Information on EC 2.4.2.29 - tRNA-guanosine34 transglycosylase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY
2.4.2.29
-
RECOMMENDED NAME
GeneOntology No.
tRNA-guanosine34 transglycosylase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
guanine34 in tRNA + 7-aminomethyl-7-carbaguanine = 7-aminomethyl-7-carbaguanine34 in tRNA + guanine
show the reaction diagram
(1); (2)
-
-
-
guanine34 in tRNA + queuine = queuine34 in tRNA + guanine
show the reaction diagram
ping-pong kinetic mechanism
-
guanine34 in tRNA + queuine = queuine34 in tRNA + guanine
show the reaction diagram
double-displacement mechanism that involves the formation of a covalent enzyme-RNA intermediate
-
guanine34 in tRNA + queuine = queuine34 in tRNA + guanine
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
pentosyl group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
queuosine biosynthesis
-
SYSTEMATIC NAME
IUBMB Comments
tRNA-guanosine34:queuine tRNA-D-ribosyltransferase
Certain prokaryotic and eukaryotic tRNAs contain the modified base queuine at position 34. In eukaryotes queuine is salvaged from food and incorporated into tRNA directly via a base-exchange reaction, replacing guanine. 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 [4,5]. The eubacterial enzyme can also use an earlier intermediate, preQ0, to replace guanine in unmodified tRNATyr and tRNAAsn [2]. This enzyme acts after EC 1.7.1.13, preQ1 synthase, in the queuine-biosynthesis pathway.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
guanine insertion enzyme
-
-
-
-
guanine, queuine-tRNA transglycosylase
-
-
-
-
Q-insertase
-
-
-
-
QTRT1
Q9BXR0
-
QTRTD1
Q9BXR0
-
QueTGT
P28720
-
queuine insertase
-
-
-
-
queuine tRNA ribosyltransferase
-
-
-
-
queuine tRNA-ribosyltransferase
-
-
-
-
queuine tRNA-ribosyltransferase 1
Q9BXR0
-
queuine tRNA-ribosyltransferase domain-containing 1
Q9BXR0
-
ribosyltransferase, queuine transfer ribonucleate
-
-
-
-
TGT
-
-
-
-
TGT
P0A847
-
TGT
Q9BXR0
-
TGT
Q54177
-
transfer ribonucleate glycosyltransferase
-
-
-
-
tRNA guanine transglycosidase
-
-
-
-
tRNA guanine transglycosylase
-
-
-
-
tRNA transglycosylase
-
-
-
-
tRNA-guanine transglycosylase
-
-
-
-
tRNA-guanine transglycosylase
-
-
tRNA-guanine transglycosylase
Q9BXR0
-
tRNA-guanine transglycosylase
-
-
tRNA-guanine transglycosylase
P28720
-
tRNA-guanine transglycosylases
Q9BXR0
-
tRNAguanine transglycosylase
P28720
-
virulence-associated protein VACC
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
72162-89-1
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
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
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
-
-
?
2-thiohypoxanthine + tRNAguanine
guanine + tRNA2-thiohypoxanthine
show the reaction diagram
-
-
-
-
?
6-thioguanine + tRNAguanine
guanine + tRNA6-thioguanine
show the reaction diagram
-
-
-
-
?
7-(cyano)-7-deazaguanine + tRNAguanine
guanine + tRNA(7-(cyano)-7-deazaguanine)
show the reaction diagram
-
-
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
7-aminomethyl-7-carbaguanine + [tRNA]-guanine
guanine + [tRNA]-pre Q1
show the reaction diagram
-
Tyr106 in the active site is hydrogen bonded in the ligand-free structure
-
-
?
7-deazaguanine + tRNAguanine
guanine + tRNA(7-deazaguanine)
show the reaction diagram
-
-
-
ir
8-azaguanine + tRNAguanine
guanine + tRNA(8-azaguanine)
show the reaction diagram
-
-
-
-
r
8-azaguanine + tRNAguanine
guanine + tRNA(8-azaguanine)
show the reaction diagram
-
-
-
-
r
dihydroqueuine + tRNAguanine
guanine + tRNAdihydroqueuine
show the reaction diagram
-
-
-
-
ir
dihydroqueuine + tRNAguanine
guanine + tRNAdihydroqueuine
show the reaction diagram
-
-
-
-
?
guanine + tRNAguanine
tRNAguanine + guanine
show the reaction diagram
-
-
-
-
r
guanine + tRNAguanine
tRNAguanine + guanine
show the reaction diagram
-
-
-
-
?
guanine + tRNAguanine
tRNAguanine + guanine
show the reaction diagram
-
-
-
-
r
guanine + tRNAguanine
tRNAguanine + guanine
show the reaction diagram
-
-
-
-
r
guanine + tRNAguanine
tRNAguanine + guanine
show the reaction diagram
-
yeast tRNAAsp
-
-
?
guanine + tRNAguanine
tRNAguanine + guanine
show the reaction diagram
-
yeast tRNA
-
-
?
guanine34 in tRNA + 7-aminomethyl-7-carbaguanine
7-aminomethyl-7-carbaguanine34 in tRNA + guanine
show the reaction diagram
-
-
-
-
?
guanine34 in tRNA + 7-aminomethyl-7-carbaguanine
7-aminomethyl-7-carbaguanine34 in tRNA + guanine
show the reaction diagram
-
-
-
-
?
guanine34 in tRNA + 7-aminomethyl-7-carbaguanine
7-aminomethyl-7-carbaguanine34 in tRNA + guanine
show the reaction diagram
-
-
-
-
?
guanine34 in tRNA + 7-aminomethyl-7-carbaguanine
7-aminomethyl-7-carbaguanine34 in tRNA + guanine
show the reaction diagram
-
-
-
-
?
guanine34 in tRNA + 7-aminomethyl-7-carbaguanine
7-aminomethyl-7-carbaguanine34 in tRNA + guanine
show the reaction diagram
-
-
-
-
?
guanine34 in tRNA + 7-aminomethyl-7-carbaguanine
7-aminomethyl-7-carbaguanine34 in tRNA + guanine
show the reaction diagram
P0A847
-
-
-
?
guanine34 in tRNA + 7-aminomethyl-7-carbaguanine
7-aminomethyl-7-carbaguanine34 in tRNA + guanine
show the reaction diagram
Q54177
-
-
-
?
guanine34 in tRNA + 7-aminomethyl-7-carbaguanine
7-aminomethyl-7-carbaguanine34 in tRNA + guanine
show the reaction diagram
-
no activity
-
-
-
guanine34 in tRNA + 7-aminomethyl-7-carbaguanine
7-aminomethyl-7-carbaguanine34 in tRNA + guanine
show the reaction diagram
-
poor substrate
-
-
ir
guanine34 in tRNA + 7-aminomethyl-7-carbaguanine
7-aminomethyl-7-carbaguanine34 in tRNA + guanine
show the reaction diagram
-
E. coli preQ0-tRNATyr, containing7-(cyano)-7-deazaguanine in the anticodon and E. coli guaninetRNATyr containing guanosine in the anticodon are good acceptors
-
ir
guanine34 in tRNA + 7-aminomethyl-7-carbaguanine
7-aminomethyl-7-carbaguanine34 in tRNA + guanine
show the reaction diagram
-
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
-
-
?
guanine34 in tRNA + 7-aminomethyl-7-carbaguanine
7-aminomethyl-7-carbaguanine34 in tRNA + guanine
show the reaction diagram
-
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
show the reaction diagram
-
the enzyme exchanges the genetically encoded guanine at position 34 with a queuine precursor 7-(aminomethyl)-7-deazaguanine
-
-
?
guanine34 in tRNA + 7-aminomethyl-7-carbaguanine
7-aminomethyl-7-carbaguanine34 in tRNA + guanine
show the reaction diagram
-
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
-
-
?
guanine34 in tRNA + 7-aminomethyl-7-carbaguanine
7-aminomethyl-7-carbaguanine34 in tRNA + guanine
show the reaction diagram
-
prefers pre-queuine 1 over pre-queuine 0
-
-
?
guanine34 in tRNA + queuine
queuine34 in tRNA + guanine
show the reaction diagram
-
-
-
-
?
guanine34 in tRNA + queuine
queuine34 in tRNA + guanine
show the reaction diagram
-
-
-
-
?
guanine34 in tRNA + queuine
queuine34 in tRNA + guanine
show the reaction diagram
-
-
-
-
ir
guanine34 in tRNA + queuine
queuine34 in tRNA + guanine
show the reaction diagram
P28720
-
-
-
?
guanine34 in tRNA + queuine
queuine34 in tRNA + guanine
show the reaction diagram
-
nucleosides in position 36, 37 and 38 influence the efficiency of conversion of G-34 to queuosine-34
-
-
?
guanine34 in tRNA + queuine
queuine34 in tRNA + guanine
show the reaction diagram
-
tRNATyr, tRNAHis, tRNAAsn, or tRNAASp from an E. coli mutant or rat ascites hepatoma cells
-
-
?
guanine34 in tRNA + queuine
queuine34 in tRNA + guanine
show the reaction diagram
P28720
catalyses a base-exchange reaction that leads to anticodon modifications of certain tRNAs
-
-
?
guanine34 in tRNA + queuine
queuine34 in tRNA + guanine
show the reaction diagram
-
the tRNA-modifying enzyme catalyzes the posttranscriptional exchange of guanine in position 34 of tRNA(Y, H, N, D) with the modified base queuine in eukaryotes or its precursor, preQ(1) base in eubacteria
-
-
?
pre-queuine 0 + tRNA guanine
guanine + tRNA pre-queuine 0
show the reaction diagram
-
-
-
-
?
pre-queuine 1 + virF minihelix RNA
?
show the reaction diagram
P0A847
-
-
-
?
pre-queuine 1 + virF mRNA
?
show the reaction diagram
P0A847
TGT may modulate the translation of VirF via modification of the virF mRNA
-
-
?
tRNAqueuine + guanine
tRNAguanine + queuine
show the reaction diagram
-
-
-
-
?
tRNAqueuine + hypoxanthine
tRNAhypoxanthine + queuine
show the reaction diagram
-
-
-
-
?
tRNAqueuine + xanthine
tRNAxanthine + queuine
show the reaction diagram
-
-
-
-
?
[tRNATyr]7-aminomethyl-7-carbaguanine + guanine
[tRNATyr]-guanine + 7-aminomethyl-7-carbaguanine
show the reaction diagram
-
-
-
-
?
[tRNATyr]7-aminomethyl-7-carbaguanine + guanine
[tRNATyr]-guanine + 7-aminomethyl-7-carbaguanine
show the reaction diagram
-
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
show the reaction diagram
-
Tgt dimer binds specifically to a single tRNA molecule
-
-
?
[tRNATyr]queuine + guanine
[tRNATyr]-guanine + queuine
show the reaction diagram
-, Q9BXR0
human TGT is composed of a catalytic subunit, QTRT1, and QTRTD1, not USP14. QTRTD1 is the salvage enzyme that generates free queuine from QMP
-
-
?
guanine34 in tRNA + queuine
guanine34 in tRNA + guanine
show the reaction diagram
-
-
-
-
r
additional information
?
-
-
-
-
-
-
additional information
?
-
-
post-translational modification of tRNA
-
-
-
additional information
?
-
-
post-translational modification of tRNA
-
-
-
additional information
?
-
-
key enzyme involved in the incorporation of the modified base queuine into tRNA
-
-
-
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
?
-
-
formation of queuosine
-
-
-
additional information
?
-
-
the enzyme is required for virulence
-
-
-
additional information
?
-
-
the 60000 Da subunit of the enzyme plays a role in colon carcinogenesis
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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 + 7-aminomethyl-7-carbaguanine
7-aminomethyl-7-carbaguanine34 in tRNA + guanine
show the reaction diagram
-
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
-
-
?
guanine34 in tRNA + 7-aminomethyl-7-carbaguanine
7-aminomethyl-7-carbaguanine34 in tRNA + guanine
show the reaction diagram
-
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
show the reaction diagram
-
the enzyme exchanges the genetically encoded guanine at position 34 with a queuine precursor 7-(aminomethyl)-7-deazaguanine
-
-
?
guanine34 in tRNA + 7-aminomethyl-7-carbaguanine
7-aminomethyl-7-carbaguanine34 in tRNA + guanine
show the reaction diagram
-
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
-
-
?
guanine34 in tRNA + queuine
queuine34 in tRNA + guanine
show the reaction diagram
P28720
catalyses a base-exchange reaction that leads to anticodon modifications of certain tRNAs
-
-
?
guanine34 in tRNA + queuine
queuine34 in tRNA + guanine
show the reaction diagram
-
the tRNA-modifying enzyme catalyzes the posttranscriptional exchange of guanine in position 34 of tRNA(Y, H, N, D) with the modified base queuine in eukaryotes or its precursor, preQ(1) base in eubacteria
-
-
?
additional information
?
-
-
-
-
-
-
additional information
?
-
-
post-translational modification of tRNA
-
-
-
additional information
?
-
-
post-translational modification of tRNA
-
-
-
additional information
?
-
-
key enzyme involved in the incorporation of the modified base queuine into tRNA
-
-
-
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
?
-
-
formation of queuosine
-
-
-
additional information
?
-
-
the enzyme is required for virulence
-
-
-
additional information
?
-
-
the 60000 Da subunit of the enzyme plays a role in colon carcinogenesis
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ba2+
-
1 mM, less effective than Mg2+ in meeting the divalent ion requirement
Ca2+
-
1 mM, less effective than Mg2+ in meeting the divalent ion requirement
Cs+
-
less effective than Na+ in meeting the monovalent ion requirement
K+
-
less effective than Na+ in meeting the monovalent ion requirement
Li+
-
less effective than Na+ in meeting the monovalent ion requirement
Mg2+
-
the enzyme requires a monovalent or a divalent cation. Mg2+ is most effective in meeting the divalent cation requirement. Optimal Mg2+ concentration is 5.0 mM
Na+
-
the enzyme requires a monovalent or a divalent cation. Na+ is most effective in meeting the monovalent requirement. Optimal concentration is 114 mM
Rb+
-
less effective than Na+ in meeting the monovalent ion requirement
Sr2+
-
1 mM, less effective than Mg2+ in meeting the divalent ion requirement
Zn2+
-
one structural Zn2+ per subunit
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2,3-Dihydroxybenzoic acid
-
-
2,4-Diamino-6-hydroxypyrimidine
-
1.2 mM, 52% inhibition
2,6-bis(methylamino)-1,4a,7,8a-tetrahydro-8H-imidazo[4,5-g]quinazolin-8-one
-
-
-
2,6-diamino-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
Q54177
-
2,6-diamino-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
-
-
2,6-diamino-8-(2-phenylethyl)quinazolin-4(3H)-one
-
-
2,6-diamino-8-[[(1H-imidazol-2-yl)sulfanyl]methyl]quinazolin-4(3H)-one
P28720
-
2,6-diaminoquinazolin-4(3H)-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-amino-5-(fluoromethyl)pyrrolo[2,3-d]pyrimidin-4(3H)-one
-
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-amino-7-(dimethylamino)quinazolin-4(3H)-one
-
-
2-amino-7-[benzyl(methyl)amino]quinazolin-4(3H)-one
-
-
2-amino-8-methylquinazolin-4(3H)-one
-
-
2-aminopteridin-4(3H)-one
-
-
2-aminoquinazolin-4(3H)-one
-
-
2-butyl-5,6-dihydro-1H-imidazo[4,5-d]pyridazine-4,7-dione
P28720
-
2-methylamino-lin-benzoguanine
-
-
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
-
-
-
3,5-diaminophthalhydrazide
-
-
3,5-diaminophthalimide
-
-
3-Deazaguanine
-
0.25 mM, 50% inhibition
4-(2-phenylethyl)-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
-
-
4-(2-[(cyclohexylmethyl)amino]ethyl)2-(methylamino)-1,7-dihydro-8Himidazo[4,5-g]quinazolin-8-one
-
-
-
4-(2-[(cyclopentylmethyl)amino]ethyl)-2-(methylamino)-1,7-dihydro-8Himidazo[4,5-g]quinazolin-8-one
-
-
-
4-aminophthalhydrazide
-
-
4-aminophthalimide
-
-
5,7-diamino-2,3-dihydro-phthalazine-1,4-dione
P28720
-
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
-
-
6-(ethylamino)-2-(methylamino)-1,4a,7,8a-tetrahydro-8H-imidazo[4,5-g]quinazolin-8-one
-
-
-
6-amino-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
-
-
6-amino-2-(benzylamino)-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
Q54177
-
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
Q54177
-
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-methyl-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
Q54177
-
6-amino-2-methyl-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
-
-
6-amino-2-[(1,3-benzodioxol-5-ylmethyl)amino]-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
Q54177
-
6-amino-2-[(2-morpholin-4-ylethyl)amino]-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
Q54177
-
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
Q54177
-
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-[(4-morpholin-4-ylbenzyl)amino]-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
Q54177
-
6-amino-2-[(naphthalen-1-ylmethyl)amino]-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
Q54177
-
6-amino-2-[(naphthalen-1-ylmethyl)amino]-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
-
-
6-amino-2-[(quinolin-4-ylmethyl)amino]-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
Q54177
-
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
Q54177
-
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-benzyl-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-phenyl-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-(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-amino-4-[2-(methoxyphenyl)ethyl]-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
6-aminoimidazol[4,5-g]quinazolin-8(7H)-one
-
-
6-aminoimidazol[4,5-g]quinazolin-8(7H)-one
Q54177
mixed competitive-uncompetitive inhibition with respect to tRNA binding
6-Methylmercaptoguanine
-
0.05 mM, 65% inhibition
6-Thioguanine
-
0.05 mM, 74% inhibition
7-Deazaguanine
-
0.06 mM, 27% inhibition
7-methylguanine
-
0.05 mM, 94% inhibition
7-methylguanine
-
-
8-Azaguanine
-
0.05 mM, complete inhibition
8-Bromoguanine
-
0.05 mM, 86% inhibition
8-dimethylaminomethyl-7-deazaguanine
-
0.05 mM, 32% inhibition
adenine
-
0.05 mM, 14% inhibition
benzimidazole-5-carboxylate
-
-
biopterin
-
0.02 mM, 39% inhibition
dimethylsuberimidate
-
inactivates by cross-linking, tRNA protects
ethylacetimidate
-
-
folic acid
-
1.2 mM, complete inhibition
isocytosine
-
1.2 mM, 52% inhibition
lumazine
-
1.2 mM, 18% inhibition
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
-
-
neplanocin A
-
0.1 mM, 45% inhibition; poor
pterin
-
0.0048 mM, 82% inhibition
pterin-6-carboxylic acid
-
1.2 mM, 57% inhibition
queuine
-
0.01 mM, 93% inhibition
sepiapterin
-
0.13 mM, 33% inhibition
tetrahydrobiopterin
-
0.02 mM, 82% inhibition
xanthine
-
for the mutant enzyms D143S and D143T, xanthine is competitive, with respect to guanine
additional information
-
design, synthesis, and in vitro evaluation of novel tricyclic TGT inhibitors based on the lin-benzoguanine scaffold
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
QTRT1 subunit is responsible for the transglycosylase activity. Transglycosylase activity of QTRT1 is only observed when QTRT1 and QTRTD1 are coexpressed and copurified
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.152
-
2-amino-5-(fluoromethyl)pyrrolo[2,3-d]pyrimidin-4(3H)-one
-
-
0.000014
-
7-(aminomethyl)-7-deazaguanine
-
-
0.0021
-
7-(aminomethyl)-7-deazaguanine
-
-
0.000053
-
Guanine
-
-
0.00006
-
Guanine
-
-
0.0001
-
Guanine
-
histidine-tagged wild-type enzyme, pH 7.3
0.0001
-
Guanine
-
wild-type enzyme
0.00015
-
Guanine
-
-
0.0003
-
Guanine
-
mutant enzyme D264E
0.00035
-
Guanine
-
pH 7.3, 37C, wild-type
0.00038
-
Guanine
P28720
wild-type enzyme
0.00038
-
Guanine
-
wild-type
0.00057
-
Guanine
-
histidine-tagged wild-type enzyme, pH 8.5
0.00083
-
Guanine
-
-
0.00087
-
Guanine
-
pH 7.3, 37C, mutant C145V/T146V
0.001
-
Guanine
-
pH 7.3, 37C, mutant V217G
0.0011
-
Guanine
-
mutant enzyme S90A
0.0012
-
Guanine
-
wild type enzyme, in 200 mM HEPES, pH 7.3, 20 mM MgCl2
0.0013
-
Guanine
P28720
mutant enzyme Y106F
0.0013
-
Guanine
-
mutant Y106F
0.00209
-
Guanine
-
pH 7.3, 37C, mutant C145V/T146V/V217G
0.00261
-
Guanine
-
histidine-tagged mutant enzyme D89E, pH 7.3
0.00261
-
Guanine
-
-
0.003
-
Guanine
-
wild-type enzyme
0.0033
-
Guanine
-
mutant enzyme E235Q, in 200 mM HEPES, pH 7.3, 20 mM MgCl2
0.00632
-
Guanine
-
histidine-tagged mutant enzyme D89E, pH 8.5
0.0114
-
Guanine
-
37C, pH 7.3, mutant enzyme D143A
0.0218
-
Guanine
-
37C, pH 7.3, mutant enzyme D143N
0.035
-
Guanine
-
pH 7.3, 37C, mutant C145V/T146V/P147N/V217G
0.057
-
Guanine
-
37C, pH 7.3, mutant enzyme D143S
0.105
-
Guanine
-
37C, pH 7.3, mutant enzyme D143T
0.49
-
hypoxanthine
-
37C, pH 7.3, mutant enzyme D143N
0.8
11
hypoxanthine
-
37C, pH 7.3, wild-type enzyme
1.55
-
hypoxanthine
-
37C, pH 7.3, mutant enzyme D143A
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
0.00026
-
queuine
-
pH 7.3, 37C, wild-type
0.00011
-
tRNA
-
histidine-tagged mutant enzyme D89E, pH 7.3
0.00012
-
tRNA
-
histidine-tagged wild-type enzyme, pH 7.3
0.00012
-
tRNA
-
wild-type enzyme
0.00036
-
tRNA
P28720
mutant enzyme Y106F
0.00039
-
tRNA
-
histidine-tagged wild-type enzyme, pH 8.5
0.00046
-
tRNA
-
mutant enzyme D264E
0.00051
-
tRNA
-
histidine-tagged mutant enzyme D89E, pH 8.5
0.001
-
tRNA
P28720
wild-type enzyme
0.00016
-
tRNA guanine
P0A847
at pH 7.3
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
0.00032
-
tRNA(Tyr)
-
wild-type enzyme
0.0097
-
tRNA(Tyr)
-
mutant enzyme S90C
0.0000033
-
tRNAAsp
-
yeast tRNAAsp
0.00087
-
virF minihelix RNA
P0A847
at pH 7.3
-
0.0018
-
virF mRNA
P0A847
at pH 7.3
-
0.0026
-
xanthine
-
37C, pH 7.3, mutant enzyme D143N
0.013
-
xanthine
-
37C, pH 7.3, mutant enzyme D143A
0.224
-
xanthine
-
37C, pH 7.3, wild-type enzyme
0.00262
-
[RNAECYMA]-2'-deoxyguanine 34
-
-
-
0.00287
-
[RNAECYMA]-guanine
-
-
-
0.00098
-
[tRNATyr]7-aminomethyl-7-carbaguanine
-
mutant K52M
-
0.00158
-
[tRNATyr]7-aminomethyl-7-carbaguanine
-
mutant Y330F
-
0.00217
-
[tRNATyr]7-aminomethyl-7-carbaguanine
-
wild-type
-
0.00036
-
[tRNA]-guanine
-
mutant Y106F
0.001
-
[tRNA]-guanine
-
wild-type
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.461
-
2-amino-5-(fluoromethyl)pyrrolo[2,3-d]pyrimidin-4(3H)-one
-
-
0.000259
-
Guanine
-
pH 7.3, 37C, mutant V217G
0.00053
-
Guanine
-
pH 7.3, 37C, mutant C145V/T146V
0.00062
-
Guanine
-
pH 7.3, 37C, mutant C145V/T146V/P147N/V217G
0.0012
-
Guanine
-
pH 7.3, 37C, mutant C145V/T146V/V217G
0.004
-
Guanine
P28720
mutant enzyme Y106F
0.004
-
Guanine
-
mutant Y106F
0.00629
-
Guanine
-
pH 7.3, 37C, wild-type
0.011
-
Guanine
P28720
wild-type enzyme
0.011
-
Guanine
-
wild-type
0.056
-
Guanine
-
wild type enzyme
0.076
-
Guanine
-
mutant enzyme E235Q
0.59
-
Guanine
-
histidine-tagged mutant enzyme D89E, pH 7.3
0.75
-
Guanine
-
histidine-tagged mutant enzyme D89E, pH 8.5
1.21
-
Guanine
-
histidine-tagged wild-type enzyme, pH 7.3
7.57
-
Guanine
-
histidine-tagged wild-type enzyme, pH 8.5
0.00012
-
hypoxanthine
-
37C, pH 7.3, mutant enzyme D143N
0.00019
-
hypoxanthine
-
37C, pH 7.3, mutant enzyme D143A
0.00297
-
hypoxanthine
-
37C, pH 7.3, wild-type enzyme
0.0006
-
pre-queuine 0
-
mutant enzyme E235Q, Km less than 0.0005 mM
0.012
-
pre-queuine 0
-
wild type enzyme
0.1
-
pre-queuine 1
-
mutant enzyme E235Q
0.102
-
pre-queuine 1
-
wild type enzyme
0.008
-
queuine
-
pH 7.3, 37C, wild-type
0.005
-
tRNA
P28720
mutant enzyme Y106F
0.014
-
tRNA
P28720
wild-type enzyme
0.71
-
tRNA
-
histidine-tagged mutant enzyme D89E, pH 7.3
0.93
-
tRNA
-
histidine-tagged mutant enzyme D89E, pH 8.5
1.21
-
tRNA
-
histidine-tagged wild-type enzyme, pH 7.3
5.85
-
tRNA
-
histidine-tagged wild-type enzyme, pH 8.5
0.004
-
tRNA guanine
P0A847
at pH 7.3
0.054
-
tRNA guanine
-
wild type enzyme
0.07
-
tRNA guanine
-
mutant enzyme E235Q
0.00033
-
virF minihelix RNA
P0A847
at pH 7.3
-
0.00011
-
virF mRNA
P0A847
at pH 7.3
-
0.0000055
-
xanthine
-
37C, pH 7.3, mutant enzyme D143A
0.0000088
-
xanthine
-
37C, pH 7.3, mutant enzyme D143N
0.000069
-
xanthine
-
37C, pH 7.3, wild-type enzyme
0.011
-
[RNAECYMA]-2'-deoxyguanine 34
-
-
-
0.0094
-
[RNAECYMA]-guanine
-
-
-
0.00023
-
[tRNATyr]7-aminomethyl-7-carbaguanine
-
mutant K52M
-
0.00095
-
[tRNATyr]7-aminomethyl-7-carbaguanine
-
mutant Y330F
-
0.011
-
[tRNATyr]7-aminomethyl-7-carbaguanine
-
wild-type
-
0.005
-
[tRNA]-guanine
-
mutant Y106F
0.014
-
[tRNA]-guanine
-
wild-type
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.017
-
Guanine
-
pH 7.3, 37C, mutant C145V/T146V/P147N/V217G
11206
0.26
-
Guanine
-
pH 7.3, 37C, mutant V217G
11206
0.58
-
Guanine
-
pH 7.3, 37C, mutant C145V/T146V/V217G
11206
0.61
-
Guanine
-
pH 7.3, 37C, mutant C145V/T146V
11206
3.4
-
Guanine
-
mutant Y106F
11206
18
-
Guanine
-
pH 7.3, 37C, wild-type
11206
28.9
-
Guanine
-
wild-type
11206
31.6
-
queuine
-
pH 7.3, 37C, wild-type
16088
13.3
-
[tRNA]-guanine
-
mutant Y106F
293196
13.9
-
[tRNA]-guanine
-
wild-type
293196
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
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
3
-
2,3-Dihydroxybenzoic acid
-
-
0.02805
-
2,6-bis(methylamino)-1,4a,7,8a-tetrahydro-8H-imidazo[4,5-g]quinazolin-8-one
-
pH 7.3, 37C
-
0.000077
-
2,6-diamino-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
Q54177
-
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
0.0006
-
2,6-diaminoquinazolin-4(3H)-one
-
37C, pH 7.3
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, 37C
-
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, 37C
-
0.114
-
2-amino-5-(fluoromethyl)pyrrolo[2,3-d]pyrimidin-4(3H)-one
-
,competitive inhibition
0.136
-
2-amino-5-(fluoromethyl)pyrrolo[2,3-d]pyrimidin-4(3H)-one
-
inactivation
0.0031
-
2-amino-7-(dimethylamino)quinazolin-4(3H)-one
-
-
0.0041
-
2-amino-7-[benzyl(methyl)amino]quinazolin-4(3H)-one
-
-
0.001
-
2-amino-8-methylquinazolin-4(3H)-one
-
competitive inhibition, in 200 mM HEPES buffer (pH 7.3), 20 mM MgCl2
0.0191
-
2-amino-8-methylquinazolin-4(3H)-one
-
37C, pH 7.3
0.0022
-
2-aminopteridin-4(3H)-one
-
37C, pH 7.3
0.0017
-
2-aminoquinazolin-4(3H)-one
-
37C, pH 7.3
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 37C, 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, 37C
-
0.0029
-
2-[(thiophen-2-ylmethyl)amino]-1,4a,7,8a-tetrahydro-8H-imidazo[4,5-g]quinazolin-8-one
-
pH 7.3, 37C
-
0.0002
-
3,5-diaminophthalhydrazide
-
-
0.0021
-
3,5-diaminophthalimide
-
-
0.25
-
3-Deazaguanine
-
-
0.0028
-
4-(2-phenylethyl)-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
-
37C, pH 7.3
0.0011
-
4-(2-[(cyclohexylmethyl)amino]ethyl)2-(methylamino)-1,7-dihydro-8Himidazo[4,5-g]quinazolin-8-one
-
pH 7.3, 37C
-
0.00074
-
4-(2-[(cyclopentylmethyl)amino]ethyl)-2-(methylamino)-1,7-dihydro-8Himidazo[4,5-g]quinazolin-8-one
-
pH 7.3, 37C
-
0.0083
-
4-aminophthalhydrazide
-
-
0.00048
-
4-aminophthalimide
-
-
0.038
-
5-amino-3-(1H-[1,2,4]triazole-3-yl-sulfanyl)-phthalhydrazide
-
-
0.04083
-
6-(ethylamino)-2-(methylamino)-1,4a,7,8a-tetrahydro-8H-imidazo[4,5-g]quinazolin-8-one
-
pH 7.3, 37C
-
0.00076
-
6-amino-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
-
-
0.00007
-
6-amino-2-(benzylamino)-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
Q54177
-
0.000058
-
6-amino-2-(methylamino)-1,4a,7,8a-tetrahydro-8H-imidazo[4,5-g]quinazolin-8-one
-
pH 7.3, 37C
-
0.000058
-
6-amino-2-(methylamino)-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
Q54177
-
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 37C, 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 37C, 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 37C, 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, 37C
-
0.0015
-
6-amino-2-methyl-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
-
-
0.0016
-
6-amino-2-methyl-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
Q54177
-
0.000035
-
6-amino-2-[(1,3-benzodioxol-5-ylmethyl)amino]-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
Q54177
-
0.000006
-
6-amino-2-[(2-morpholin-4-ylethyl)amino]-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
Q54177
-
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, 37C
-
0.00001
-
6-amino-2-[(2-phenylethyl)amino]-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
Q54177
-
0.00001
-
6-amino-2-[(2-phenylethyl)amino]-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
-
-
0.00004
-
6-amino-2-[(4-morpholin-4-ylbenzyl)amino]-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
Q54177
-
0.000055
-
6-amino-2-[(naphthalen-1-ylmethyl)amino]-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
Q54177
-
0.000055
-
6-amino-2-[(naphthalen-1-ylmethyl)amino]-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
-
-
0.000027
-
6-amino-2-[(quinolin-4-ylmethyl)amino]-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
Q54177
-
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, 37C
-
0.000035
-
6-amino-2-[(thiophen-2-ylmethyl)amino]-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
Q54177
-
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
-
37C, pH 7.3, Kic
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
-
37C, pH 7.3, Kic
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 37C, 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 37C, pH 7.3, in 200 mM HEPES buffer, 20 mM MgCl2, 2.95 mM Tween 20 containing both substrates
0.001
-
6-amino-4-(2-phenylethyl)-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
-
37C, pH 7.3, Kic
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 37C, 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 37C, 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 37C, 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
-
37C, pH 7.3, Kic
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
-
37C, pH 7.3, Kic
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 37C, pH 7.3, in 200 mM HEPES buffer, 20 mM MgCl2, 2.95 mM Tween 20 containing both substrates
0.0037
-
6-amino-4-[2-(methoxyphenyl)ethyl]-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
-
37C, pH 7.3, Kic
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, 37C
-
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, 37C
-
0.0041
-
6-aminoimidazol[4,5-g]quinazolin-8(7H)-one
-
37C, pH 7.3, Kic
0.0041
-
6-aminoimidazol[4,5-g]quinazolin-8(7H)-one
Q54177
-
0.0079
-
6-aminoimidazol[4,5-g]quinazolin-8(7H)-one
-
37C, pH7.3, Kiu
0.054
-
7-Deazaguanine
-
-
0.001
-
7-methylguanine
-
-
0.000023
-
8-Azaguanine
-
-
0.0087
-
biopterin
-
pH 7.3, 37C, wild-type
0.16
-
biopterin
-
pH 7.3, 37C, mutant C145V/T146V/V217G
0.55
-
biopterin
-
pH 7.3, 37C, mutant C145V/T146V; pH 7.3, 37C, mutant V217G
1.05
-
biopterin
-
pH 7.3, 37C, mutant C145V/T146V/P147N/V217G
3
-
biopterin
-
pH 7.3, 37C, wild-type
0.011
-
folic acid
-
-
0.0014
-
N-(2-[6-amino-2-(methylamino)-8-oxo-7,8-dihydro-1H-imidazo[4,5-g]quinazolin-4-yl]ethyl)cyclohexanecarboxamide
-
at 37C, pH 7.3, in 200 mM HEPES buffer, 20 mM MgCl2, 2.95 mM Tween 20 containing both substrates
0.1
-
neplanocin A
-
-
0.00009
-
pterin
-
-
0.00042
-
pterin
-
pH 7.3, 37C, wild-type
0.0009
-
pterin
-
pH 7.3, 37C, mutant V217G
0.0013
-
pterin
-
pH 7.3, 37C, mutant C145V/T146V/V217G
0.0022
-
pterin
-
pH 7.3, 37C, mutant C145V/T146V
0.037
-
pterin
-
pH 7.3, 37C, mutant C145V/T146V/P147N/V217G
0.000095
-
queuine
-
-
0.09
-
xanthine
-
37C, pH 7.3, mutant enzyme D143T
0.12
-
xanthine
-
37C, pH 7.3, mutant enzyme D143S
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
the expression level of the 60000 Da subunit is elevated in four of five colon cancer cell lines and 83% of colon cancer tissue compared with normal tissue
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
85600
-
-
expected for a Tgt dimer containing one structural Zn2+ per subunit
85610
-
-
Tgt, noncovalent mass spectrometry
104000
-
-
gel filtration
113100
-
-
Tgt:tRNA complex, noncovalent mass spectrometry
140000
-
-
gel filtration
additional information
-
-
sequence identities between prokaryotic, eukaryotic and archaebacterial enzymes
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 44000, histidine-tagged wild-type enzyme
dimer
-
1 * 60000 + 1 * 43000, denaturing PAGE in presence of urea
dimer
-
2 * 68000, SDS-PAGE
dimer
-
x-ray crystallography
heterodimer
-
-
homodimer
-
noncovalent mass spectrometry, Tgt in solution
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
one subunit has a MW of 60000-61000 Da as determined by SDS-PAGE and 55921 Da calculated from nucleotide sequence, this suggests that the protein is posstranslationally modified
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
2-aminolin-benzoguanine inhibitors in complex with TGT, by hanging-drop, vapor diffusion method at 0C 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
-
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; 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 20C
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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
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mutant enzyme D280E
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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
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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
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wild-type and mutant enzyme Y106F, hanging drop method, crystals with a size of approximately 0.7 * 0.7 * 0.2 mm grew within five to seven days
P28720
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
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GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
linear KCl gradient to elute the enzyme from phosphocellulose results in complete loss of activity
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STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-80C, 10% glycerol, 25% loss of activity per month
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Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
LITERATURE
mutant enzymes S90F and S90C
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overexpression of D89E, D89D, D89C and D89A in Escherichia coli
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hQTRT1 and ubiquitin-specific protease 14 (USP14) coexpressed in Escherichia coli
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cDNA sequence of the 60000 Da subunit, 55921 Da calculated from nucleotide sequence
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expressed in Escherichia coli
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mutant expressed in Escherichia coli BL21(DE3) pLysS cells
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mutants introduced into plasmid pET9d-ZM4 and transformed into Escherichia coli BL21(DE3) GOLD cells
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ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C145V/T146V
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mutant shows lower kcat and higher Km value compared to wild-type
C145V/T146V/P147N/V217G
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quadruble mutant is affected least by pteridine inhibitors, mutant shows lowest kcat and highest Km value compared to wild-type and other mutants
C145V/T146V/V217G
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triple mutant shows lowest Ki value for biopterin, mutant shows lower kcat and higher Km value compared to wild-type
D143A
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mutant enzymes in order of ascending Km-values: D143A, D143N, D143S, D143T. Mutant enzmyes in order of descending binding affinity: wild-type, D143A, d143N, D143S, D143T
D143N
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mutant enzymes in order of ascending Km-values: D143A, D143N, D143S, D143T. Mutant enzmyes in order of descending binding affinity: wild-type, D143A, d143N, D143S, D143T
D143S
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mutant enzymes in order of ascending Km-values: D143A, D143N, D143S, D143T. Mutant enzmyes in order of descending binding affinity: wild-type, D143A, d143N, D143S, D143T
D143T
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mutant enzymes in order of ascending Km-values: D143A, D143N, D143S, D143T. Mutant enzmyes in order of descending binding affinity: wild-type, D143A, d143N, D143S, D143T
D264A
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mutant shows no catalytic activity
D264E
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mutant enzyme is capable of forming an enzyme-RNA covalent intermediate, however , unlike wild-type enzyme, only hydroxylamine is capable of cleaving the enzyme-RNA covalent complex
D264H
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mutant shows no catalytic activity
D264K
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mutant shows no catalytic activity
D264N
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mutant shows no catalytic activity
D264N
-
is inactive and incapable of forming the covalent intermediate, while maintaining the ability to bind noncovalently to RNA
D264Q
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mutant shows no catalytic activity
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
V217G
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mutant shows lower kcat and higher Km value compared to wild-type
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
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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
Y106F
P28720
2.8fold decrease in turnover-number for guanine and tRNA, 2.8fold decrease in Km-value for tRNA, 3.4fold increase in turnover-number for guanine, in contrast to Phe106 the residue Tyr106 is hydrogen bonded in the ligand-free structure, this is not the reason for the kinetic difference, other structurally less evident factors are responsible for this behaviour
Y106F
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crystallises similarly to the wild-type
Y330F
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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
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
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the enzyme is required for pathogenicity in Shigella flexneri and therefor is a potentially novel antibacterial target
medicine
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the enzyme is a target for the design of potent drugs against Shigellosis