6.3.5.7: glutaminyl-tRNA synthase (glutamine-hydrolysing)
This is an abbreviated version!
For detailed information about glutaminyl-tRNA synthase (glutamine-hydrolysing), go to the full flat file.
Word Map on EC 6.3.5.7
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6.3.5.7
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gln-trnagln
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gatcabs
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archaea
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aminoacyl-trnas
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trna-dependent
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transamidation
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misacylated
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mischarged
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asp-trnaasn
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aspartyl-trna
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asparaginyl-trna
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aminoacylation
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gln-trna
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methanothermobacter
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glutaminase
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thermautotrophicus
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trnaasn
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non-discriminating
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transamidase
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misaminoacylated
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glnrs
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analysis
- 6.3.5.7
- gln-trnagln
- gatcabs
- archaea
- aminoacyl-trnas
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trna-dependent
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transamidation
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misacylated
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mischarged
- asp-trnaasn
- aspartyl-trna
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asparaginyl-trna
- aminoacylation
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gln-trna
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methanothermobacter
- glutaminase
- thermautotrophicus
- trnaasn
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non-discriminating
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transamidase
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misaminoacylated
- glnrs
- analysis
Reaction
Synonyms
aa-tRNA amidotransferase, AdT, amidotransferase B, amidotransferase C, amidotransferase, glutamyl-transfer ribonucleate (glutamine-specific), aminoacyl-tRNA amidotransferase, BANKA_112750, gatA, GatB, GatCAB, GatCAB amidotransferase, GatDE, Gln4, GlnRS, Glu-AdT, Glu-amidotransferase, Glu-tRNAGln amidotransferase, Glu-tRNAGlnAT, GluAdT GatDE, GluRS, glutamyl-tRNA(Gln) amidotransferase, glutamyl-tRNAGln amidotransferase, nondiscriminating GluRS, PBANKA_071810, PF3D7_0416100, PF3D7_0628800, Qrsl1
ECTree
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Substrates Products
Substrates Products on EC 6.3.5.7 - glutaminyl-tRNA synthase (glutamine-hydrolysing)
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REACTION DIAGRAM
ATP + Glu-tRNAGln + L-asparagine
ADP + phosphate + Gln-tRNAGln + L-glutamate
-
-
-
-
?
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)
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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
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-
?
ATP + L-glutamate + tRNAGln2(CUG)
AMP + diphosphate + L-glutamyl-tRNAGln2(CUG)
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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
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-
-
-
?
ATP + L-glutamyl-tRNAGln + L-glutamine
ADP + phosphate + L-glutaminyl-tRNAGln + L-glutamate
ATP-gammaS + Glu-tRNAGln + L-glutamine
? + phosphate + Gln-tRNAGln + L-glutamate
-
-
-
?
ADP + phosphate + Asn-tRNAAsn + L-glutamate
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-
-
?
ATP + Asp-tRNAAsn + L-glutamine
ADP + phosphate + Asn-tRNAAsn + L-glutamate
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-
-
-
?
ATP + Asp-tRNAAsn + L-glutamine
ADP + phosphate + Asn-tRNAAsn + L-glutamate
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the enzyme transamidates Asp-tRNAAsn and Glu-tRNAGln with similar efficiency
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-
?
ATP + Asp-tRNAAsn + L-glutamine
ADP + phosphate + Asn-tRNAAsn + L-glutamate
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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
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-
?
ADP + phosphate + Gln-tRNAGln + Asp
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Asn is much less effective as amide donor than glutamine
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-
?
ATP + Glu-tRNAGln + Asn
ADP + phosphate + Gln-tRNAGln + Asp
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-
-
-
?
ADP + phosphate + Gln-tRNAGln + L-glutamate
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-
-
-
?
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
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the amidation of Glu-tRNAGln proceeds via a gamma-phosphorylated intermediate
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-
?
ATP + Glu-tRNAGln + L-glutamine
ADP + phosphate + Gln-tRNAGln + L-glutamate
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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
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-
?
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
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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
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-
-
?
ATP + Glu-tRNAGln + L-glutamine
ADP + phosphate + Gln-tRNAGln + L-glutamate
-
-
-
-
?
ATP + Glu-tRNAGln + L-glutamine
ADP + phosphate + Gln-tRNAGln + L-glutamate
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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
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-
?
ATP + Glu-tRNAGln + L-glutamine
ADP + phosphate + Gln-tRNAGln + L-glutamate
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Ser176A is the active-site nucleophile for facilitating Gln hydrolysis by the enzyme
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?
ATP + Glu-tRNAGln + L-glutamine
ADP + phosphate + Gln-tRNAGln + L-glutamate
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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
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?
ATP + Glu-tRNAGln + L-glutamine
ADP + phosphate + Gln-tRNAGln + L-glutamate
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the enzyme produces Gln-tRNAGln required for plastidal protein biosynthesis
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-
?
ADP + phosphate + Gln-tRNAGln + L-glutamate
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-
-
-
?
ATP + Glu-tRNAGln + L-glutamine + H2O
ADP + phosphate + Gln-tRNAGln + L-glutamate
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-
-
-
?
ADP + phosphate + Gln-tRNAGln + ?
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NH4Cl is much less effective as amide donor than glutamine
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-
?
ATP + Glu-tRNAGln + NH4Cl
ADP + phosphate + Gln-tRNAGln + ?
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-
-
-
?
ADP + phosphate + L-glutaminyl-tRNAGln + L-glutamate
A0A509AHQ9; A0A509AM58
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-
-
?
ATP + L-glutamyl-tRNAGln + L-glutamine
ADP + phosphate + L-glutaminyl-tRNAGln + L-glutamate
A0A509AHQ9; A0A509AM58
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-
-
?
ATP + L-glutamyl-tRNAGln + L-glutamine
ADP + phosphate + L-glutaminyl-tRNAGln + L-glutamate
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-
-
?
ATP + L-glutamyl-tRNAGln + L-glutamine
ADP + phosphate + L-glutaminyl-tRNAGln + L-glutamate
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-
-
?
ATP + L-glutamyl-tRNAGln + L-glutamine
ADP + phosphate + L-glutaminyl-tRNAGln + L-glutamate
Saccharomyces cerevisiae ATCC 204508 / S288c
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-
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?
?
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the enzyme possesses low glutaminase activity
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-
?
additional information
?
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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
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-
?
additional information
?
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A0A509AHQ9; A0A509AM58
no substrate: L-glutamate
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-
?
additional information
?
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A0A509AHQ9; A0A509AM58
no substrate: L-glutamate
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-
?
additional information
?
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no substrate: L-glutamate
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-
?
additional information
?
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in absence of the amido acceptor, Glu-tRNAGln, the enzyme has basal glutaminase activity that is unaffected by ATP
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-
?