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Information on EC 2.4.2.29 - tRNA-guanosine34 preQ1 transglycosylase and Organism(s) Zymomonas mobilis and UniProt Accession P28720
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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
-
queuosine
-
wobble
- mobilis
- trnatyr
- shigella
-
zymomonas
-
hypermodified
-
archaeosine
- shigellosis
- preq0
-
trna-modifying
- trnaasn
- trnahis
- 7-cyano-7-deazaguanine
- minihelix
- 7-deazaguanosine
- garcia
- medicine
The taxonomic range for the selected organisms is: Zymomonas mobilis
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
guanine insertion enzyme
-
-
-
-
guanine, queuine-tRNA transglycosylase
-
-
-
-
Q-insertase
-
-
-
-
queuine insertase
-
-
-
-
queuine tRNA ribosyltransferase
-
-
-
-
queuine tRNA-ribosyltransferase
-
-
-
-
ribosyltransferase, queuine transfer ribonucleate
-
-
-
-
TGT
-
-
-
-
transfer ribonucleate glycosyltransferase
-
-
-
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tRNA guanine transglycosidase
-
-
-
-
tRNA guanine transglycosylase
-
-
-
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tRNA transglycosylase
-
-
-
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tRNA-guanine transglycosylase
-
-
-
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virulence-associated protein VACC
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pentosyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
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
72162-89-1
-
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
7-aminomethyl-7-carbaguanine + [tRNA]-guanine
guanine + [tRNA]-pre Q1
Tyr106 in the active site is hydrogen bonded in the ligand-free structure
-
-
?
guanine34 in tRNA + 7-aminomethyl-7-carbaguanine
7-aminomethyl-7-carbaguanine34 in tRNA + guanine
[tRNATyr]7-aminomethyl-7-carbaguanine + guanine
[tRNATyr]-guanine + 7-aminomethyl-7-carbaguanine
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
-
-
-
?
guanine34 in tRNA + 7-aminomethyl-7-carbaguanine
7-aminomethyl-7-carbaguanine34 in tRNA + guanine
prefers pre-queuine 1 over pre-queuine 0
-
-
?
[tRNATyr]7-aminomethyl-7-carbaguanine + guanine
[tRNATyr]-guanine + 7-aminomethyl-7-carbaguanine
-
-
-
?
[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
-
-
?
[tRNATyr]7-aminomethyl-7-carbaguanine + guanine
[tRNATyr]-guanine + 7-aminomethyl-7-carbaguanine
Tgt dimer binds specifically to a single tRNA molecule
-
-
?
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
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,6-bis(methylamino)-1,4a,7,8a-tetrahydro-8H-imidazo[4,5-g]quinazolin-8-one
-
2-(methylamino)-1,4a,7,8a-tetrahydro-8H-imidazo[4,5-g]quinazolin-8-one
-
2-([2-(morpholin-4-yl)ethyl]amino)-1,4a,7,8a-tetrahydro-8H-imidazo[4,5-g]quinazolin-8-one
-
2-[(2-phenylethyl)amino]-1,4a,7,8a-tetrahydro-8H-imidazo[4,5-g]quinazolin-8-one
-
2-[(thiophen-2-ylmethyl)amino]-1,4a,7,8a-tetrahydro-8H-imidazo[4,5-g]quinazolin-8-one
-
4-(2-[(cyclohexylmethyl)amino]ethyl)2-(methylamino)-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
-
4-(2-[(cyclopentylmethyl)amino]ethyl)-2-(methylamino)-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
-
6-(ethylamino)-2-(methylamino)-1,4a,7,8a-tetrahydro-8H-imidazo[4,5-g]quinazolin-8-one
-
6-amino-2-(methylamino)-1,4a,7,8a-tetrahydro-8H-imidazo[4,5-g]quinazolin-8-one
-
6-amino-2-(methylamino)-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
-
6-amino-2-(methylamino)-3-[(methylamino)methyl]-3,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
-
6-amino-2-(methylamino)-3-[2-(methylamino)ethyl]-3,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
-
6-amino-2-(methylamino)-4-(2-[(1-naphthylmethyl)amino]ethyl)-1,7-dihydro-8Himidazo[4,5-g]quinazolin-8-one
-
6-amino-2-(methylamino)-4-(4-phenylbutyl)-1,7-dihydro-8H-imidazo-[4,5-g]quinazolin-8-one
-
6-amino-2-(methylamino)-4-[(methylamino)methyl]-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
-
6-amino-2-(methylamino)-4-[2-(methylamino)ethyl]-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
-
6-amino-2-([2-(morpholin-4-yl)ethyl]amino)-1,4a,7,8a-tetrahydro-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]-1,4a,7,8a-tetrahydro-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-[(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-[(naphthalen-1-ylmethyl)amino]-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
-
6-amino-2-[(thiophen-2-ylmethyl)amino]-1,4a,7,8a-tetrahydro-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-4-(2-aminoethyl)-2-(methylamino)-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
-
6-amino-4-(2-hydroxyethyl)-2-(methylamino)-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-[(cycloheptylmethyl)amino]ethyl)-2-(methylamino)-1,7-dihydro-8Himidazo[4,5-g]quinazolin-8-one
-
6-amino-4-(2-[(cyclohexylmethyl)amino]ethyl)-2-(methylamino)-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
-
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-(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-[(cyclohexylmethyl)amino]ethyl]-2-(methylamino)-1,4a,7,8a-tetrahydro-8H-imidazo[4,5-g]quinazolin-8-one
-
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
-
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
-
methyl 5-amino-1-[(dimethylamino)sulfonyl]-2-(methylamino)-1H-benz-imidazol-6-carboxylate
-
methyl 5-amino-1-[(dimethylamino)sulfonyl]-2-(methylamino)-4-(4-phenyl-1-butyn-1-yl)-1H-benzimidazole-6-carboxylate
-
methyl 5-amino-1-[(dimethylamino)sulfonyl]-2-(methylamino)-4-(4-phenylbutyl)-1Hbenzimidazole-6-carboxylate
-
methyl 5-amino-1-[(dimethylamino)sulfonyl]-2-(methylamino)-4-vinyl-1H-benzimidazole-6-carboxylate
-
methyl 5-amino-1-[(dimethylamino)sulfonyl]-2-(methylamino)-4-[2-(methylamino)ethyl]-1H-benzimidazole-6-carboxylate
-
methyl 5-amino-1-[(dimethylamino)sulfonyl]-2-(methylamino)-4-{2-[(1-naphthylmethyl)amino]ethyl}-1H-benzimidazole-6-carboxylate
-
methyl 5-amino-1-[(dimethylamino)sulfonyl]-4-(2-hydroxyethyl)-2-(methylamino)-1H-benzimidazole-6-carboxylate
-
methyl 5-amino-1-[(dimethylamino)sulfonyl]-4-iodo-2-(methylamino)-1H-benzimidazole-6-carboxylate
-
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
-
methyl 5-amino-4-(2-[(cycloheptylmethyl)amino]ethyl)-1-[(dimethyl-amino)sulfonyl]-2-(methylamino)-1H-benzimidazole-6-carboxylate
-
methyl 5-amino-4-(2-[(cyclohexylmethyl)amino]ethyl)-1-[(dimethylamino)sulfonyl]-2-(methylamino)-1H-benzimidazole-6-carboxylate
-
methyl 5-amino-4-(2-[(cyclopentylmethyl)amino]ethyl)-1-[(dimethylamino)sulfonyl]-2-(methylamino)-1H-benzimidazole-6-carboxylate
-
methyl 5-amino-4-(2-[benzyl(methyl)amino]ethyl)-1-[(dimethylamino)sulfonyl]-2-(methylamino)-1H-benzimidazole-6-carboxylate
-
methyl 5-amino-4-[2-(benzylamino)ethyl]-1-[(dimethylamino)sulfonyl]-2-(methylamino)-1H-benzimidazole-6-carboxylate
-
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
-
5-amino-3-(5-amino-1H-[1,2,4]triazol-3-yl-sulfanyl)-phthalhydrazide
-
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-(4-methylphenyl)ethyl]-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
-
-
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-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-(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
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
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0041
(6-aminoimidazol[4,5-g]quinazolin-8(7H)-one)
competitive inhibition, in 200 mM HEPES buffer (pH 7.3), 20 mM MgCl2
0.02805
2,6-bis(methylamino)-1,4a,7,8a-tetrahydro-8H-imidazo[4,5-g]quinazolin-8-one
pH 7.3, 37°C
0.000077
2,6-diamino-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
-
0.0026
2,6-diamino-8-(2-phenylethyl)quinazolin-4(3H)-one
competitive inhibition, in 200 mM HEPES buffer (pH 7.3), 20 mM MgCl2
0.0015
2,6-diaminoquinazolin-4(3H)-one
competitive inhibition, in 200 mM HEPES buffer (pH 7.3), 20 mM MgCl2
0.0065
2-(methylamino)-1,4a,7,8a-tetrahydro-8H-imidazo[4,5-g]quinazolin-8-one
pH 7.3, 37°C
0.0041
2-([2-(morpholin-4-yl)ethyl]amino)-1,4a,7,8a-tetrahydro-8H-imidazo[4,5-g]quinazolin-8-one
pH 7.3, 37°C
0.001
2-amino-8-methylquinazolin-4(3H)-one
competitive inhibition, in 200 mM HEPES buffer (pH 7.3), 20 mM MgCl2
0.0021
2-aminoquinazolin-4(3H)-one
competitive inhibition, in 200 mM HEPES buffer (pH 7.3), 20 mM MgCl2
0.000058
2-methylamino-lin-benzoguanine
at 37°C, pH 7.3, in 200 mM HEPES buffer, 20 mM MgCl2, 2.95 mM Tween 20 containing both substrates
0.0037
2-[(2-phenylethyl)amino]-1,4a,7,8a-tetrahydro-8H-imidazo[4,5-g]quinazolin-8-one
pH 7.3, 37°C
0.0029
2-[(thiophen-2-ylmethyl)amino]-1,4a,7,8a-tetrahydro-8H-imidazo[4,5-g]quinazolin-8-one
pH 7.3, 37°C
0.0011
4-(2-[(cyclohexylmethyl)amino]ethyl)2-(methylamino)-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
pH 7.3, 37°C
0.00074
4-(2-[(cyclopentylmethyl)amino]ethyl)-2-(methylamino)-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
pH 7.3, 37°C
0.04083
6-(ethylamino)-2-(methylamino)-1,4a,7,8a-tetrahydro-8H-imidazo[4,5-g]quinazolin-8-one
pH 7.3, 37°C
0.000058
6-amino-2-(methylamino)-1,4a,7,8a-tetrahydro-8H-imidazo[4,5-g]quinazolin-8-one
pH 7.3, 37°C
0.000058
6-amino-2-(methylamino)-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
-
0.000105
6-amino-2-(methylamino)-4-(2-[(1-naphthylmethyl)amino]ethyl)-1,7-dihydro-8Himidazo[4,5-g]quinazolin-8-one
at 37°C, pH 7.3, in 200 mM HEPES buffer, 20 mM MgCl2, 2.95 mM Tween 20 containing both substrates
0.000235
6-amino-2-(methylamino)-4-(4-phenylbutyl)-1,7-dihydro-8H-imidazo-[4,5-g]quinazolin-8-one
at 37°C, pH 7.3, in 200 mM HEPES buffer, 20 mM MgCl2, 2.95 mM Tween 20 containing both substrates
0.000026
6-amino-2-(methylamino)-4-[2-(methylamino)ethyl]-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
at 37°C, pH 7.3, in 200 mM HEPES buffer, 20 mM MgCl2, 2.95 mM Tween 20 containing both substrates
0.000006
6-amino-2-([2-(morpholin-4-yl)ethyl]amino)-1,4a,7,8a-tetrahydro-8H-imidazo[4,5-g]quinazolin-8-one
pH 7.3, 37°C
0.0015
6-amino-2-methyl-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
-
0.000006
6-amino-2-[(2-morpholin-4-ylethyl)amino]-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
-
0.00001
6-amino-2-[(2-phenylethyl)amino]-1,4a,7,8a-tetrahydro-8H-imidazo[4,5-g]quinazolin-8-one
pH 7.3, 37°C
0.00001
6-amino-2-[(2-phenylethyl)amino]-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
-
0.000055
6-amino-2-[(naphthalen-1-ylmethyl)amino]-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
-
0.000035
6-amino-2-[(thiophen-2-ylmethyl)amino]-1,4a,7,8a-tetrahydro-8H-imidazo[4,5-g]quinazolin-8-one
pH 7.3, 37°C
0.000035
6-amino-2-[(thiophen-2-ylmethyl)amino]-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
-
0.0073
6-amino-3-(2-phenylethyl)-3,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
competitive inhibition, in 200 mM HEPES buffer (pH 7.3), 20 mM MgCl2
0.015
6-amino-3-benzyl-3,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
competitive inhibition, in 200 mM HEPES buffer (pH 7.3), 20 mM MgCl2
0.000055
6-amino-4-(2-aminoethyl)-2-(methylamino)-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
at 37°C, pH 7.3, in 200 mM HEPES buffer, 20 mM MgCl2, 2.95 mM Tween 20 containing both substrates
0.000097
6-amino-4-(2-hydroxyethyl)-2-(methylamino)-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
at 37°C, pH 7.3, in 200 mM HEPES buffer, 20 mM MgCl2, 2.95 mM Tween 20 containing both substrates
0.05
6-amino-4-(2-phenylethyl)-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
in 200 mM HEPES buffer (pH 7.3), 20 mM MgCl2
0.0000025
6-amino-4-(2-[(cycloheptylmethyl)amino]ethyl)-2-(methylamino)-1,7-dihydro-8Himidazo[4,5-g]quinazolin-8-one
at 37°C, pH 7.3, in 200 mM HEPES buffer, 20 mM MgCl2, 2.95 mM Tween 20 containing both substrates
0.000004
6-amino-4-(2-[(cyclohexylmethyl)amino]ethyl)-2-(methylamino)-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
at 37°C, pH 7.3, in 200 mM HEPES buffer, 20 mM MgCl2, 2.95 mM Tween 20 containing both substrates
0.000002
6-amino-4-(2-[(cyclopentylmethyl)amino]ethyl)-2-(methylamino)-1,7-dihydro-8Himidazo[4,5-g]quinazolin-8-one
at 37°C, pH 7.3, in 200 mM HEPES buffer, 20 mM MgCl2, 2.95 mM Tween 20 containing both substrates
0.029
6-amino-4-phenyl-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
competitive inhibition, in 200 mM HEPES buffer (pH 7.3), 20 mM MgCl2
0.0037
6-amino-4-[2-(4-methoxyphenyl)ethyl]-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
competitive inhibition, in 200 mM HEPES buffer (pH 7.3), 20 mM MgCl2
0.0069
6-amino-4-[2-(4-methylphenyl)ethyl]-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
competitive inhibition, in 200 mM HEPES buffer (pH 7.3), 20 mM MgCl2
0.000025
6-amino-4-[2-(benzylamino)ethyl]-2-(methylamino)-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
at 37°C, pH 7.3, in 200 mM HEPES buffer, 20 mM MgCl2, 2.95 mM Tween 20 containing both substrates
0.000004
6-amino-4-[2-[(cyclohexylmethyl)amino]ethyl]-2-(methylamino)-1,4a,7,8a-tetrahydro-8H-imidazo[4,5-g]quinazolin-8-one
pH 7.3, 37°C
0.000002
6-amino-4-[2-[(cyclopentylmethyl)amino]ethyl]-2-(methylamino)-1,4a,7,8a-tetrahydro-8H-imidazo[4,5-g]quinazolin-8-one
pH 7.3, 37°C
0.0014
N-(2-[6-amino-2-(methylamino)-8-oxo-7,8-dihydro-1H-imidazo[4,5-g]quinazolin-4-yl]ethyl)cyclohexanecarboxamide
at 37°C, pH 7.3, in 200 mM HEPES buffer, 20 mM MgCl2, 2.95 mM Tween 20 containing both substrates
0.0028
4-(2-phenylethyl)-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
-
37°C, pH 7.3
0.038
5-amino-3-(1H-[1,2,4]triazole-3-yl-sulfanyl)-phthalhydrazide
-
0.0073
6-amino-3-(2-phenylethyl)-3,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
-
37°C, pH 7.3, Kic
0.015
6-amino-3-benzyl-3,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
-
37°C, pH 7.3, Kic
0.001
6-amino-4-(2-phenylethyl)-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
-
37°C, pH 7.3, Kic
0.029
6-amino-4-phenyl-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
-
37°C, pH 7.3, Kic
0.0069
6-amino-4-[2-(4-methylphenyl)ethyl]-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
-
37°C, pH 7.3, Kic
0.0037
6-amino-4-[2-(methoxyphenyl)ethyl]-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
-
37°C, pH 7.3, Kic
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
85600
expected for a Tgt dimer containing one structural Zn2+ per subunit
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
2-aminolin-benzoguanine inhibitors in complex with TGT, by hanging-drop, vapor diffusion method at 0°C and macro-seeding, to 1.28-1.78 A resolution, crystals belong to space group C2. The 2-amino-lin-benzoguanines are protonated upon binding to TGT. At pH 5.5, Asp102 is rotated to 75% into the guanine binding pocket whereas at pH 8.5 the same residue is oriented to 100% out of the pocket. Pronounced disorder of the attached side chains addressing the ribose 33 binding pocket
in complex with guanine, pre-queuine 0, and pre-queuine 1, hanging drop vapour diffusion method, in 100 mM MES, pH 5.5, 1 mM dithiothreitol, 13% (w/v) PEG 8000, 10% (v/v) dimethyl sulfoxide
in complex with linbenzoguanine (6-aminoimidazol[4,5-g]quinazolin-8(7H)-one), hanging drop vapour diffusion method, in with 100 mM MES buffer (pH 5.5), 1 mM dithiothreitol, 8% (w/v) PEG 8000, 10% DMSO, at 20°C
mutant K52M, by hanging-drop, vapor-diffusion method and followed by macroseeding, at a resolution of 2.0 A, forms crystals under the same conditions as wild-type, while all attempts to obtain diffracting crystals from mutant Y330F are unsuccessful. Compared to wild-type, crystals of mutant K52M are very fragile and show only a limited diffraction quality
TGT in complex with 6-amino-4-{2-[(cyclohexylmethyl)amino]ethyl}-2-(methylamino)-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one, residues Val45 and Leu68 form a hydrophobic surface that hosts the cyclohexane ring
wild-type at pH 5.5 to 1.9 A resolution and in complex with pre-queuine 0 to 1.7 A resolution (both crystals belong to space group C2), and in complex with its natural substrate pre-queuine 1 to 2.4 A resolution (crystal belongs to space group C2221). Mutant Y106F alone to 1.95 A resolution and in complex with pre-queuine 1 to 1.9 A resolution (both crystals belong to space group C2). By macroseeding and the hanging-drop method
enzyme-inhibitor complexes with 3,5-diaminophthalhydrazide, 4-aminophthalhydrazide, 5-aminonaphthalene-2,3-hydrazide, 5-amino-3-(1H-[1,2,4]triazole-3-yl-sulfanyl)-phthalhydrazide, 5-amino-3-(5-amino-1H-[1,2,4]triazol-3-yl-sulfanyl)-phthalhydrazide. 1.95 A crystal structure of 4-aminophthalhydrazide in complex with the enzyme
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E235Q
the mutation has no significant influence on kcat, but Km for preQ1 is drastically increased, while Km for preQ0 seems to be decreased
K52M
reduced turnover value. At a concentration of protein of 0.01 mM appears almost exclusively as a homodimer as the wild-type, when the concentration of protein is lowered to a minimal value of 0.001 mM, a substantial proportion of monomer becomes evident
Y330F
reduced turnover value. At a concentration of protein of 0.01 mM reveals a significant amount of monomer, when the concentration of protein is lowered to a minimal value of 0.001 mM, a substantial proportion of monomer becomes evident
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
mutants introduced into plasmid pET9d-ZM4 and transformed into Escherichia coli BL21(DE3) GOLD cells
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
the enzyme is a target for the design of potent drugs against Shigellosis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Romier, C.; Reuter, K.; Suck, D.; Ficner, R.
Crystal structure of tRNA-guanine transglycosylase: RNA modification by base exchange
EMBO J.
15
2850-2857
1996
Zymomonas mobilis
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)
Meyer, E.A.; Donati, N.; Guillot, M.; Schweizer, W.B.; Diederich, F.; Stengl, B.; Brenk, R.; Reuter, K.; Klebe, G.
Synthesis, biological evaluation, and crystallographic studies of extended guanine-based (lin-benzoguanine) inhibitors for tRNA-guanine transglycosylase (TGT)
Helv. Chim. Acta
89
573-597
2006
Zymomonas mobilis
-
Stengl, B.; Meyer, E.A.; Heine, A.; Brenk, R.; Diederich, F.; Klebe, G.
Crystal structures of tRNA-guanine transglycosylase (TGT) in complex with novel and potent inhibitors unravel pronounced induced-fit adaptations and suggest dimer formation upon substrate binding
J. Mol. Biol.
370
492-511
2007
Zymomonas mobilis, Zymomonas mobilis (P28720)
Tidten, N.; Stengl, B.; Heine, A.; Garcia, G.A.; Klebe, G.; Reuter, K.
Glutamate versus glutamine exchange swaps substrate selectivity in tRNA-guanine transglycosylase: insight into the regulation of substrate selectivity by kinetic and crystallographic studies
J. Mol. Biol.
374
764-776
2007
Zymomonas mobilis (P28720), Zymomonas mobilis
Ritschel, T.; Hoertner, S.; Heine, A.; Diederich, F.; Klebe, G.
Crystal structure analysis and in silico pKa calculations suggest strong pKa shifts of ligands as driving force for high-affinity binding to TGT
ChemBioChem
10
716-727
2009
Zymomonas mobilis (P28720)
Kohler, P.C.; Ritschel, T.; Schweizer, W.B.; Klebe, G.; Diederich, F.
High-affinity inhibitors of tRNA-guanine transglycosylase replacing the function of a structural water cluster
Chemistry
15
10809-10817
2009
Zymomonas mobilis (P28720)
Ritschel, T.; Kohler, P.C.; Neudert, G.; Heine, A.; Diederich, F.; Klebe, G.
How to replace the residual solvation shell of polar active site residues to achieve nanomolar inhibition of tRNA-guanine transglycosylase
ChemMedChem
4
2012-2023
2009
Zymomonas mobilis (P28720)
Ritschel, T.; Atmanene, C.; Reuter, K.; Van Dorsselaer, A.; Sanglier-Cianferani, S.; Klebe, G.
An integrative approach combining noncovalent mass spectrometry, enzyme kinetics and X-ray crystallography to decipher Tgt protein-protein and protein-RNA interaction
J. Mol. Biol.
393
833-847
2009
Zymomonas mobilis (P28720)
Barandun, L.J.; Immekus, F.; Kohler, P.C.; Tonazzi, S.; Wagner, B.; Wendelspiess, S.; Ritschel, T.; Heine, A.; Kansy, M.; Klebe, G.; Diederich, F.
From lin-benzoguanines to lin-benzohypoxanthines as ligands for Zymomonas mobilis tRNA-guanine transglycosylase: replacement of protein-ligand hydrogen bonding by importing water clusters
Chemistry
18
9246-9257
2012
Zymomonas mobilis (P28720), Zymomonas mobilis
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