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Information on EC 2.4.2.29 - tRNA-guanosine34 preQ1 transglycosylase
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2.4.2.29 tRNA-guanosine34 preQ1 transglycosylaseIUBMB 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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Word Map
- 2.4.2.29
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anticodon
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queuosine
-
wobble
- mobilis
- trnatyr
- shigella
-
zymomonas
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hypermodified
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archaeosine
- shigellosis
- preq0
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trna-modifying
- trnaasn
- trnahis
- 7-cyano-7-deazaguanine
- minihelix
- 7-deazaguanosine
- garcia
- medicine
The enzyme appears in viruses and cellular organisms
Reaction Schemes
+
=
7-aminomethyl-7-carbaguanine34 in tRNA
+
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
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ArcTGT
guanine insertion enzyme
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guanine, queuine-tRNA transglycosylase
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Q-insertase
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QueTGT
queuine insertase
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queuine tRNA ribosyltransferase
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queuine tRNA-ribosyltransferase
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ribosyltransferase, queuine transfer ribonucleate
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TGT
transfer ribonucleate glycosyltransferase
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tRNA guanine transglycosidase
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tRNA guanine transglycosylase
tRNA transglycosylase
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tRNA-guanine transglycosylase
virulence-associated protein VACC
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TGT
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tRNA guanine transglycosylase
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tRNA-guanine transglycosylase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
guanine34 in tRNA + 7-aminomethyl-7-carbaguanine = 7-aminomethyl-7-carbaguanine34 in tRNA + guanine
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pentosyl group transfer
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PATHWAY SOURCE
PATHWAYS
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,
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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.
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CAS REGISTRY NUMBER
COMMENTARY
72162-89-1
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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
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
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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)
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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
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TGT-RNA covalent intermediate
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-
?
7-aminomethyl-7-carbaguanine + [RNAECYMA]-guanine
guanine + [RNAECYMA]-pre Q1
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hairpin RNA corresponding to the tRNAtyr anticodon stem-loop motif, TGT-RNA covalent intermediate
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-
?
guanine34 in tRNA + 7-aminomethyl-7-carbaguanine
7-aminomethyl-7-carbaguanine34 in tRNA + guanine
pre-queuine 1 + virF mRNA
?
TGT may modulate the translation of VirF via modification of the virF mRNA
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-
?
[tRNATyr]7-aminomethyl-7-carbaguanine + guanine
[tRNATyr]-guanine + 7-aminomethyl-7-carbaguanine
7-aminomethyl-7-carbaguanine + [tRNA]-guanine
guanine + [tRNA]-pre Q1
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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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-
?
7-aminomethyl-7-carbaguanine + [tRNA]-guanine
guanine + [tRNA]-pre Q1
Tyr106 in the active site is hydrogen bonded in the ligand-free structure
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?
guanine34 in tRNA + 7-aminomethyl-7-carbaguanine
7-aminomethyl-7-carbaguanine34 in tRNA + guanine
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?
guanine34 in tRNA + 7-aminomethyl-7-carbaguanine
7-aminomethyl-7-carbaguanine34 in tRNA + guanine
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?
guanine34 in tRNA + 7-aminomethyl-7-carbaguanine
7-aminomethyl-7-carbaguanine34 in tRNA + guanine
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E. coli preQ0-tRNATyr, containing7-(cyano)-7-deazaguanine in the anticodon and E. coli guaninetRNATyr containing guanosine in the anticodon are good acceptors
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ir
guanine34 in tRNA + 7-aminomethyl-7-carbaguanine
7-aminomethyl-7-carbaguanine34 in tRNA + guanine
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the enzyme catalyzes the posttranscriptional base exchange of the queuosine precursor 7-(aminomethyl)-7-deazaguanine with the genetically encoded guanine in tRNAASp, tRNAAsn, tRNAHis and tRNATyr
-
?
guanine34 in tRNA + 7-aminomethyl-7-carbaguanine
7-aminomethyl-7-carbaguanine34 in tRNA + guanine
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the enzyme exchanges the genetically encoded guanine at position 34 with a queuine precursor 7-(aminomethyl)-7-deazaguanine
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-
?
guanine34 in tRNA + 7-aminomethyl-7-carbaguanine
7-aminomethyl-7-carbaguanine34 in tRNA + guanine
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the enzyme is responsible for the posttranscriptional modification of specific tRNAs (Asn, Asp, His and Tyr) with queuine. The enzyme catalyzes base exchange of guanosine34 with 7-aminomethyl-7-deazaguanine
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?
guanine34 in tRNA + 7-aminomethyl-7-carbaguanine
7-aminomethyl-7-carbaguanine34 in tRNA + guanine
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?
guanine34 in tRNA + 7-aminomethyl-7-carbaguanine
7-aminomethyl-7-carbaguanine34 in tRNA + guanine
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?
guanine34 in tRNA + 7-aminomethyl-7-carbaguanine
7-aminomethyl-7-carbaguanine34 in tRNA + guanine
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?
guanine34 in tRNA + 7-aminomethyl-7-carbaguanine
7-aminomethyl-7-carbaguanine34 in tRNA + guanine
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the enzyme is involved in the hypermodification of cognate tRNAs, leading to the exchange of G34 by 7-methylamino-7-deazaguanine at the wobble position in the anticodon loop
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?
guanine34 in tRNA + 7-aminomethyl-7-carbaguanine
7-aminomethyl-7-carbaguanine34 in tRNA + guanine
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?
guanine34 in tRNA + 7-aminomethyl-7-carbaguanine
7-aminomethyl-7-carbaguanine34 in tRNA + guanine
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?
guanine34 in tRNA + 7-aminomethyl-7-carbaguanine
7-aminomethyl-7-carbaguanine34 in tRNA + guanine
prefers pre-queuine 1 over pre-queuine 0
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-
?
[tRNATyr]7-aminomethyl-7-carbaguanine + guanine
[tRNATyr]-guanine + 7-aminomethyl-7-carbaguanine
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?
[tRNATyr]7-aminomethyl-7-carbaguanine + guanine
[tRNATyr]-guanine + 7-aminomethyl-7-carbaguanine
TGT active site exhibits a hydrophobic patch formed by Val45 and Leu68, where the phosphate, linking ribose-34 to ribose-35, in bound tRNA is located
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?
[tRNATyr]7-aminomethyl-7-carbaguanine + guanine
[tRNATyr]-guanine + 7-aminomethyl-7-carbaguanine
Tgt dimer binds specifically to a single tRNA molecule
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?
additional information
?
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higher expression of the subunit TGT60KD in cancer cells than in normal cells. The expression levels of the TGT60KD subunit regulate enzyme activity and the level of queuosine. TGT60KD plays significant roles in carcinogenesis
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?
additional information
?
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the 60000 Da subunit of the enzyme plays a role in colon carcinogenesis
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?
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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
guanine34 in tRNA + 7-aminomethyl-7-carbaguanine
7-aminomethyl-7-carbaguanine34 in tRNA + guanine
guanine34 in tRNA + 7-aminomethyl-7-carbaguanine
7-aminomethyl-7-carbaguanine34 in tRNA + guanine
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the enzyme catalyzes the posttranscriptional base exchange of the queuosine precursor 7-(aminomethyl)-7-deazaguanine with the genetically encoded guanine in tRNAASp, tRNAAsn, tRNAHis and tRNATyr
-
?
guanine34 in tRNA + 7-aminomethyl-7-carbaguanine
7-aminomethyl-7-carbaguanine34 in tRNA + guanine
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the enzyme exchanges the genetically encoded guanine at position 34 with a queuine precursor 7-(aminomethyl)-7-deazaguanine
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?
guanine34 in tRNA + 7-aminomethyl-7-carbaguanine
7-aminomethyl-7-carbaguanine34 in tRNA + guanine
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the enzyme is responsible for the posttranscriptional modification of specific tRNAs (Asn, Asp, His and Tyr) with queuine. The enzyme catalyzes base exchange of guanosine34 with 7-aminomethyl-7-deazaguanine
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?
guanine34 in tRNA + 7-aminomethyl-7-carbaguanine
7-aminomethyl-7-carbaguanine34 in tRNA + guanine
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?
guanine34 in tRNA + 7-aminomethyl-7-carbaguanine
7-aminomethyl-7-carbaguanine34 in tRNA + guanine
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the enzyme is involved in the hypermodification of cognate tRNAs, leading to the exchange of G34 by 7-methylamino-7-deazaguanine at the wobble position in the anticodon loop
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?
guanine34 in tRNA + 7-aminomethyl-7-carbaguanine
7-aminomethyl-7-carbaguanine34 in tRNA + guanine
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?
additional information
?
-
-
higher expression of the subunit TGT60KD in cancer cells than in normal cells. The expression levels of the TGT60KD subunit regulate enzyme activity and the level of queuosine. TGT60KD plays significant roles in carcinogenesis
-
-
?
additional information
?
-
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the 60000 Da subunit of the enzyme plays a role in colon carcinogenesis
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,6-bis(methylamino)-1,4a,7,8a-tetrahydro-8H-imidazo[4,5-g]quinazolin-8-one
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2-(methylamino)-1,4a,7,8a-tetrahydro-8H-imidazo[4,5-g]quinazolin-8-one
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2-([2-(morpholin-4-yl)ethyl]amino)-1,4a,7,8a-tetrahydro-8H-imidazo[4,5-g]quinazolin-8-one
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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
2-[(2-phenylethyl)amino]-1,4a,7,8a-tetrahydro-8H-imidazo[4,5-g]quinazolin-8-one
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2-[(thiophen-2-ylmethyl)amino]-1,4a,7,8a-tetrahydro-8H-imidazo[4,5-g]quinazolin-8-one
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4-(2-[(cyclohexylmethyl)amino]ethyl)2-(methylamino)-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
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4-(2-[(cyclopentylmethyl)amino]ethyl)-2-(methylamino)-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
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5-amino-3-(5-amino-1H-[1,2,4]triazol-3-yl-sulfanyl)-phthalhydrazide
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6-(ethylamino)-2-(methylamino)-1,4a,7,8a-tetrahydro-8H-imidazo[4,5-g]quinazolin-8-one
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6-amino-2-(benzylamino)-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
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6-amino-2-(methylamino)-1,4a,7,8a-tetrahydro-8H-imidazo[4,5-g]quinazolin-8-one
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6-amino-2-(methylamino)-3-[(methylamino)methyl]-3,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
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6-amino-2-(methylamino)-3-[2-(methylamino)ethyl]-3,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
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6-amino-2-(methylamino)-4-(2-[(1-naphthylmethyl)amino]ethyl)-1,7-dihydro-8Himidazo[4,5-g]quinazolin-8-one
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6-amino-2-(methylamino)-4-(4-phenylbutyl)-1,7-dihydro-8H-imidazo-[4,5-g]quinazolin-8-one
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6-amino-2-(methylamino)-4-[(methylamino)methyl]-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
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6-amino-2-(methylamino)-4-[2-(methylamino)ethyl]-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
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6-amino-2-([2-(morpholin-4-yl)ethyl]amino)-1,4a,7,8a-tetrahydro-8H-imidazo[4,5-g]quinazolin-8-one
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6-amino-2-[(1,3-benzodioxol-5-ylmethyl)amino]-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
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6-amino-2-[(2-phenylethyl)amino]-1,4a,7,8a-tetrahydro-8H-imidazo[4,5-g]quinazolin-8-one
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6-amino-2-[(3-piperidin-1-ylpropyl)amino]-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
cannot modify the structure of the dimer interface, prevents the formation of the catalytically active Tgt:tRNA complex, and can disrupt the preformed complex
6-amino-2-[(4-morpholin-4-ylbenzyl)amino]-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
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6-amino-2-[(quinolin-4-ylmethyl)amino]-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
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6-amino-2-[(thiophen-2-ylmethyl)amino]-1,4a,7,8a-tetrahydro-8H-imidazo[4,5-g]quinazolin-8-one
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6-amino-4-(2-aminoethyl)-2-(methylamino)-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
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6-amino-4-(2-hydroxyethyl)-2-(methylamino)-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
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6-amino-4-(2-[(cycloheptylmethyl)amino]ethyl)-2-(methylamino)-1,7-dihydro-8Himidazo[4,5-g]quinazolin-8-one
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6-amino-4-(2-[(cyclohexylmethyl)amino]ethyl)-2-(methylamino)-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
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6-amino-4-(2-[(cyclopentylmethyl)amino]ethyl)-2-(methylamino)-1,7-dihydro-8Himidazo[4,5-g]quinazolin-8-one
strongest inhibitor
6-amino-4-[2-(benzylamino)ethyl]-2-(methylamino)-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
6-amino-4-[2-(methoxyphenyl)ethyl]-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
-
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6-amino-4-[2-[(cyclohexylmethyl)amino]ethyl]-2-(methylamino)-1,4a,7,8a-tetrahydro-8H-imidazo[4,5-g]quinazolin-8-one
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6-amino-4-[2-[(cyclohexylmethyl)amino]ethyl]-2-(methylamino)-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
can modify the structure of the dimer interface, prevents the formation of the catalytically active Tgt:tRNA complex, and can disrupt the preformed complex
6-amino-4-[2-[(cyclopentylmethyl)amino]ethyl]-2-(methylamino)-1,4a,7,8a-tetrahydro-8H-imidazo[4,5-g]quinazolin-8-one
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6-amino-4-[2-[(cyclopentylmethyl)amino]ethyl]-2-(methylamino)-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
addresses a hydrophobic subpocket close to the dimer interface that may affect quarternary structure formation, prevents the formation of the catalytically active Tgt:tRNA complex, and can disrupt the preformed complex
methyl 1-[(dimethylamino)sulfonyl]-2-(methylamino)-5-nitro-1H-benz-imidazol-6-carboxylate
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methyl 5-amino-1-[(dimethylamino)sulfonyl]-2-(methylamino)-1H-benz-imidazol-6-carboxylate
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methyl 5-amino-1-[(dimethylamino)sulfonyl]-2-(methylamino)-4-(4-phenyl-1-butyn-1-yl)-1H-benzimidazole-6-carboxylate
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methyl 5-amino-1-[(dimethylamino)sulfonyl]-2-(methylamino)-4-(4-phenylbutyl)-1Hbenzimidazole-6-carboxylate
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methyl 5-amino-1-[(dimethylamino)sulfonyl]-2-(methylamino)-4-vinyl-1H-benzimidazole-6-carboxylate
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methyl 5-amino-1-[(dimethylamino)sulfonyl]-2-(methylamino)-4-[2-(methylamino)ethyl]-1H-benzimidazole-6-carboxylate
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methyl 5-amino-1-[(dimethylamino)sulfonyl]-2-(methylamino)-4-{2-[(1-naphthylmethyl)amino]ethyl}-1H-benzimidazole-6-carboxylate
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methyl 5-amino-1-[(dimethylamino)sulfonyl]-4-(2-hydroxyethyl)-2-(methylamino)-1H-benzimidazole-6-carboxylate
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methyl 5-amino-1-[(dimethylamino)sulfonyl]-4-iodo-2-(methylamino)-1H-benzimidazole-6-carboxylate
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methyl 5-amino-1-[(dimethylamino)sulfonyl]-4-[2-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)ethyl]-2-(methylamino)-1H-benzimidazole-6-carboxylate
-
methyl 5-amino-4-(2-aminoethyl)-1-[(dimethylamino)sulfonyl]-2-(methylamino)-1H-benzimidazole-6-carboxylate
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methyl 5-amino-4-(2-[(cycloheptylmethyl)amino]ethyl)-1-[(dimethyl-amino)sulfonyl]-2-(methylamino)-1H-benzimidazole-6-carboxylate
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methyl 5-amino-4-(2-[(cyclohexylmethyl)amino]ethyl)-1-[(dimethylamino)sulfonyl]-2-(methylamino)-1H-benzimidazole-6-carboxylate
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methyl 5-amino-4-(2-[(cyclopentylmethyl)amino]ethyl)-1-[(dimethylamino)sulfonyl]-2-(methylamino)-1H-benzimidazole-6-carboxylate
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methyl 5-amino-4-(2-[benzyl(methyl)amino]ethyl)-1-[(dimethylamino)sulfonyl]-2-(methylamino)-1H-benzimidazole-6-carboxylate
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methyl 5-amino-4-[2-(benzylamino)ethyl]-1-[(dimethylamino)sulfonyl]-2-(methylamino)-1H-benzimidazole-6-carboxylate
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methyl 5-amino-4-{2-[(cyclohexylcarbonyl)amino]ethyl}-1-[(dimethylamino)sulfonyl]-2-(methylamino)-1H-benzimidazole-6-carboxylate
-
methyl 8-benzyl-3-[(dimethylamino)sulfonyl]-2-(methylamino)-3,6,7,8,9,10-hexahydroimidazo[4,5-g][1,3]benzodiazepine-5-carboxylate
-
N-(2-[6-amino-2-(methylamino)-8-oxo-7,8-dihydro-1H-imidazo[4,5-g]quinazolin-4-yl]ethyl)cyclohexanecarboxamide
-
additional information
-
design, synthesis, and in vitro evaluation of novel tricyclic TGT inhibitors based on the lin-benzoguanine scaffold
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6-amino-2-(methylamino)-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
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6-amino-2-(methylamino)-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
-
6-amino-2-[(2-morpholin-4-ylethyl)amino]-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
-
6-amino-2-[(2-morpholin-4-ylethyl)amino]-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
-
6-amino-2-[(2-phenylethyl)amino]-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
-
6-amino-2-[(2-phenylethyl)amino]-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
-
6-amino-2-[(naphthalen-1-ylmethyl)amino]-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
-
6-amino-2-[(naphthalen-1-ylmethyl)amino]-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
-
6-amino-2-[(thiophen-2-ylmethyl)amino]-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
-
6-amino-2-[(thiophen-2-ylmethyl)amino]-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
-
6-amino-3-(2-phenylethyl)-3,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
-
-
6-amino-3-(2-phenylethyl)-3,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
-
6-amino-4-(2-phenylethyl)-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
-
-
6-amino-4-(2-phenylethyl)-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
-
6-amino-4-[2-(4-methoxyphenyl)ethyl]-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
-
6-amino-4-[2-(4-methoxyphenyl)ethyl]-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
can modify the structure of the dimer interface, prevents the formation of the catalytically active Tgt:tRNA complex, and can disrupt the preformed complex
6-amino-4-[2-(4-methylphenyl)ethyl]-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
-
-
6-amino-4-[2-(4-methylphenyl)ethyl]-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
-
6-amino-4-[2-(benzylamino)ethyl]-2-(methylamino)-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
-
6-amino-4-[2-(benzylamino)ethyl]-2-(methylamino)-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
addresses a hydrophobic subpocket close to the dimer interface that may affect quarternary structure formation, prevents the formation of the catalytically active Tgt:tRNA complex, and can disrupt the preformed complex
6-aminoimidazol[4,5-g]quinazolin-8(7H)-one
mixed competitive-uncompetitive inhibition with respect to tRNA binding
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Breast Neoplasms
tRNA Queuosine Modification Enzyme Modulates the Growth and Microbiome Recruitment to Breast Tumors.
Carcinogenesis
tRNA Queuosine Modification Enzyme Modulates the Growth and Microbiome Recruitment to Breast Tumors.
Colonic Neoplasms
Absence of tRNA-guanine transglycosylase in a human colon adenocarcinoma cell line.
Colonic Neoplasms
Elevated expression level of 60-kDa subunit of tRNA-guanine transglycosylase in colon cancer.
Dysentery, Bacillary
A new target for shigellosis: rational design and crystallographic studies of inhibitors of tRNA-guanine transglycosylase.
Dysentery, Bacillary
An Immucillin-based Transition State-Analogous Inhibitor of tRNA-Guanine Transglycosylase (TGT).
Dysentery, Bacillary
Crystal structure analysis and in silico pKa calculations suggest strong pKa shifts of ligands as driving force for high-affinity binding to TGT.
Dysentery, Bacillary
Fragment Screening Hit Draws Attention to a Novel Transient Pocket Adjacent to the Recognition Site of the tRNA-Modifying Enzyme TGT.
Dysentery, Bacillary
High-Affinity Inhibitors of tRNA-Guanine Transglycosylase Replacing the Function of a Structural Water Cluster.
Dysentery, Bacillary
High-affinity inhibitors of Zymomonas mobilis tRNA-guanine transglycosylase through convergent optimization.
Dysentery, Bacillary
How to replace the residual solvation shell of polar active site residues to achieve nanomolar inhibition of tRNA-guanine transglycosylase.
Dysentery, Bacillary
Launching Spiking Ligands into a Protein-Protein Interface: A Promising Strategy to Destabilize and Break Interface Formation in a tRNA Modifying Enzyme.
Dysentery, Bacillary
Replacement of water molecules in a phosphate binding site by furanoside-appended lin-benzoguanine ligands of tRNA-guanine transglycosylase (TGT).
Dysentery, Bacillary
Soaking suggests "alternative facts": Only co-crystallization discloses major ligand-induced interface rearrangements of a homodimeric tRNA-binding protein indicating a novel mode-of-inhibition.
Dysentery, Bacillary
Structure-based drug design: exploring the proper filling of apolar pockets at enzyme active sites.
Dysentery, Bacillary
Swapping Interface Contacts in the Homodimeric tRNA-Guanine Transglycosylase: An Option for Functional Regulation.
Dysentery, Bacillary
Targeting a Cryptic Pocket in a Protein-Protein Contact by Disulfide-Induced Rupture of a Homodimeric Interface.
Dysentery, Bacillary
Unraveling a Ligand-Induced Twist of a Homodimeric Enzyme by Pulsed Electron-Electron Double Resonance.
Foodborne Diseases
High-affinity inhibitors of Zymomonas mobilis tRNA-guanine transglycosylase through convergent optimization.
Foodborne Diseases
Replacement of water molecules in a phosphate binding site by furanoside-appended lin-benzoguanine ligands of tRNA-guanine transglycosylase (TGT).
Liver Neoplasms, Experimental
Detection of unique tRNA species in tumor tissues by Escherichia coli guanine insertion enzyme.
Multiple Sclerosis
The human tRNA-guanine transglycosylase displays promiscuous nucleobase preference but strict tRNA specificity.
Neoplasms
Characterization and analysis of oncofetal tRNA and its possible application for cancer diagnosis and therapy.
Neoplasms
Detection of unique tRNA species in tumor tissues by Escherichia coli guanine insertion enzyme.
Neoplasms
tRNA Queuosine Modification Enzyme Modulates the Growth and Microbiome Recruitment to Breast Tumors.
trna-guanosine34 preq1 transglycosylase
deficiency
tRNA Queuosine Modification Enzyme Modulates the Growth and Microbiome Recruitment to Breast Tumors.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0012
guanine
wild type enzyme, in 200 mM HEPES, pH 7.3, 20 mM MgCl2
0.0033
guanine
mutant enzyme E235Q, in 200 mM HEPES, pH 7.3, 20 mM MgCl2
0.0005
pre-queuine 0
mutant enzyme E235Q, Km less than 0.0005 mM, in 200 mM HEPES, pH 7.3, 20 mM MgCl2
0.0009
pre-queuine 0
wild type enzyme, in 200 mM HEPES, pH 7.3, 20 mM MgCl2
0.0007
pre-queuine 1
wild type enzyme, in 200 mM HEPES, pH 7.3, 20 mM MgCl2
0.032
pre-queuine 1
mutant enzyme E235Q, in 200 mM HEPES, pH 7.3, 20 mM MgCl2
0.0009
tRNA guanine
wild type enzyme, in 200 mM HEPES, pH 7.3, 20 mM MgCl2
0.001
tRNA guanine
mutant enzyme E235Q, in 200 mM HEPES, pH 7.3, 20 mM MgCl2