the primary precursor in the biosynthesis of queuosine, which in a series of steps is converted to 7-(cyano)-7-deazaguanine, i.e. preQ0. PreQ0 is then reduced to PreQ1, and preQ1 is subsequently inserted into the tRNA by the enzyme TGT in a transglycosylation reaction in which the genetically encoded base guanine is eliminated
additional information
the nature of the temperature dependence is consistent with a requirement for some degree of tRNA tertiary structure in order for recognition by the enzyme to occur
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant TGT 16.8fold from Escherichia coli strain BL21(DE3)/pYB-I-120 by ammonium sulfate fractionation, anion and cation exchange chromatography, and heat treatment
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene tgt, overexpression in Escherichia coli strain BL21(DE3)/pYB-I-120, subcloning in Escherichia coli strain DH5alpha
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bai, Y.; Fox, D.; Lacy, J.; Van Lanen, S.; Iwata-Reuyl, D.
Hypermodification of tRNA in thermophilic archaea. Cloning, overexpression, and characterization of tRNA-guanine transglycosylase from Methanococcus jannaschii
J. Biol. Chem.
275
28731-28738
2000
Methanocaldococcus jannaschii (Q57878)
Manually annotated by BRENDA team