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Information on EC 2.4.2.48 - tRNA-guanine15 transglycosylase
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2.4.2.48 tRNA-guanine15 transglycosylaseIUBMB 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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Word Map
- 2.4.2.48
- horikoshii
- arctgt
- preq0
-
pyrococcus
- 7-cyano-7-deazaguanine
-
anticodon
-
d-loop
The expected taxonomic range for this enzyme is: Archaea, Bacteria
Reaction Schemes
guanine15 in tRNA
+
=
7-cyano-7-carbaguanine15 in tRNA
+
Synonyms
archaeosine trna-guanine transglycosylase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
archaeosine tRNA-guanine transglycosylase
archaeosine tRNAguanine transglycosylase
ArcTGT
multisite-specific archaeosine tRNA-guanine transglycosylase
-
transfer ribonucleic acid guanine15 transglycosylase
-
-
-
-
tRNA guanine15 transglycosidase
-
-
-
-
tRNA-guanine transglycosylase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
guanine15 in tRNA + 7-cyano-7-carbaguanine = 7-cyano-7-carbaguanine15 in tRNA + guanine
-
-
-
-
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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].
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
guanine13 in tRNA(Leu) + 7-cyano-7-carbaguanine
7-cyano-7-carbaguanine13 in tRNA(Leu) + guanine
-
-
-
?
guanine15 in tRNA(Leu) + 7-cyano-7-carbaguanine
7-cyano-7-carbaguanine15 in tRNA(Leu) + guanine
tRNAguanine + 7-cyano-7-deazaguanine
?
-
archaeal TGT substitutes 7-cyano-7-deazaguanine for the G in position 15 of tRNA as the first step in archaeosine formation
-
-
?
additional information
?
-
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
-
-
?
guanine15 in tRNA + 7-cyano-7-carbaguanine
7-cyano-7-carbaguanine15 in tRNA + guanine
key enzyme for the biosynthetic pathway leading to archaeosine in archaeal tRNAs
-
-
?
guanine15 in tRNA + 7-cyano-7-carbaguanine
7-cyano-7-carbaguanine15 in tRNA + guanine
archaeosine base and 7-aminomethyl-7-deazaguanine are not incorporated into tRNA by this enzyme. Does not require ATP for the base replacement reaction
-
-
?
guanine15 in tRNA + 7-cyano-7-carbaguanine
7-cyano-7-carbaguanine15 in tRNA + guanine
key enzyme for the biosynthetic pathway leading to archaeosine in archaeal tRNAs
-
-
?
guanine15 in tRNA + 7-cyano-7-carbaguanine
7-cyano-7-carbaguanine15 in tRNA + guanine
archaeosine base and 7-aminomethyl-7-deazaguanine are not incorporated into tRNA by this enzyme. Does not require ATP for the base replacement reaction
-
-
?
guanine15 in tRNA + 7-cyano-7-carbaguanine
7-cyano-7-carbaguanine15 in tRNA + guanine
i.e. 7-(cyano)-7-deazaguanine = preQ0
-
-
?
guanine15 in tRNA + 7-cyano-7-carbaguanine
7-cyano-7-carbaguanine15 in tRNA + guanine
i.e. 7-(cyano)-7-deazaguanine = preQ0. Haloferax volcanii tRNASer is used as substrate
-
-
?
guanine15 in tRNA + 7-cyano-7-carbaguanine
7-cyano-7-carbaguanine15 in tRNA + guanine
-
-
-
?
guanine15 in tRNA + 7-cyano-7-carbaguanine
7-cyano-7-carbaguanine15 in tRNA + guanine
-
-
-
?
guanine15 in tRNA + 7-cyano-7-deazaguanine
7-cyano-7-deazaguanine15 in tRNA + guanine
-
-
-
-
?
guanine15 in tRNA + 7-cyano-7-deazaguanine
7-cyano-7-deazaguanine15 in tRNA + guanine
-
-
-
-
?
guanine15 in tRNA + 7-cyano-7-deazaguanine
7-cyano-7-deazaguanine15 in tRNA + guanine
-
-
-
-
?
guanine15 in tRNA(Leu) + 7-cyano-7-carbaguanine
7-cyano-7-carbaguanine15 in tRNA(Leu) + guanine
-
-
-
?
guanine15 in tRNA(Leu) + 7-cyano-7-carbaguanine
7-cyano-7-carbaguanine15 in tRNA(Leu) + guanine
-
-
-
?
guanine15 in tRNA(Leu) + 7-cyano-7-carbaguanine
7-cyano-7-carbaguanine15 in tRNA(Leu) + guanine
-
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
guanine15 in tRNA + 7-cyano-7-carbaguanine
7-cyano-7-carbaguanine15 in tRNA + guanine
key enzyme for the biosynthetic pathway leading to archaeosine in archaeal tRNAs
-
-
?
guanine15 in tRNA + 7-cyano-7-carbaguanine
7-cyano-7-carbaguanine15 in tRNA + guanine
key enzyme for the biosynthetic pathway leading to archaeosine in archaeal tRNAs
-
-
?
guanine15 in tRNA + 7-cyano-7-carbaguanine
7-cyano-7-carbaguanine15 in tRNA + guanine
i.e. 7-(cyano)-7-deazaguanine = preQ0
-
-
?
guanine15 in tRNA + 7-cyano-7-carbaguanine
7-cyano-7-carbaguanine15 in tRNA + guanine
-
-
-
?
guanine15 in tRNA + 7-cyano-7-carbaguanine
7-cyano-7-carbaguanine15 in tRNA + guanine
-
-
-
?
guanine15 in tRNA + 7-cyano-7-deazaguanine
7-cyano-7-deazaguanine15 in tRNA + guanine
-
-
-
-
?
guanine15 in tRNA + 7-cyano-7-deazaguanine
7-cyano-7-deazaguanine15 in tRNA + guanine
-
-
-
-
?
guanine15 in tRNA + 7-cyano-7-deazaguanine
7-cyano-7-deazaguanine15 in tRNA + guanine
-
-
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
additional information
high salt concentration approximately 2.4 M is necessary for maximum activity
Mg2+
Mg2+ may be responsible for conformational rigidity of the tRNA, but not for the enzymatic activity itself. Mg2+ ion is required for activity with the T7 transcript as a substrate. Activity with unfractionated Escherichia coli tRNA does not require Mg2+
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0012
guanine15 in tRNA
native enzyme, at pH 7.5 and 37°C
-
0.0021
guanine15 in tRNA
recombinant enzyme, at pH 7.5 and 37°C
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0311
guanine15 in tRNA
native enzyme, at pH 7.5 and 37°C
-
0.0667
guanine15 in tRNA
recombinant enzyme, at pH 7.5 and 37°C
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
31
guanine15 in tRNA
recombinant enzyme, at pH 7.5 and 37°C
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
27
native enzyme, after 2900fold purification, at pH 7.5 and 37°C
31
recombinant enzyme, after 14fold purification, at pH 7.5 and 37°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
optimal activity at high temperatures
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
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
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterotetramer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of tRNAVal in complex with archaeosine tRNA-guanine transglycosylase at 3.3 A resolution. The enzyme binds a different tRNA conformation (lambda form), in which the canonical core is completely disrupted and the melted D arm is protruded. The PUA domain is found to be crucial for the precise location of the tRNA molecule on the enzyme
crystal structures of the enzyme at 2.2 A resolution and its complexes with guanine and 7-cyano-7-deazaguanine, at 2.3 and 2.5 A resolutions, respectively
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
the C-terminal extension of the enzyme is not required for the selection of G15 as the site of base exchange. Truncated forms of Pyrococcus furiosus TGT retain their specificity for guanine exchange at position 15. Deletion of the PUA domain causes a 4fold drop in the observed kcat and results in a 75fold increased Km for tRNAAsp compared with full-length TGT
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, phenyl Sepharose column chromatography, HiTrap Q column chromatography, HiTrap heparin column chromatography, Mono Q column chromatography, and Sephacryl S-200 gel filtration
HiTrap Q-Sepharose and HiTrap Heparin-Sepharose column chromatography
-
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
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
because the Thermoplasma acidophilum enzyme can not be expressed as a soluble protein in Escherichia coli, an expression system using another thermophilic archaeon, Thermococcus kodakarensis is employed. The arcTGT gene in Thermococcus kodakarensis is disrupted, complemented with the Thermoplasma acidophilum arcTGT gene, and tRNALeu variants are expressed. Mass spectrometry analysis of purified tRNALeu variants reveals the modifications of archaeosine13 and archaeosine15 in the wild-type tRNALeu
gene tgt, overexpression in Escherichia coli strain BL21(DE3)/pYB-I-120, subcloning in Escherichia coli strain DH5alpha
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sabina, J.; Soell, D.
The RNA-binding PUA domain of archaeal tRNA-guanine transglycosylase is not required for archaeosine formation
J. Biol. Chem.
281
6993-7001
2006
Pyrococcus furiosus
brenda
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)
brenda
Ishitani, R.; Nureki, O.; Nameki, N.; Okada, N.; Nishimura, S.; Yokoyama, S.
Alternative tertiary structure of tRNA for recognition by a posttranscriptional modification enzyme
Cell
113
383-394
2005
Pyrococcus horikoshii (O58843)
brenda
Watanabe, M.; Matsuo, M.; Tanaka, S.; Akimoto, H.; Asahi, S.; Nishimura, S.; Katze, J.R.; Hashizume, T.; Crain, P.F.; McCloskey, J.A.; Okada, N.
Biosynthesis of archaeosine, a novel derivative of 7-deazaguanosine specific to archaeal tRNA, proceeds via a pathway involving base replacement on the tRNA polynucleotide chain
J. Biol. Chem.
272
20146-20151
1997
Haloferax volcanii (Q9C4M3), Haloferax volcanii ATCC 29605 (Q9C4M3)
brenda
Ishitani, R.; Nureki, O.; Fukai, S.; Kijimoto, T.; Nameki, N.; Watanabe, M.; Kondo, H.; Sekine, M.; Okada, N.; Nishimura, S.; Yokoyama, S.
Crystal structure of archaeosine tRNA-guanine transglycosylase
J. Mol. Biol.
318
665-677
2002
Pyrococcus horikoshii (O58843), Pyrococcus horikoshii
brenda
Nomura, Y.; Onda, Y.; Ohno, S.; Taniguchi, H.; Ando, K.; Oka, N.; Nishikawa, K.; Yokogawa, T.
Purification and comparison of native and recombinant tRNA-guanine transglycosylases from Methanosarcina acetivorans
Protein Expr. Purif.
88
13-19
2013
Methanosarcina acetivorans (Q8THU2), Methanosarcina acetivorans, Methanosarcina acetivorans DSM 2834 (Q8THU2)
brenda
Nomura, Y.; Ohno, S.; Nishikawa, K.; Yokogawa, T.
Correlation between the stability of tRNA tertiary structure and the catalytic efficiency of a tRNA-modifying enzyme, archaeal tRNA-guanine transglycosylase
Genes Cells
21
41-52
2016
Methanosarcina acetivorans
brenda
Kawamura, T.; Hirata, A.; Ohno, S.; Nomura, Y.; Nagano, T.; Nameki, N.; Yokogawa, T.; Hori, H.
Multisite-specific archaeosine tRNA-guanine transglycosylase (ArcTGT) from Thermoplasma acidophilum, a thermo-acidophilic archaeon
Nucleic Acids Res.
44
1894-1908
2016
Thermoplasma acidophilum, Thermoplasma acidophilum HO-62
brenda
Kawamura, T.; Hirata, A.; Ohno, S.; Nomura, Y.; Nagano, T.; Nameki, N.; Yokogawa, T.; Hori, H.
Multisite-specific archaeosine tRNA-guanine transglycosylase (ArcTGT) from Thermoplasma acidophilum, a thermo-acidophilic archaeon
Nucleic Acids Res.
44
1894-1908
2015
Pyrococcus horikoshii (O58843), Pyrococcus horikoshii, Thermoplasma acidophilum (Q9HI54), Thermoplasma acidophilum, Pyrococcus horikoshii OT-3 (O58843)
brenda
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