Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + Asp-tRNAAsn + L-glutamine
ADP + phosphate + Asn-tRNAAsn + L-glutamate
ATP + Glu-tRNAGln + Asn
ADP + phosphate + Gln-tRNAGln + Asp
ATP + Glu-tRNAGln + L-asparagine
ADP + phosphate + Gln-tRNAGln + L-glutamate
-
-
-
-
?
ATP + Glu-tRNAGln + L-glutamine
ADP + phosphate + Gln-tRNAGln + L-glutamate
ATP + Glu-tRNAGln + L-glutamine + H2O
ADP + phosphate + Gln-tRNAGln + L-glutamate
ATP + Glu-tRNAGln + NH4Cl
ADP + phosphate + Gln-tRNAGln + ?
ATP + L-aspartyl-tRNAAsn + L-glutamine + H2O
ADP + phosphate + L-asparaginyl-tRNAAsn + L-glutamate
-
-
-
-
?
ATP + L-glutamate + tRNAGln1(UUG)
AMP + diphosphate + L-glutamyl-tRNAGln1(UUG)
-
the enzyme is active toward the two tRNAGln isoacceptors, but with a significant catalytic preference for tRNAGln2(CUG). The less active tRNAGln1(UUG) responds to the less common CAA codon for Gln
-
-
?
ATP + L-glutamate + tRNAGln2(CUG)
AMP + diphosphate + L-glutamyl-tRNAGln2(CUG)
-
the enzyme is active toward the two tRNAGln isoacceptors, but with a significant catalytic preference for tRNAGln2(CUG). The less active tRNAGln1(UUG) responds to the less common CAA codon for Gln. The wild-type enzyme shows a 24fold catalytic preference for tRNAGln2 over tRNAGlu
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
-
?
ATP + L-glutamyl-tRNAGln + L-glutamine
ADP + phosphate + L-glutaminyl-tRNAGln + L-glutamate
ATP-gammaS + Glu-tRNAGln + L-glutamine
? + phosphate + Gln-tRNAGln + L-glutamate
-
-
-
?
additional information
?
-
ATP + Asp-tRNAAsn + L-glutamine

ADP + phosphate + Asn-tRNAAsn + L-glutamate
-
-
-
?
ATP + Asp-tRNAAsn + L-glutamine
ADP + phosphate + Asn-tRNAAsn + L-glutamate
-
-
-
-
?
ATP + Asp-tRNAAsn + L-glutamine
ADP + phosphate + Asn-tRNAAsn + L-glutamate
-
the enzyme transamidates Asp-tRNAAsn and Glu-tRNAGln with similar efficiency
-
-
?
ATP + Asp-tRNAAsn + L-glutamine
ADP + phosphate + Asn-tRNAAsn + L-glutamate
-
identity elements used by GatCAB to discriminate tRNAAsn from tRNAAsp. GatCAB specifically binds Asp-tRNAAsn. Therefore, modified nucleotides do not play an essential role in GatCAB discrimination of Asp-tRNAAsn from Asp-tRNAAsp
-
-
?
ATP + Glu-tRNAGln + Asn

ADP + phosphate + Gln-tRNAGln + Asp
-
Asn is much less effective as amide donor than glutamine
-
-
?
ATP + Glu-tRNAGln + Asn
ADP + phosphate + Gln-tRNAGln + Asp
-
-
-
-
?
ATP + Glu-tRNAGln + L-glutamine

ADP + phosphate + Gln-tRNAGln + L-glutamate
-
-
-
-
?
ATP + Glu-tRNAGln + L-glutamine
ADP + phosphate + Gln-tRNAGln + L-glutamate
-
-
-
?
ATP + Glu-tRNAGln + L-glutamine
ADP + phosphate + Gln-tRNAGln + L-glutamate
-
-
-
-
?
ATP + Glu-tRNAGln + L-glutamine
ADP + phosphate + Gln-tRNAGln + L-glutamate
-
the amidation of Glu-tRNAGln proceeds via a gamma-phosphorylated intermediate
-
-
?
ATP + Glu-tRNAGln + L-glutamine
ADP + phosphate + Gln-tRNAGln + L-glutamate
-
disruption of this operon is lethal. Transamidation is the only pathway to Gln-tRNAGln in Bacillus subtilis. The enzyme furnishes a means for formation of correctly charged Gln-tRNAGln through the transamidation of misacylated Glu-tRNAGln, functionally replacing the lack of glutaminyl-tRNA synthetase activity in Gram-positive eubacteria, cyanobacteria, archaea and organelles
-
-
?
ATP + Glu-tRNAGln + L-glutamine
ADP + phosphate + Gln-tRNAGln + L-glutamate
-
-
-
?
ATP + Glu-tRNAGln + L-glutamine
ADP + phosphate + Gln-tRNAGln + L-glutamate
-
-
-
?
ATP + Glu-tRNAGln + L-glutamine
ADP + phosphate + Gln-tRNAGln + L-glutamate
-
-
-
-
?
ATP + Glu-tRNAGln + L-glutamine
ADP + phosphate + Gln-tRNAGln + L-glutamate
-
the enzyme transamidates Asp-tRNAAsn and Glu-tRNAGln with similar efficiency. GatCAB uses the amide donor glutamine 129fold more efficiently than asparagine
-
-
?
ATP + Glu-tRNAGln + L-glutamine
ADP + phosphate + Gln-tRNAGln + L-glutamate
-
-
-
?
ATP + Glu-tRNAGln + L-glutamine
ADP + phosphate + Gln-tRNAGln + L-glutamate
-
-
-
-
?
ATP + Glu-tRNAGln + L-glutamine
ADP + phosphate + Gln-tRNAGln + L-glutamate
-
GatDE is a heterodimeric amidotransferase. GatD acts as a glutaminase but only in the presence of both Glu-tRNAGln and the other subunit, GatE. The fact that only Glu-tRNAGln but not tRNA Gln could activate the glutaminase activity of GatD suggests that glutamine hydrolysis is coupled tightly to transamidation. GatE is a Glu-tRNAGln kinase that activates Glu-tRNAGln via gamma-phosphorylation
-
-
?
ATP + Glu-tRNAGln + L-glutamine
ADP + phosphate + Gln-tRNAGln + L-glutamate
-
Ser176A is the active-site nucleophile for facilitating Gln hydrolysis by the enzyme
-
?
ATP + Glu-tRNAGln + L-glutamine
ADP + phosphate + Gln-tRNAGln + L-glutamate
-
organisms lacking Gln-tRNA synthetase produce Gln-tRNAGln from misacylated Glu-tRNAGln through the transamidation activity of Glu-tRNAGln amidotransferase. The enzyme hydrolyzes Gln to Glu and NH3, using the latter product to transamidate Glu-tRNAGln in concert with ATP hydrolysis
-
?
ATP + Glu-tRNAGln + L-glutamine
ADP + phosphate + Gln-tRNAGln + L-glutamate
-
the enzyme produces Gln-tRNAGln required for plastidal protein biosynthesis
-
-
?
ATP + Glu-tRNAGln + L-glutamine + H2O

ADP + phosphate + Gln-tRNAGln + L-glutamate
-
-
-
-
?
ATP + Glu-tRNAGln + L-glutamine + H2O
ADP + phosphate + Gln-tRNAGln + L-glutamate
-
-
-
-
?
ATP + Glu-tRNAGln + NH4Cl

ADP + phosphate + Gln-tRNAGln + ?
-
NH4Cl is much less effective as amide donor than glutamine
-
-
?
ATP + Glu-tRNAGln + NH4Cl
ADP + phosphate + Gln-tRNAGln + ?
-
-
-
-
?
ATP + L-glutamyl-tRNAGln + L-glutamine

ADP + phosphate + L-glutaminyl-tRNAGln + L-glutamate
A0A509AHQ9; A0A509AM58
-
-
-
?
ATP + L-glutamyl-tRNAGln + L-glutamine
ADP + phosphate + L-glutaminyl-tRNAGln + L-glutamate
A0A509AHQ9; A0A509AM58
-
-
-
?
ATP + L-glutamyl-tRNAGln + L-glutamine
ADP + phosphate + L-glutaminyl-tRNAGln + L-glutamate
-
-
-
?
ATP + L-glutamyl-tRNAGln + L-glutamine
ADP + phosphate + L-glutaminyl-tRNAGln + L-glutamate
-
-
-
?
ATP + L-glutamyl-tRNAGln + L-glutamine
ADP + phosphate + L-glutaminyl-tRNAGln + L-glutamate
-
-
-
-
?
additional information

?
-
-
the enzyme possesses low glutaminase activity
-
-
?
additional information
?
-
-
the association of archaeal glutamyl-tRNA synthetase (ND-GluRS) with GatDE sequesters the tRNA synthetase for Gln-tRNAGln formation, with GatDE reducing the affinity of glutamyl-tRNA synthetase (ND-GluRS) for tRNAGlu 13fold
-
-
?
additional information
?
-
A0A509AHQ9; A0A509AM58
no substrate: L-glutamate
-
-
?
additional information
?
-
A0A509AHQ9; A0A509AM58
no substrate: L-glutamate
-
-
?
additional information
?
-
no substrate: L-glutamate
-
-
?
additional information
?
-
-
in absence of the amido acceptor, Glu-tRNAGln, the enzyme has basal glutaminase activity that is unaffected by ATP
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + Asp-tRNAAsn + L-glutamine
ADP + phosphate + Asn-tRNAAsn + L-glutamate
-
-
-
-
?
ATP + Glu-tRNAGln + L-glutamine
ADP + phosphate + Gln-tRNAGln + L-glutamate
ATP + Glu-tRNAGln + L-glutamine + H2O
ADP + phosphate + Gln-tRNAGln + L-glutamate
ATP + Glu-tRNAGln + L-glutamine

ADP + phosphate + Gln-tRNAGln + L-glutamate
-
disruption of this operon is lethal. Transamidation is the only pathway to Gln-tRNAGln in Bacillus subtilis. The enzyme furnishes a means for formation of correctly charged Gln-tRNAGln through the transamidation of misacylated Glu-tRNAGln, functionally replacing the lack of glutaminyl-tRNA synthetase activity in Gram-positive eubacteria, cyanobacteria, archaea and organelles
-
-
?
ATP + Glu-tRNAGln + L-glutamine
ADP + phosphate + Gln-tRNAGln + L-glutamate
-
-
-
-
?
ATP + Glu-tRNAGln + L-glutamine
ADP + phosphate + Gln-tRNAGln + L-glutamate
-
organisms lacking Gln-tRNA synthetase produce Gln-tRNAGln from misacylated Glu-tRNAGln through the transamidation activity of Glu-tRNAGln amidotransferase. The enzyme hydrolyzes Gln to Glu and NH3, using the latter product to transamidate Glu-tRNAGln in concert with ATP hydrolysis
-
-
?
ATP + Glu-tRNAGln + L-glutamine
ADP + phosphate + Gln-tRNAGln + L-glutamate
-
the enzyme produces Gln-tRNAGln required for plastidal protein biosynthesis
-
-
?
ATP + Glu-tRNAGln + L-glutamine + H2O

ADP + phosphate + Gln-tRNAGln + L-glutamate
-
-
-
-
?
ATP + Glu-tRNAGln + L-glutamine + H2O
ADP + phosphate + Gln-tRNAGln + L-glutamate
-
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(1R,2R)-1-(4-methylsulfonylphenyl)-2-(S-dioxo-L-methioneamido)-1,3-propanediol
-
-
(1R,2R)-1-(4-nitrophenyl)-2-(S-dioxo-L-methioneamido)-1,3-propanediol
-
-
(1R,2R)-1-phenyl-2-(S-dioxo-L-methioneamido)-1,3-propanediol
-
-
(1R,2S)-1-(4-nitrophenyl)-2-(S-dioxo-L-methioneamido)-1,3-propanediol
-
-
(1S,2R)-1-(4-nitrophenyl)-2-(S-dioxo-L-methioneamido)-1,3-propanediol
-
-
(1S,2S)-1-(4-nitrophenyl)-2-(S-dioxo-L-methioneamido)-1,3-propanediol
-
-
2'-O-(trinitrophenyl)adenosine 5'-triphosphate
-
IC50: 2.4 mM
3'-(L-alpha-aspartylamino)-3'-deoxy-N,N-dimethyladenosine
-
puromycin analogue
3'-deoxy-3'-(L-alpha-glutamylamino)-N,N-dimethyladenosine
-
puromycin analogue
3'-deoxy-3'-(L-glutaminylamino)-N,N-dimethyladenosine
-
puromycin analogue
3'-O-(trinitrophenyl)adenosine 5'-triphosphate
-
IC50: 2.4 mM
3'-[[(2S)-2-amino-4-(methylsulfinyl)butanoyl]amino]-3'-deoxy-N,N-dimethyladenosine
-
puromycin analogue
3'-[[(2S)-2-amino-4-(methylsulfonyl)butanoyl]amino]-3'-deoxy-N,N-dimethyladenosine
-
puromycin analogue
3'-[[(2S)-4-carboxy-2-hydroxybutanoyl]amino]-3'-deoxy-N,N-dimethyladenosine
-
puromycin analogue
3'-[[2-amino-4-(methylphosphinato)butanoyl]amino]-3'-deoxy-N,N-dimethyladenosine
-
puromycin analogue
6-diazo-5-oxonorleucine
-
blocking of glutamine-dependent reaction, no inhibition of ammonia-dependent reaction
adenosine 5'-[beta,gamma-methylene]triphosphate
-
IC50: 2.3 mM
ATP-gammaS
-
IC50: 0.19 mM
gamma-Glu boronic acid
-
IC50: 0.0016 mM
L-methionine-S-sulfoximine
-
at 1 mM, 3 mM or 5 mM, 20% inhibition
puromycin
-
aminonucleoside antibiotic produced by Streptomyces alboniger, very weak inhibitor of AdT
additional information
-
no inhibition by 6-diazo-5-oxonorleucine
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.00095
Asp-tRNAAsn
-
37°C, pH 7.2, amidotransferase activity
0.00118
Asp-tRNAGln
-
37°C, pH 7.2, amidotransferase activity
0.00042 - 0.0024
Glu-tRNAGln
0.0224
L-aspartyl-tRNAAsn
-
37°C, pH 7.2, amidotransferase activity
0.19 - 5.6
L-glutamyl-tRNAGln
0.0002
L-glutamyl-tRNAGlu
-
-
0.00539
tRNAGln1(UUG)
-
pH 7.2, 37°C
-
0.00133
tRNAGln2(CUG)
-
pH 7.2, 37°C
-
0.00361
tRNAGlu
-
pH 7.2, 37°C
additional information
additional information
-
aminoacylation kinetics of enzyme variants
-
0.117
ATP

-
-
0.2068
ATP
-
37°C, pH 7.2, amidotransferase activity
0.01
Gln

-
-
0.0207
Gln
-
37°C, pH 7.2, amidotransferase activity
0.0402
Gln
-
37°C, cosubstrate Asp-tRNAAsn + ATP, glutaminase activity
0.0509
Gln
-
37°C, cosubstrate Glu-tRNAGln + ATP, glutaminase activity
0.00042
Glu-tRNAGln

-
in the absence of GluRS2, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 12 mM MgCl2, at 37°C
0.00097
Glu-tRNAGln
-
in the presence of equimolar amounts of GluRS2, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 12 mM MgCl2, at 37°C
0.00134
Glu-tRNAGln
-
in the presence of 440fold excess of GluRS2, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 12 mM MgCl2, at 37°C
0.0017
Glu-tRNAGln
-
37°C, pH not specified in the publication
0.0023
Glu-tRNAGln
-
37°C, pH not specified in the publication, in the presence of glutamyl-tRNA synthetase (0.002 mM)
0.0024
Glu-tRNAGln
-
37°C, pH not specified in the publication, in the presence of bovine serum albumin (0.002 mM)
0.16
L-glutamine

wild-type, pH 7.5, 37°C
1.2
L-glutamine
N-terminal deletion mutant, pH 7.5, 37°C
0.19
L-glutamyl-tRNAGln

wild-type, pH 7.5, 37°C
5.6
L-glutamyl-tRNAGln
N-terminal deletion mutant, pH 7.5, 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1.3
Asp-tRNAAsn
-
37°C, pH 7.2, amidotransferase activity
3.61
Asp-tRNAGln
-
37°C, pH 7.2, amidotransferase activity
0.027
L-aspartyl-tRNAAsn
-
37°C, pH 7.2, amidotransferase activity
0.006
tRNAGln1(UUG)
-
pH 7.2, 37°C
-
0.41
tRNAGln2(CUG)
-
pH 7.2, 37°C
-
0.04
tRNAGlu
-
pH 7.2, 37°C
additional information
additional information
-
aminoacylation kinetics of enzyme variants
-
0.59
ATP

-
-
6.1
ATP
-
37°C, pH 7.2, amidotransferase activity
0.052 - 2.1
Gln

-
37°C, pH 7.2, cosubstrate: Glu-tRNAGln
3 - 6
Gln
-
37°C, pH 7.2, amidotransferase activity
3.49
Gln
-
37°C, pH 7.2, amidotransferase activity
10.29
Gln
-
37°C, pH 7.2, cosubstrate: Glu-tRNAGln
11.8
Gln
-
37°C, pH 7.2, cosubstrate Asp-tRNAAsn + ATP, glutaminase activity
0.21
Glu-tRNAGln

-
in the absence of GluRS2, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 12 mM MgCl2, at 37°C
0.21
Glu-tRNAGln
-
in the presence of 440fold excess of GluRS2, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 12 mM MgCl2, at 37°C
0.23
Glu-tRNAGln
-
in the presence of equimolar amounts of GluRS2, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 12 mM MgCl2, at 37°C
0.9
Glu-tRNAGln
-
37°C, pH not specified in the publication
0.9
Glu-tRNAGln
-
37°C, pH not specified in the publication, in the presence of bovine serum albumin (0.002 mM)
1.2
Glu-tRNAGln
-
37°C, pH not specified in the publication, in the presence of glutamyl-tRNA synthetase (0.002 mM)
1.4
L-glutamine

wild-type, pH 7.5, 37°C
1.7
L-glutamine
N-terminal deletion mutant, pH 7.5, 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.12
(1R,2R)-1-(4-methylsulfonylphenyl)-2-(S-dioxo-L-methioneamido)-1,3-propanediol
-
pH 7, temperature not specified in the publication
0.027
(1R,2R)-1-(4-nitrophenyl)-2-(S-dioxo-L-methioneamido)-1,3-propanediol
-
pH 7, temperature not specified in the publication
0.4
(1R,2R)-1-phenyl-2-(S-dioxo-L-methioneamido)-1,3-propanediol
-
pH 7, temperature not specified in the publication
0.37
(1R,2S)-1-(4-nitrophenyl)-2-(S-dioxo-L-methioneamido)-1,3-propanediol
-
pH 7, temperature not specified in the publication
2.8
(1S,2R)-1-(4-nitrophenyl)-2-(S-dioxo-L-methioneamido)-1,3-propanediol
-
pH 7, temperature not specified in the publication
0.16
(1S,2S)-1-(4-nitrophenyl)-2-(S-dioxo-L-methioneamido)-1,3-propanediol
-
pH 7, temperature not specified in the publication
0.134
3'-(L-alpha-aspartylamino)-3'-deoxy-N,N-dimethyladenosine
-
-
0.105
3'-deoxy-3'-(L-alpha-glutamylamino)-N,N-dimethyladenosine
-
-
0.045
3'-deoxy-3'-(L-glutaminylamino)-N,N-dimethyladenosine
-
-
0.011
3'-[[(2S)-2-amino-4-(methylsulfinyl)butanoyl]amino]-3'-deoxy-N,N-dimethyladenosine
-
-
0.004
3'-[[(2S)-2-amino-4-(methylsulfonyl)butanoyl]amino]-3'-deoxy-N,N-dimethyladenosine
-
-
0.13
3'-[[(2S)-4-carboxy-2-hydroxybutanoyl]amino]-3'-deoxy-N,N-dimethyladenosine
-
-
0.033
3'-[[2-amino-4-(methylphosphinato)butanoyl]amino]-3'-deoxy-N,N-dimethyladenosine
-
-
1.85
chloramphenicol
-
pH 7, temperature not specified in the publication
4.1
puromycin
-
very weak inhibitor of AdT
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.