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Asp-tRNAAsn + ?
Asn-tRNAAsn + ?
ATP + Asp-tRNAAsn + glutamine
ADP + phosphate + Asn-tRNAAsn + glutamate
ATP + Asp-tRNAAsn + L-glutamine
ADP + phosphate + Asn-tRNAAsn + L-glutamate
ATP + Asp-tRNAAsn + L-glutamine + H2O
ADP + phosphate + Asn-tRNAAsn + L-glutamate
-
-
-
-
?
ATP + Glu-tRNAGln + glutamine
ADP + Gln-tRNAGln + glutamate + phosphate
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 + L-aspartyl-tRNAAsn + L-glutamine
ADP + phosphate + L-asparaginyl-tRNAAsn + L-glutamate
ATP + L-aspartyl-tRNAAsn + L-glutamine + H2O
ADP + phosphate + L-asparaginyl-tRNAAsn + L-glutamate
-
-
-
-
?
Glu-tRNAGln + ?
Gln-tRNAGln + ?
additional information
?
-
Asp-tRNAAsn + ?
Asn-tRNAAsn + ?
-
tRNA-dependent transamidation pathway of Asn-tRNA formation, which is required for protein synthesis or under certain metabolic situations for asparagine synthesis
-
?
Asp-tRNAAsn + ?
Asn-tRNAAsn + ?
-
it is likely that the dual specificity amidotransferase serves in Asn-tRNA and Gln-tRNA formation in vivo
-
?
Asp-tRNAAsn + ?
Asn-tRNAAsn + ?
-
it is likely that the dual specificity amidotransferase serves in Asn-tRNA and Gln-tRNA formation in vivo
-
?
Asp-tRNAAsn + ?
Asn-tRNAAsn + ?
-
AdT is related to the biosynthesis of asparagine rather than to provide charged tRNA for protein biosynthesis
-
?
Asp-tRNAAsn + ?
Asn-tRNAAsn + ?
-
tRNA-dependent transamidation pathway of Asn-tRNA formation, only biosynthetic route to asparagine is via Asn-tRNA
-
?
Asp-tRNAAsn + ?
Asn-tRNAAsn + ?
-
tRNA-dependent transamidation pathway of Asn-tRNA formation, only biosynthetic route to asparagine is via Asn-tRNA
-
?
Asp-tRNAAsn + ?
Asn-tRNAAsn + ?
-
gatCAB genes encoded Asp-AdT may be responsible for biosynthesis of asparagine, glutamine as amide source
-
?
Asp-tRNAAsn + ?
Asn-tRNAAsn + ?
-
in vivo only Asn-tRNAAsn formation occurs
-
?
Asp-tRNAAsn + ?
Asn-tRNAAsn + ?
-
in vivo only Asn-tRNAAsn formation occurs
-
?
Asp-tRNAAsn + ?
Asn-tRNAAsn + ?
-
enzyme of the two-step pathway for the synthesis of Asn-tRNA that requires misacylated Asp-tRNAAsn as intermediate, which is generated by a Asp-tRNA synthetase
-
?
Asp-tRNAAsn + ?
Asn-tRNAAsn + ?
-
enzyme of the two-step pathway for the synthesis of Asn-tRNA that requires misacylated Asp-tRNAAsn as intermediate, which is generated by a Asp-tRNA synthetase
-
?
Asp-tRNAAsn + ?
Asn-tRNAAsn + ?
-
enzyme of the two-step pathway for the synthesis of Asn-tRNA that requires misacylated Asp-tRNAAsn as intermediate, which is generated by a Asp-tRNA synthetase
-
?
Asp-tRNAAsn + ?
Asn-tRNAAsn + ?
-
in vivo only Asn-tRNAAsn formation, because the substrate availability of Asp-tRNAAsn allows only one final product
-
?
Asp-tRNAAsn + ?
Asn-tRNAAsn + ?
-
tRNA-dependent transamidation pathway of Asn-tRNA formation, only biosynthetic route to asparagine is via Asn-tRNA
-
?
Asp-tRNAAsn + ?
Asn-tRNAAsn + ?
-
enzyme of the two-step pathway for the synthesis of Asn-tRNA that requires misacylated Asp-tRNAAsn as intermediate, which is generated by a Asp-tRNA synthetase
-
?
Asp-tRNAAsn + ?
Asn-tRNAAsn + ?
-
it is likely that the dual specificity amidotransferase serves in Asn-tRNA and Gln-tRNA formation in vivo
-
?
Asp-tRNAAsn + ?
Asn-tRNAAsn + ?
-
-
-
?
Asp-tRNAAsn + ?
Asn-tRNAAsn + ?
-
-
-
?
Asp-tRNAAsn + ?
Asn-tRNAAsn + ?
-
the mischarging Asp-tRNA synthetase correlates with the absence in the genome of Asn-tRNA synthetase and the presence of Asp-tRNAAsn amidotransferase, employed by the transamidation pathway
-
?
Asp-tRNAAsn + ?
Asn-tRNAAsn + ?
-
enzyme of the two-step pathway for the synthesis of Asn-tRNA that requires misacylated Asp-tRNAAsn as intermediate, which is generated by a Asp-tRNA synthetase
-
?
Asp-tRNAAsn + ?
Asn-tRNAAsn + ?
-
-
-
?
Asp-tRNAAsn + ?
Asn-tRNAAsn + ?
-
in vivo only Asn-tRNAAsn formation occurs, since Thermus possesses a mischarging Asp-tRNA synthetase, but lacks a mischarging Glu-tRNA synthetase, and cellular activity of AdTs only depends upon presence or lack of the mischarging amino acyl-tRNA synthetases, explaining why those enzymes have not restricted their specificity
-
?
Asp-tRNAAsn + ?
Asn-tRNAAsn + ?
-
AdT is related to the biosynthesis of asparagine rather than to provide charged tRNA for protein biosynthesis
-
?
Asp-tRNAAsn + ?
Asn-tRNAAsn + ?
-
tRNA-dependent transamidation pathway of Asn-tRNA formation, only biosynthetic route to asparagine is via Asn-tRNA
-
?
Asp-tRNAAsn + ?
Asn-tRNAAsn + ?
-
enzyme of the two-step pathway for the synthesis of Asn-tRNA that requires misacylated Asp-tRNAAsn as intermediate, which is generated by a Asp-tRNA synthetase
-
?
Asp-tRNAAsn + ?
Asn-tRNAAsn + ?
-
enzyme of the two-step pathway for the synthesis of Asn-tRNA that requires misacylated Asp-tRNAAsn as intermediate, which is generated by a Asp-tRNA synthetase
-
?
Asp-tRNAAsn + ?
Asn-tRNAAsn + ?
-
in vivo only Asn-tRNAAsn formation occurs, since Thermus possesses a mischarging Asp-tRNA synthetase, but lacks a mischarging Glu-tRNA synthetase, and cellular activity of AdTs only depends upon presence or lack of the mischarging amino acyl-tRNA synthetases, explaining why those enzymes have not restricted their specificity
-
?
Asp-tRNAAsn + ?
Asn-tRNAAsn + ?
-
enzyme of the two-step pathway for the synthesis of Asn-tRNA that requires misacylated Asp-tRNAAsn as intermediate, which is generated by a Asp-tRNA synthetase
-
?
ATP + Asp-tRNA + L-Gln
?
-
in presence of tRNA-dependent amidotransferase AdT, amidation activity
-
-
?
ATP + Asp-tRNA + L-Gln
?
-
in presence of tRNA-dependent amidotransferase AdT, amidation activity
-
-
?
ATP + Asp-tRNAAsn + glutamine
ADP + phosphate + Asn-tRNAAsn + glutamate
-
-
-
?
ATP + Asp-tRNAAsn + glutamine
ADP + phosphate + Asn-tRNAAsn + glutamate
-
-
-
?
ATP + Asp-tRNAAsn + glutamine
ADP + phosphate + Asn-tRNAAsn + glutamate
-
-
-
?
ATP + Asp-tRNAAsn + glutamine
ADP + phosphate + Asn-tRNAAsn + glutamate
-
-
-
?
ATP + Asp-tRNAAsn + glutamine
ADP + phosphate + Asn-tRNAAsn + glutamate
-
-
-
?
ATP + Asp-tRNAAsn + glutamine
ADP + phosphate + Asn-tRNAAsn + glutamate
-
-
-
?
ATP + Asp-tRNAAsn + glutamine
ADP + phosphate + Asn-tRNAAsn + glutamate
-
-
-
?
ATP + Asp-tRNAAsn + glutamine
ADP + phosphate + Asn-tRNAAsn + glutamate
-
-
-
?
ATP + Asp-tRNAAsn + glutamine
ADP + phosphate + Asn-tRNAAsn + glutamate
-
dual-specific Asp/Glu-AdT, rates for conversion of Glu to Gln are about twice as fast as the rate of Asp to Asn conversion, enzyme uses glutamine, asparagine or ammonia as amide donors in the presence of ATP, GTP or CTP
-
?
ATP + Asp-tRNAAsn + glutamine
ADP + phosphate + Asn-tRNAAsn + glutamate
-
dual tRNA specificity: formation of Asn-tRNA and Gln-tRNA
-
?
ATP + Asp-tRNAAsn + glutamine
ADP + phosphate + Asn-tRNAAsn + glutamate
-
-
-
?
ATP + Asp-tRNAAsn + glutamine
ADP + phosphate + Asn-tRNAAsn + glutamate
-
-
-
?
ATP + Asp-tRNAAsn + glutamine
ADP + phosphate + Asn-tRNAAsn + glutamate
-
single enzyme with both Gln-tRNA and Asp-tRNA transamidation activities, but functions as Asp-AdT, since Deinococcus do not produce the required mischarged Glu-tRNAGln substrate
-
?
ATP + Asp-tRNAAsn + glutamine
ADP + phosphate + Asn-tRNAAsn + glutamate
-
dual-specific Asp/Glu-AdT is able to amidate both mischarged tRNAGln and tRNAAsn, but functions as Asp-AdT
-
?
ATP + Asp-tRNAAsn + glutamine
ADP + phosphate + Asn-tRNAAsn + glutamate
-
dual-specific Asp/Glu-AdT is able to amidate both mischarged tRNAGln and tRNAAsn, but functions as Asp-AdT
-
?
ATP + Asp-tRNAAsn + glutamine
ADP + phosphate + Asn-tRNAAsn + glutamate
-
dual tRNA specificity: formation of Asn-tRNA and Gln-tRNA
-
?
ATP + Asp-tRNAAsn + glutamine
ADP + phosphate + Asn-tRNAAsn + glutamate
-
dual tRNA specificity: formation of Asn-tRNA and Gln-tRNA
-
?
ATP + Asp-tRNAAsn + glutamine
ADP + phosphate + Asn-tRNAAsn + glutamate
-
single enzyme with both Gln-tRNA and Asp-tRNA transamidation activities, but functions as Asp-AdT, since Deinococcus do not produce the required mischarged Glu-tRNAGln substrate
-
?
ATP + Asp-tRNAAsn + glutamine
ADP + phosphate + Asn-tRNAAsn + glutamate
-
dual tRNA specificity: formation of Asn-tRNA and Gln-tRNA
-
?
ATP + Asp-tRNAAsn + glutamine
ADP + phosphate + Asn-tRNAAsn + glutamate
-
-
-
?
ATP + Asp-tRNAAsn + glutamine
ADP + phosphate + Asn-tRNAAsn + glutamate
-
-
-
?
ATP + Asp-tRNAAsn + glutamine
ADP + phosphate + Asn-tRNAAsn + glutamate
-
-
-
?
ATP + Asp-tRNAAsn + glutamine
ADP + phosphate + Asn-tRNAAsn + glutamate
-
dual tRNA specificity: formation of Asn-tRNA and Gln-tRNA
-
?
ATP + Asp-tRNAAsn + glutamine
ADP + phosphate + Asn-tRNAAsn + glutamate
-
-
-
?
ATP + Asp-tRNAAsn + glutamine
ADP + phosphate + Asn-tRNAAsn + glutamate
-
-
-
?
ATP + Asp-tRNAAsn + glutamine
ADP + phosphate + Asn-tRNAAsn + glutamate
-
-
-
?
ATP + Asp-tRNAAsn + glutamine
ADP + phosphate + Asn-tRNAAsn + glutamate
-
-
-
?
ATP + Asp-tRNAAsn + glutamine
ADP + phosphate + Asn-tRNAAsn + glutamate
-
-
-
?
ATP + Asp-tRNAAsn + glutamine
ADP + phosphate + Asn-tRNAAsn + glutamate
-
dual tRNA specificity: formation of Asn-tRNA and Gln-tRNA
-
?
ATP + Asp-tRNAAsn + glutamine
ADP + phosphate + Asn-tRNAAsn + glutamate
-
dual tRNA specificity: formation of Asn-tRNA and Gln-tRNA
-
?
ATP + Asp-tRNAAsn + glutamine
ADP + phosphate + Asn-tRNAAsn + glutamate
-
-
-
-
?
ATP + Asp-tRNAAsn + glutamine
ADP + phosphate + Asn-tRNAAsn + glutamate
-
-
-
?
ATP + Asp-tRNAAsn + glutamine
ADP + phosphate + Asn-tRNAAsn + glutamate
-
-
-
?
ATP + Asp-tRNAAsn + glutamine
ADP + phosphate + Asn-tRNAAsn + glutamate
-
-
-
?
ATP + Asp-tRNAAsn + glutamine
ADP + phosphate + Asn-tRNAAsn + glutamate
-
no restricted substrate specificity of tRNA-dependent AdT: dual-specific Asp/Glu-AdT, enzyme catalyzes transamidation of Asp-tRNAAsn, since Thermus possesses a mischarging Asp-tRNA synthetase, but lacks a mischarging Glu-tRNA synthetase, GatA subunit can discriminate between Asp-tRNAAsn and Glu-tRNAGln and therefore is implicated in binding of the tRNA
forms Asn-tRNAAsn
?
ATP + Asp-tRNAAsn + glutamine
ADP + phosphate + Asn-tRNAAsn + glutamate
-
dual-specific Asp/Glu-AdT is able to amidate both mischarged tRNAGln and tRNAAsn, but functions as Asp-AdT
-
?
ATP + Asp-tRNAAsn + glutamine
ADP + phosphate + Asn-tRNAAsn + glutamate
-
no restricted substrate specificity of tRNA-dependent AdT: dual-specific Asp/Glu-AdT, enzyme catalyzes transamidation of Asp-tRNAAsn, since Thermus possesses a mischarging Asp-tRNA synthetase, but lacks a mischarging Glu-tRNA synthetase, GatA subunit can discriminate between Asp-tRNAAsn and Glu-tRNAGln and therefore is implicated in binding of the tRNA
forms Asn-tRNAAsn
?
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 + glutamine
ADP + Gln-tRNAGln + glutamate + phosphate
-
-
-
?
ATP + Glu-tRNAGln + glutamine
ADP + Gln-tRNAGln + glutamate + phosphate
-
in vitro both Asp-tRNAAsn and Glu-tRNAGln amidation activities, in vivo only Gln-tRNAGln formation
-
?
ATP + Glu-tRNAGln + glutamine
ADP + Gln-tRNAGln + glutamate + phosphate
-
in vitro both Asp-tRNAAsn and Glu-tRNAGln amidation activities, in vivo only Gln-tRNAGln formation
-
?
ATP + Glu-tRNAGln + glutamine
ADP + Gln-tRNAGln + glutamate + phosphate
-
Asp/Glu-AdT carries out Gln-tRNA formation, since Bacillus contains a non-discriminating GluRS, but lacks a mischarging AspRS
-
?
ATP + Glu-tRNAGln + glutamine
ADP + Gln-tRNAGln + glutamate + phosphate
-
Asp/Glu-AdT carries out Gln-tRNA formation, since Bacillus contains a non-discriminating GluRS, but lacks a mischarging AspRS
-
?
ATP + Glu-tRNAGln + glutamine
ADP + Gln-tRNAGln + glutamate + phosphate
-
dual tRNA specificity: formation of Asn-tRNA and Gln-tRNA
-
?
ATP + Glu-tRNAGln + glutamine
ADP + Gln-tRNAGln + glutamate + phosphate
-
dual-specific Asp/Glu-AdT, rates for conversion of Glu to Gln are about twice as fast as the rate of Asp to Asn conversion, enzyme uses glutamine, asparagine or ammonia as amide donors in the presence of ATP or GTP
-
?
ATP + Glu-tRNAGln + glutamine
ADP + Gln-tRNAGln + glutamate + phosphate
-
-
-
?
ATP + Glu-tRNAGln + glutamine
ADP + Gln-tRNAGln + glutamate + phosphate
-
dual-specific Asp/Glu-AdT is able to amidate both mischarged tRNAGln and tRNAAsn, but functions as Asp-AdT
-
?
ATP + Glu-tRNAGln + glutamine
ADP + Gln-tRNAGln + glutamate + phosphate
-
dual-specific Asp/Glu-AdT is able to amidate both mischarged tRNAGln and tRNAAsn, but functions as Asp-AdT
-
?
ATP + Glu-tRNAGln + glutamine
ADP + Gln-tRNAGln + glutamate + phosphate
-
in vitro both Asp-tRNAAsn and Glu-tRNAGln amidation activities, in vivo only Asn-tRNAAsn formation
-
?
ATP + Glu-tRNAGln + glutamine
ADP + Gln-tRNAGln + glutamate + phosphate
-
dual-specific Asp/Glu-AdT is able to amidate both mischarged tRNAGln and tRNAAsn, but functions as Asp-AdT
-
?
ATP + Glu-tRNAGln + glutamine
ADP + Gln-tRNAGln + glutamate + phosphate
-
dual tRNA specificity: formation of Asn-tRNA and Gln-tRNA
-
?
ATP + Glu-tRNAGln + glutamine
ADP + Gln-tRNAGln + glutamate + phosphate
-
-
-
-
?
ATP + Glu-tRNAGln + glutamine
ADP + Gln-tRNAGln + glutamate + phosphate
-
dual tRNA specificity: formation of Asn-tRNA and Gln-tRNA
-
-
?
ATP + Glu-tRNAGln + glutamine
ADP + Gln-tRNAGln + glutamate + phosphate
-
dual tRNA specificity: formation of Asn-tRNA and Gln-tRNA
-
-
?
ATP + Glu-tRNAGln + glutamine
ADP + Gln-tRNAGln + glutamate + phosphate
-
the enzyme has no Glu-tRNAGln substrate in its host, but it can transamidate heterologous Glu-tRNAGln
-
-
?
ATP + Glu-tRNAGln + glutamine
ADP + Gln-tRNAGln + glutamate + phosphate
-
dual-specific Asp/Glu-AdT is able to amidate both mischarged tRNAGln and tRNAAsn, but functions as Asp-AdT
-
?
ATP + Glu-tRNAGln + glutamine
ADP + Gln-tRNAGln + glutamate + phosphate
-
in vitro both Asp-tRNAAsn and Glu-tRNAGln amidation activities, in vivo only Asn-tRNAAsn formation
-
?
ATP + Glu-tRNAGln + glutamine
ADP + Gln-tRNAGln + glutamate + phosphate
-
in vitro both Asp-tRNAAsn and Glu-tRNAGln amidation activities, in vivo only Asn-tRNAAsn formation
-
?
ATP + L-aspartyl-tRNAAsn + L-glutamine
ADP + phosphate + L-asparaginyl-tRNAAsn + L-glutamate
-
-
-
-
?
ATP + L-aspartyl-tRNAAsn + L-glutamine
ADP + phosphate + L-asparaginyl-tRNAAsn + L-glutamate
-
recombinantly produced tRNA substrate
-
-
?
ATP + L-aspartyl-tRNAAsn + L-glutamine
ADP + phosphate + L-asparaginyl-tRNAAsn + L-glutamate
-
-
-
-
?
ATP + L-aspartyl-tRNAAsn + L-glutamine
ADP + phosphate + L-asparaginyl-tRNAAsn + L-glutamate
-
recombinantly produced tRNA substrate
-
-
?
ATP + L-aspartyl-tRNAAsn + L-glutamine
ADP + phosphate + L-asparaginyl-tRNAAsn + L-glutamate
-
-
-
-
?
ATP + L-aspartyl-tRNAAsn + L-glutamine
ADP + phosphate + L-asparaginyl-tRNAAsn + L-glutamate
-
the Halobacter pylori Asp/Glu-Adt can utilize Escherichia coli Asp-tRNAAsn as a substrate, recombinantly produced tRNA substrate
-
-
?
Glu-tRNAGln + ?
Gln-tRNAGln + ?
-
it is likely that the dual specificity amidotransferase serves in Asn-tRNA and Gln-tRNA formation in vivo
-
?
Glu-tRNAGln + ?
Gln-tRNAGln + ?
-
it is likely that the dual specificity amidotransferase serves in Asn-tRNA and Gln-tRNA formation in vivo
-
?
Glu-tRNAGln + ?
Gln-tRNAGln + ?
-
tRNA-dependent transamidation pathway of Gln-tRNA formation, which is required for protein synthesis or under certain metabolic situations for glutamine synthesis
-
?
Glu-tRNAGln + ?
Gln-tRNAGln + ?
-
it is likely that the dual specificity amidotransferase serves in Asn-tRNA and Gln-tRNA formation in vivo
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
archaeal enzyme resembles the bacterial Glu/Asp-AdT, but can only amidate Asp-tRNAAsn and not Glu-tRNAGln
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
archaeal enzyme resembles the bacterial Glu/Asp-AdT, but can only amidate Asp-tRNAAsn and not Glu-tRNAGln
-
-
?
additional information
?
-
-
the parasite Brugia malayi enzyme, in analogy to the human enzyme, induces human leukocyte chemotaxis and activates G-protein-coupled receptors CXCR1 and CXCR2, but not CXCR3, filarial asparaginyl-tRNA synthetase, AsnRS, is known to be an immunodominant antigen that induces strong human immunoglobulin G3 responses and contributes to the development of chronic inflammatory disease such as lymphatic filariasis, overview
-
-
?
additional information
?
-
-
GatA is likely to be the catalytic subunit, GatB may be responsible for tRNA binding and GatC may be involved in a channeling mechanism, in which the misacylated tRNA formed by the non-discriminating AA-tRNA synthetase could be handed off to the AdT
-
-
?
additional information
?
-
-
no substrates: correctly charged Asp-tRNAAsp and Glu-tRNAGlu
-
-
?
additional information
?
-
-
no substrates: correctly charged Asp-tRNAAsp and Glu-tRNAGlu
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
enzyme specificity depends on the biochemical context, i.e. on the availability of the mischarged aminoacyl-tRNA substrate, which is controlled by the presence of a nondiscriminating GluRS or AspRS
-
-
?
additional information
?
-
-
no substrates: correctly charged Asp-tRNAAsp and Glu-tRNAGlu
-
-
?
additional information
?
-
-
A subunit is a tRNA-independent glutaminase, B subunit is a putative tRNA-binding protein
-
-
?
additional information
?
-
-
A subunit is a tRNA-independent glutaminase, B subunit is a putative tRNA-binding protein
-
-
?
additional information
?
-
-
in bacteria that lack AsnRS, EC 6.1.1.12, AspRS is nondiscriminating, EC 6.1.1.23, and generates both Asp-tRNAAsp and the noncanonical, misacylated Asp-tRNAAsn, this misacylated tRNA is subsequently repaired by the glutamine-dependent Asp-tRNAAsn/Glu-tRNAGln amidotransferase, overview
-
-
?
additional information
?
-
-
in bacteria that lack AsnRS, EC 6.1.1.12, AspRS is nondiscriminating, EC 6.1.1.23, and generates both Asp-tRNAAsp and the noncanonical, misacylated Asp-tRNAAsn, this misacylated tRNA is subsequently repaired by the glutamine-dependent Asp-tRNAAsn/Glu-tRNAGln amidotransferase, overview
-
-
?
additional information
?
-
-
in bacteria that lack AsnRS, EC 6.1.1.12, AspRS is nondiscriminating, EC 6.1.1.23, and generates both Asp-tRNAAsp and the noncanonical, misacylated Asp-tRNAAsn, this misacylated tRNA is subsequently repaired by the glutamine-dependent Asp-tRNAAsn/Glu-tRNAGln amidotransferase, overview
-
-
?
additional information
?
-
-
human cytoplasmic aminoacyl-tRNA synthetases, which are autoantigens in idiopathic inflammatory myopathies, activate chemokine receptors on T lymphocytes, monocytes, and immature dendritic cells by recruiting immune cells that could induce innate and adaptive immune responses
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
archaeal enzyme resembles the bacterial Glu/Asp-AdT, but can only amidate Asp-tRNAAsn and not Glu-tRNAGln
-
-
?
additional information
?
-
-
archaeal enzyme resembles the bacterial Glu/Asp-AdT, but can only amidate Asp-tRNAAsn and not Glu-tRNAGln
-
-
?
additional information
?
-
-
no substrates: correctly charged Asp-tRNAAsp and Glu-tRNAGlu
-
-
?
additional information
?
-
-
no substrates: correctly charged Asp-tRNAAsp and Glu-tRNAGlu
-
-
?
additional information
?
-
-
a nondiscriminating aspartyl-tRNA synthetase, ND-DRS, first generates a mischarged aspartyl-tRNAAsn that dissociates from the enzyme and binds to a tRNA-dependent amidotransferase, AdT, which then converts the tRNA-bound aspartate into asparagine, the ND-DRS, tRNAAsn, and AdT assemble into a specific ribonucleoprotein complex called transamidosome that remains stable during the overall catalytic process, overview
-
-
?
additional information
?
-
-
enzyme specificity depends on the biochemical context, i.e. on the availability of the mischarged aminoacyl-tRNA substrate, which is controlled by the presence of a nondiscriminating GluRS or AspRS
-
-
?
additional information
?
-
-
cellular activity of AdTs only depends upon presence or lack of the mischarging amino acyl-tRNA synthetases
-
-
?
additional information
?
-
-
a nondiscriminating aspartyl-tRNA synthetase, ND-DRS, first generates a mischarged aspartyl-tRNAAsn that dissociates from the enzyme and binds to a tRNA-dependent amidotransferase, AdT, which then converts the tRNA-bound aspartate into asparagine, the ND-DRS, tRNAAsn, and AdT assemble into a specific ribonucleoprotein complex called transamidosome that remains stable during the overall catalytic process, overview
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additional information
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cellular activity of AdTs only depends upon presence or lack of the mischarging amino acyl-tRNA synthetases
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Asp-tRNAAsn + ?
Asn-tRNAAsn + ?
ATP + Asp-tRNAAsn + L-glutamine + H2O
ADP + phosphate + Asn-tRNAAsn + L-glutamate
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?
ATP + L-aspartyl-tRNAAsn + L-glutamine
ADP + phosphate + L-asparaginyl-tRNAAsn + L-glutamate
Glu-tRNAGln + ?
Gln-tRNAGln + ?
additional information
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Asp-tRNAAsn + ?
Asn-tRNAAsn + ?
-
tRNA-dependent transamidation pathway of Asn-tRNA formation, which is required for protein synthesis or under certain metabolic situations for asparagine synthesis
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?
Asp-tRNAAsn + ?
Asn-tRNAAsn + ?
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it is likely that the dual specificity amidotransferase serves in Asn-tRNA and Gln-tRNA formation in vivo
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?
Asp-tRNAAsn + ?
Asn-tRNAAsn + ?
-
it is likely that the dual specificity amidotransferase serves in Asn-tRNA and Gln-tRNA formation in vivo
-
?
Asp-tRNAAsn + ?
Asn-tRNAAsn + ?
-
AdT is related to the biosynthesis of asparagine rather than to provide charged tRNA for protein biosynthesis
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?
Asp-tRNAAsn + ?
Asn-tRNAAsn + ?
-
tRNA-dependent transamidation pathway of Asn-tRNA formation, only biosynthetic route to asparagine is via Asn-tRNA
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?
Asp-tRNAAsn + ?
Asn-tRNAAsn + ?
-
tRNA-dependent transamidation pathway of Asn-tRNA formation, only biosynthetic route to asparagine is via Asn-tRNA
-
?
Asp-tRNAAsn + ?
Asn-tRNAAsn + ?
-
gatCAB genes encoded Asp-AdT may be responsible for biosynthesis of asparagine, glutamine as amide source
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Asp-tRNAAsn + ?
Asn-tRNAAsn + ?
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in vivo only Asn-tRNAAsn formation occurs
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Asp-tRNAAsn + ?
Asn-tRNAAsn + ?
-
in vivo only Asn-tRNAAsn formation occurs
-
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Asp-tRNAAsn + ?
Asn-tRNAAsn + ?
-
enzyme of the two-step pathway for the synthesis of Asn-tRNA that requires misacylated Asp-tRNAAsn as intermediate, which is generated by a Asp-tRNA synthetase
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?
Asp-tRNAAsn + ?
Asn-tRNAAsn + ?
-
enzyme of the two-step pathway for the synthesis of Asn-tRNA that requires misacylated Asp-tRNAAsn as intermediate, which is generated by a Asp-tRNA synthetase
-
?
Asp-tRNAAsn + ?
Asn-tRNAAsn + ?
-
enzyme of the two-step pathway for the synthesis of Asn-tRNA that requires misacylated Asp-tRNAAsn as intermediate, which is generated by a Asp-tRNA synthetase
-
?
Asp-tRNAAsn + ?
Asn-tRNAAsn + ?
-
in vivo only Asn-tRNAAsn formation, because the substrate availability of Asp-tRNAAsn allows only one final product
-
?
Asp-tRNAAsn + ?
Asn-tRNAAsn + ?
-
tRNA-dependent transamidation pathway of Asn-tRNA formation, only biosynthetic route to asparagine is via Asn-tRNA
-
?
Asp-tRNAAsn + ?
Asn-tRNAAsn + ?
-
enzyme of the two-step pathway for the synthesis of Asn-tRNA that requires misacylated Asp-tRNAAsn as intermediate, which is generated by a Asp-tRNA synthetase
-
?
Asp-tRNAAsn + ?
Asn-tRNAAsn + ?
-
it is likely that the dual specificity amidotransferase serves in Asn-tRNA and Gln-tRNA formation in vivo
-
?
Asp-tRNAAsn + ?
Asn-tRNAAsn + ?
-
-
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?
Asp-tRNAAsn + ?
Asn-tRNAAsn + ?
-
-
-
?
Asp-tRNAAsn + ?
Asn-tRNAAsn + ?
-
the mischarging Asp-tRNA synthetase correlates with the absence in the genome of Asn-tRNA synthetase and the presence of Asp-tRNAAsn amidotransferase, employed by the transamidation pathway
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Asp-tRNAAsn + ?
Asn-tRNAAsn + ?
-
enzyme of the two-step pathway for the synthesis of Asn-tRNA that requires misacylated Asp-tRNAAsn as intermediate, which is generated by a Asp-tRNA synthetase
-
?
Asp-tRNAAsn + ?
Asn-tRNAAsn + ?
-
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?
Asp-tRNAAsn + ?
Asn-tRNAAsn + ?
-
in vivo only Asn-tRNAAsn formation occurs, since Thermus possesses a mischarging Asp-tRNA synthetase, but lacks a mischarging Glu-tRNA synthetase, and cellular activity of AdTs only depends upon presence or lack of the mischarging amino acyl-tRNA synthetases, explaining why those enzymes have not restricted their specificity
-
?
Asp-tRNAAsn + ?
Asn-tRNAAsn + ?
-
AdT is related to the biosynthesis of asparagine rather than to provide charged tRNA for protein biosynthesis
-
?
Asp-tRNAAsn + ?
Asn-tRNAAsn + ?
-
tRNA-dependent transamidation pathway of Asn-tRNA formation, only biosynthetic route to asparagine is via Asn-tRNA
-
?
Asp-tRNAAsn + ?
Asn-tRNAAsn + ?
-
enzyme of the two-step pathway for the synthesis of Asn-tRNA that requires misacylated Asp-tRNAAsn as intermediate, which is generated by a Asp-tRNA synthetase
-
?
Asp-tRNAAsn + ?
Asn-tRNAAsn + ?
-
enzyme of the two-step pathway for the synthesis of Asn-tRNA that requires misacylated Asp-tRNAAsn as intermediate, which is generated by a Asp-tRNA synthetase
-
?
Asp-tRNAAsn + ?
Asn-tRNAAsn + ?
-
in vivo only Asn-tRNAAsn formation occurs, since Thermus possesses a mischarging Asp-tRNA synthetase, but lacks a mischarging Glu-tRNA synthetase, and cellular activity of AdTs only depends upon presence or lack of the mischarging amino acyl-tRNA synthetases, explaining why those enzymes have not restricted their specificity
-
?
Asp-tRNAAsn + ?
Asn-tRNAAsn + ?
-
enzyme of the two-step pathway for the synthesis of Asn-tRNA that requires misacylated Asp-tRNAAsn as intermediate, which is generated by a Asp-tRNA synthetase
-
?
ATP + L-aspartyl-tRNAAsn + L-glutamine
ADP + phosphate + L-asparaginyl-tRNAAsn + L-glutamate
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-
-
-
?
ATP + L-aspartyl-tRNAAsn + L-glutamine
ADP + phosphate + L-asparaginyl-tRNAAsn + L-glutamate
-
-
-
-
?
ATP + L-aspartyl-tRNAAsn + L-glutamine
ADP + phosphate + L-asparaginyl-tRNAAsn + L-glutamate
-
-
-
-
?
Glu-tRNAGln + ?
Gln-tRNAGln + ?
-
it is likely that the dual specificity amidotransferase serves in Asn-tRNA and Gln-tRNA formation in vivo
-
?
Glu-tRNAGln + ?
Gln-tRNAGln + ?
-
it is likely that the dual specificity amidotransferase serves in Asn-tRNA and Gln-tRNA formation in vivo
-
?
Glu-tRNAGln + ?
Gln-tRNAGln + ?
-
tRNA-dependent transamidation pathway of Gln-tRNA formation, which is required for protein synthesis or under certain metabolic situations for glutamine synthesis
-
?
Glu-tRNAGln + ?
Gln-tRNAGln + ?
-
it is likely that the dual specificity amidotransferase serves in Asn-tRNA and Gln-tRNA formation in vivo
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?
additional information
?
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the parasite Brugia malayi enzyme, in analogy to the human enzyme, induces human leukocyte chemotaxis and activates G-protein-coupled receptors CXCR1 and CXCR2, but not CXCR3, filarial asparaginyl-tRNA synthetase, AsnRS, is known to be an immunodominant antigen that induces strong human immunoglobulin G3 responses and contributes to the development of chronic inflammatory disease such as lymphatic filariasis, overview
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additional information
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human cytoplasmic aminoacyl-tRNA synthetases, which are autoantigens in idiopathic inflammatory myopathies, activate chemokine receptors on T lymphocytes, monocytes, and immature dendritic cells by recruiting immune cells that could induce innate and adaptive immune responses
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Curnow, A.W.; Tumbula, D.L.; Pelaschier, J.T.; Min, B.; Sll, D.
Glutamyl-tRNAGln amidotransferase in Deinococcus radiodurans may be confined to asparagine biosynthesis
Proc. Natl. Acad. Sci. USA
95
12838-12843
1998
Bacillus subtilis, Deinococcus radiodurans, Haloferax volcanii, Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539
brenda
Becker, H.D.; Min, B.; Jacobi, C.; Raczniak, G.; Pelaschier, J.; Roy, H.; Klein, S.; Kern, D.; Sll, D.
The heterotrimeric Thermus thermophilus Asp-tRNA(Asn) amidotransferase can also generate Gln-tRNA(Gln)
FEBS Lett.
476
140-144
2000
Bacillus subtilis, Deinococcus radiodurans, Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
brenda
Tumbula-Hansen, D.; Feng, L.; Toogood, H.; Stetter, K.O.; Sll, D.
Evolutionary divergence of the archaeal aspartyl-tRNA synthetases into discriminating and nondiscriminating forms
J. Biol. Chem.
277
37184-37190
2002
Methanothermobacter thermautotrophicus
brenda
Raczniak, G.; Becker, H.D.; Min, B.; Sll, D.
A single amidotransferase forms asparaginyl-tRNA and glutaminyl-tRNA in Chlamydia trachomatis
J. Biol. Chem.
276
45862-45867
2001
Chlamydia trachomatis
brenda
Min, B.; Pelaschier, J.T.; Graham, D.E.; Tumbula-Hansen, D.; Sll, D.
Transfer RNA-dependent amino acid biosynthesis: An essential route to asparagine formation
Proc. Natl. Acad. Sci. USA
99
2678-2683
2002
Deinococcus radiodurans, Thermus thermophilus, Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539
brenda
Ibba, M.; Sll, D.
Aminoacyl-tRNA synthesis
Annu. Rev. Biochem.
69
617-650
2000
Aeropyrum pernix, Archaeoglobus fulgidus, Bacillus subtilis, Deinococcus radiodurans, Thermus thermophilus, Methanothermobacter thermautotrophicus, Methanocaldococcus jannaschii
brenda
Tumbula, D.L.; Becker, H.D.; Chang, W.Z.; Sll, D.
Domain-specific recruitment of amide amino acids for protein synthesis
Nature
407
106-110
2000
Aeropyrum pernix, Archaeoglobus fulgidus, Bacillus subtilis, Chlamydia trachomatis, Deinococcus radiodurans, Halobacterium salinarum, Helicobacter pylori, Methanocaldococcus jannaschii, Methanosarcina mazei, Methanothermobacter thermautotrophicus, Methanothermobacter thermautotrophicus DELTAH, Saccharolobus solfataricus, Sulfurisphaera tokodaii
brenda
Akochy, P.M.; Bernard, D.; Roy, P.H.; Lapointe, J.
Direct glutaminyl-tRNA biosynthesis and indirect asparaginyl-tRNA biosynthesis in Pseudomonas aeruginosa PAO1
J. Bacteriol.
186
767-776
2004
Pseudomonas aeruginosa
brenda
Chuawong, P.; Hendrickson, T.L.
The nondiscriminating aspartyl-tRNA synthetase from Helicobacter pylori: anticodon-binding domain mutations that impact tRNA specificity and heterologous toxicity
Biochemistry
45
8079-8087
2006
Helicobacter pylori
brenda
Namgoong, S.; Sheppard, K.; Sherrer, R.L.; Soell, D.
Co-evolution of the archaeal tRNA-dependent amidotransferase GatCAB with tRNAAsn
FEBS Lett.
581
309-314
2007
Methanothermobacter thermautotrophicus
brenda
Sheppard, K.; Akochy, P.M.; Salazar, J.C.; Soell, D.
The Helicobacter pylori amidotransferase GatCAB is equally efficient in glutamine-dependent transamidation of Asp-tRNAAsn and Glu-tRNAGln
J. Biol. Chem.
282
11866-11873
2007
Helicobacter pylori
brenda
Bernard, D.; Akochy, P.M.; Bernier, S.; Fisette, O.; Brousseau, O.C.; Chenevert, R.; Roy, P.H.; Lapointe, J.
Inhibition by L-aspartol adenylate of a nondiscriminating aspartyl-tRNA synthetase reveals differences between the interactions of its active site with tRNAAsp and tRNAAsn
J. Enzyme Inhib. Med. Chem.
22
77-82
2007
Pseudomonas aeruginosa
brenda
Ramirez, B.L.; Howard, O.M.; Dong, H.F.; Edamatsu, T.; Gao, P.; Hartlein, M.; Kron, M.
Brugia malayi asparaginyl-transfer RNA synthetase induces chemotaxis of human leukocytes and activates G-protein-coupled receptors CXCR1 and CXCR2
J. Infect. Dis.
193
1164-1171
2006
Brugia malayi, Homo sapiens
brenda
Bailly, M.; Blaise, M.; Lorber, B.; Becker, H.D.; Kern, D.
The transamidosome: a dynamic ribonucleoprotein particle dedicated to prokaryotic tRNA-dependent asparagine biosynthesis
Mol. Cell
28
228-239
2007
Thermus thermophilus
brenda
Cardoso, A.M.; Polycarpo, C.; Martins, O.B.; Soell, D.
A non-discriminating aspartyl-tRNA synthetase from Halobacterium salinarum
RNA Biol.
3
110-114
2006
Halobacterium salinarum, Halobacterium salinarum NRC 1
brenda
Crepin, T.; Peterson, F.; Haertlein, M.; Jensen, D.; Wang, C.; Cusack, S.; Kron, M.
A hybrid structural model of the complete Brugia malayi cytoplasmic asparaginyl-tRNA synthetase
J. Mol. Biol.
405
1056-1069
2011
Brugia malayi (A0A0J9Y417)
brenda
Yu, Z.; Vodanovic-Jankovic, S.; Ledeboer, N.; Huang, S.X.; Rajski, S.R.; Kron, M.; Shen, B.
Tirandamycins from Streptomyces sp. 17944 inhibiting the parasite Brugia malayi asparagine tRNA synthetase
Org. Lett.
13
2034-2037
2011
Brugia malayi
brenda
Polydorides, S.; Amara, N.; Aubard, C.; Plateau, P.; Simonson, T.; Archontis, G.
Computational protein design with a generalized born solvent model: application to asparaginyl-tRNA synthetase
Proteins
79
3448-3468
2011
Thermus thermophilus
brenda
Fischer, F.; Huot, J.L.; Lorber, B.; Diss, G.; Hendrickson, T.L.; Becker, H.D.; Lapointe, J.; Kern, D.
The asparagine-transamidosome from Helicobacter pylori: a dual-kinetic mode in non-discriminating aspartyl-tRNA synthetase safeguards the genetic code
Nucleic Acids Res.
40
4965-4976
2012
Helicobacter pylori
brenda
Yu, Z.; Vodanovic-Jankovic, S.; Kron, M.; Shen, B.
New WS9326A congeners from Streptomyces sp. 9078 inhibiting Brugia malayi asparaginyl-tRNA synthetase
Org. Lett.
14
4946-4949
2012
Brugia malayi
brenda
Fuengfuloy, P.; Chuawong, P.; Suebka, S.; Wattana-Amorn, P.; Williams, C.; Crump, M.P.; Songsiriritthigul, C.
Overproduction of the N-terminal anticodon-binding domain of the non-discriminating aspartyl-tRNA synthetase from Helicobacter pylori for crystallization and NMR measurements
Protein Expr. Purif.
89
25-32
2013
no activity in Helicobacter pylori
brenda
Vijayakumar, R.; Tripathi, T.
Soluble expression and purification of a full-length asparaginyl tRNA synthetase from Fasciola gigantica
Protein Expr. Purif.
143
9-13
2018
Fasciola gigantica
brenda