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Information on EC 2.4.2.29 - tRNA-guanosine34 preQ1 transglycosylase and Organism(s) Escherichia coli and UniProt Accession P0A847

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EC Tree
     2 Transferases
         2.4 Glycosyltransferases
             2.4.2 Pentosyltransferases
                2.4.2.29 tRNA-guanosine34 preQ1 transglycosylase
IUBMB Comments
Certain prokaryotic and eukaryotic tRNAs contain the modified base queuine at position 34. In eubacteria, which produce queuine de novo, the enzyme catalyses the exchange of guanine with the queuine precursor preQ1, which is ultimately modified to queuosine . The enzyme can also use an earlier intermediate, preQ0, to replace guanine in unmodified tRNATyr and tRNAAsn . This enzyme acts after EC 1.7.1.13, preQ1 synthase, in the queuine-biosynthesis pathway. cf. EC 2.4.2.64, tRNA-guanosine34 queuine transglycosylase.
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This record set is specific for:
Escherichia coli
UNIPROT: P0A847
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
trna-guanine transglycosylase, arctgt, qtrt1, trna guanine transglycosylase, trna transglycosylase, guanine insertion enzyme, q-insertase, queuine trna-ribosyltransferase, trna-guanine 34 transglycosylase, queuine trna ribosyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
guanine insertion enzyme
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-
-
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guanine, queuine-tRNA transglycosylase
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-
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Q-insertase
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queuine insertase
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queuine tRNA ribosyltransferase
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queuine tRNA-ribosyltransferase
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-
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ribosyltransferase, queuine transfer ribonucleate
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-
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transfer ribonucleate glycosyltransferase
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-
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tRNA guanine transglycosidase
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tRNA guanine transglycosylase
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-
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tRNA transglycosylase
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-
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tRNA-guanine transglycosylase
virulence-associated protein VACC
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pentosyl group transfer
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-
-
-
PATHWAY SOURCE
PATHWAYS
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-, -
SYSTEMATIC NAME
IUBMB Comments
tRNA-guanosine34:7-aminomethyl-7-deazaguanine tRNA-D-ribosyltransferase
Certain prokaryotic and eukaryotic tRNAs contain the modified base queuine at position 34. In eubacteria, which produce queuine de novo, the enzyme catalyses the exchange of guanine with the queuine precursor preQ1, which is ultimately modified to queuosine [5]. The enzyme can also use an earlier intermediate, preQ0, to replace guanine in unmodified tRNATyr and tRNAAsn [1]. This enzyme acts after EC 1.7.1.13, preQ1 synthase, in the queuine-biosynthesis pathway. cf. EC 2.4.2.64, tRNA-guanosine34 queuine transglycosylase.
CAS REGISTRY NUMBER
COMMENTARY hide
72162-89-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
guanine34 in tRNA + 7-aminomethyl-7-carbaguanine
7-aminomethyl-7-carbaguanine34 in tRNA + guanine
show the reaction diagram
-
-
-
?
guanine34 in tRNA + queuine
queuine34 in tRNA + guanine
show the reaction diagram
-
-
-
?
pre-queuine 1 + virF minihelix RNA
?
show the reaction diagram
-
-
-
?
pre-queuine 1 + virF mRNA
?
show the reaction diagram
TGT may modulate the translation of VirF via modification of the virF mRNA
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-
?
2-amino-5-(fluoromethyl)pyrrolo[2,3-d]pyrimidin-4(3H)-one + tRNAguanine
guanine + tRNA2-amino-5-(fluoromethyl)pyrrolo[2,3-d]pyrimidin-4(3H)-one
show the reaction diagram
-
2-amino-5-(fluoromethyl)pyrrolo[2,3-d]pyrimidin-4(3H)-one appears to partition between: 1. normal turnover, 2. inactivation, 3. an alternative processing to an unidentrified fluoride-released product
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-
?
7-(cyano)-7-deazaguanine + tRNAguanine
guanine + tRNA(7-(cyano)-7-deazaguanine)
show the reaction diagram
-
-
inserted 7-(cyano)-7-deazaguanine is located in the first position of the anticodon
?
7-aminomethyl-7-carbaguanine + [RNAECYMA]-2'-deoxyguanine 34
guanine + [RNAECYMA]-2'-deoxy-pre Q1
show the reaction diagram
-
TGT-RNA covalent intermediate
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-
?
7-aminomethyl-7-carbaguanine + [RNAECYMA]-guanine
guanine + [RNAECYMA]-pre Q1
show the reaction diagram
-
hairpin RNA corresponding to the tRNAtyr anticodon stem-loop motif, TGT-RNA covalent intermediate
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-
?
7-aminomethyl-7-carbaguanine + [tRNA]-guanine
guanine + [tRNA]-pre Q1
show the reaction diagram
-
the TGT-RNA covalent complex is kinetically capable of occurring on the TGT reaction pathway. Dissociation of product RNA from the enzyme is overall rate-limiting in the steady state. Role for the 2'-hydroxyl group of the ribose in the TGT reaction
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-
?
guanine + tRNAguanine
tRNAguanine + guanine
show the reaction diagram
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-
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-
r
guanine34 in tRNA + 7-aminomethyl-7-carbaguanine
7-aminomethyl-7-carbaguanine34 in tRNA + guanine
show the reaction diagram
additional information
?
-
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
guanine34 in tRNA + 7-aminomethyl-7-carbaguanine
7-aminomethyl-7-carbaguanine34 in tRNA + guanine
show the reaction diagram
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-amino-5-(fluoromethyl)pyrrolo[2,3-d]pyrimidin-4(3H)-one
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inactivation and competitive inhibition. 2-amino-5-(fluoromethyl)pyrrolo[2,3-d]pyrimidin-4(3H)-one appears to partition between: 1. normal turnover, 2. inactivation, 3. an alternative processing to an unidentrified fluoride-released product
dimethylsuberimidate
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inactivates by cross-linking, tRNA protects
ethylacetimidate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00016
guanine34 in tRNA
at pH 7.3
0.00087
virF minihelix RNA
at pH 7.3
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0.0018
virF mRNA
at pH 7.3
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0.152
2-amino-5-(fluoromethyl)pyrrolo[2,3-d]pyrimidin-4(3H)-one
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-
0.000014
7-(aminomethyl)-7-deazaguanine
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-
0.000053 - 0.00632
guanine
0.00011 - 0.00051
tRNA
0.00032 - 0.0097
tRNA(Tyr)
0.00262
[RNAECYMA]-2'-deoxyguanine 34
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0.00287
[RNAECYMA]-guanine
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.004
guanine34 in tRNA
at pH 7.3
0.00033
virF minihelix RNA
at pH 7.3
-
0.00011
virF mRNA
at pH 7.3
-
0.461
2-amino-5-(fluoromethyl)pyrrolo[2,3-d]pyrimidin-4(3H)-one
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-
0.59 - 7.57
guanine
0.71 - 5.85
tRNA
0.011
[RNAECYMA]-2'-deoxyguanine 34
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0.0094
[RNAECYMA]-guanine
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.114 - 0.136
2-amino-5-(fluoromethyl)pyrrolo[2,3-d]pyrimidin-4(3H)-one
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D264N
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is inactive and incapable of forming the covalent intermediate, while maintaining the ability to bind noncovalently to RNA
D89A
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less than 1% of the activity of the histidine-tagged wild-type enzyme
D89C
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less than 1% of the activity of the histidine-tagged wild-type enzyme
D89E
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about 50% of the activity of the histidine-tagged wild-type enzyme
D89N
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less than 1% of the activity of the histidine-tagged wild-type enzyme
S90A
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activity of the mutant enzyme is to low to determine Vmax and Km-value
S90C
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30fold increase in Km-value for tRNATyr and 4fold increase in Km-value for guanine
S90F
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mutant enzyme has no detectable solubility and reduced solubility
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
His-tagged TGT purified by Ni2+ affinity chromatography
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mutant enzyme S90F, S90C and S90A
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wild-type and mutant enzymes D89E, D89D, D89C and D89A
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
mutant enzymes S90F and S90C
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overexpression of D89E, D89D, D89C and D89A in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Okada, N.; Noguchi, S.; Kasai, H.; Shindo-Okada, N.; Ohgi, T.; Goto, T.; Nishimura, S.
Novel mechanism of post-transcriptional modification of tRNA. Insertion of bases of Q precursors into tRNA by a specific tRNA transglycosylase reaction
J. Biol. Chem.
254
3067-3073
1979
Escherichia coli
Manually annotated by BRENDA team
Garcia, G.A.; Koch, K.A.; Chong, S.
tRNA-guanine transglycosylase from Escherichia coli. Overexpression, purification and quaternary structure
J. Mol. Biol.
231
489-497
1993
Escherichia coli
Manually annotated by BRENDA team
Kittendorf, J.D.; Barcomb, L.M.; Nonekowski, S.T.; Garcia, G.A.
tRNA-guanine transglycosylase from Escherichia coli: Molecular mechanism and role of aspartate 89
Biochemistry
40
14123-14133
2001
Escherichia coli
Manually annotated by BRENDA team
Reuter, K.; Chong, S.; Ullrich, F.; Kersten, H.; Garcia, G.A.
Serine 90 is required for enzymic activity by tRNA-guanine transglycosylase from Escherichia coli
Biochemistry
33
7041-7046
1994
Escherichia coli
Manually annotated by BRENDA team
Hoops, G.C.; Townsend, L.B.; Garcia, G.A.
Mechanism-based inactivation of tRNA-guanine transglycosylase from Escherichia coli by 2-amino-5-(fluoromethyl)pyrrolo[2,3-d]pyrimidin-4(3H)-one
Biochemistry
34
15539-15544
1995
Escherichia coli
Manually annotated by BRENDA team
Nonekowski, S.T.; Garcia, G.A.
tRNA recognition by tRNA-guanine transglycosylase from escherichia coli: the role of U33 in U-G-U sequence recognition
RNA
7
1432-1441
2001
Escherichia coli
Manually annotated by BRENDA team
Stengl, B.; Reuter, K.; Klebe, G.
Mechanism and substrate specificity of tRNA-guanine transglycosylases (TGTs): tRNA-modifying enzymes from the three different kingdoms of life share a common catalytic mechanism
Chembiochem
6
1926-1939
2005
Escherichia coli, Homo sapiens, Schizosaccharomyces pombe, Zymomonas mobilis (P28720)
Manually annotated by BRENDA team
Hurt, J.K.; Olgen, S.; Garcia, G.A.
Site-specific modification of Shigella flexneri virF mRNA by tRNA-guanine transglycosylase in vitro
Nucleic Acids Res.
35
4905-4913
2007
Escherichia coli (P0A847), Escherichia coli
Manually annotated by BRENDA team
Garcia, G.A.; Chervin, S.M.; Kittendorf, J.D.
Identification of the rate-determining step of tRNA-guanine transglycosylase from Escherichia coli
Biochemistry
48
11243-11251
2009
Escherichia coli
Manually annotated by BRENDA team