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.
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ATP + Asp + tRNAAsn
AMP + diphosphate + aspartyl-tRNAAsn
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + Asp-tRNAAsn
-
only the enzyme AspRS2 aspartylates tRNAAsn
-
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + aspartyl-tRNAAsn
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsn
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + Asp-tRNAAsp
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + aspartyl-tRNAAsp
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
ATP + L-aspartate + tRNAAsx
AMP + diphosphate + L-aspartyl-tRNAAsx
additional information
?
-
ATP + Asp + tRNAAsn
AMP + diphosphate + aspartyl-tRNAAsn
-
while large amounts pf Asp-tRNAAsn are detrimental to Escherichia coli with trypA34 missense mutation, a smaller amount supports protein synthesis and allows the formation of up to 38% of the wild-type level of missense-suppressed tryptophan synthetase
-
-
?
ATP + Asp + tRNAAsn
AMP + diphosphate + aspartyl-tRNAAsn
-
while large amounts pf Asp-tRNAAsn are detrimental to Escherichia coli with trypA34 missense mutation, a smaller amount supports protein synthesis and allows the formation of up to 38% of the wild-type level of missense-suppressed tryptophan synthetase
-
-
?
ATP + Asp + tRNAAsn
AMP + diphosphate + aspartyl-tRNAAsn
-
while large amounts of Asp-tRNAAsn are detrimental to Escherichia coli with trypA34 missense mutation, a smaller amount supports protein synthesis and allows the formation of up to 38% of the wild-type level of missense-suppressed tryptophan synthetase
-
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + aspartyl-tRNAAsn
reaction via transamidation mechanism
-
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + aspartyl-tRNAAsn
in vivo expressed Halobacterium salinarum tRNAAsn, reaction via transamidation mechanism
-
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + aspartyl-tRNAAsn
reaction via transamidation mechanism
-
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + aspartyl-tRNAAsn
in vivo expressed Halobacterium salinarum tRNAAsn, reaction via transamidation mechanism
-
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + aspartyl-tRNAAsn
-
-
-
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + aspartyl-tRNAAsn
-
recombinantly produced tRNA substrate
-
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + aspartyl-tRNAAsn
-
-
-
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + aspartyl-tRNAAsn
-
-
-
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + aspartyl-tRNAAsn
-
tRNA substrate from Escherichia coli
-
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + aspartyl-tRNAAsn
-
dual activity of the ND-AspRS since an asparaginyl-tRNA synthetase is missing in Sulfolobus tokodaii strain 7
-
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsn
about 20% activity compared to tRNAAsp
-
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsn
about 20% activity compared to tRNAAsp
-
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsn
-
-
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsn
-
-
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsn
-
about 60% activity compared to tRNAAsp
-
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsn
-
aspartyl-tRNA synthetase requires a conserved proline, P77, in the anticodon-binding loop for tRNA(Asn) recognition in vivo. Wild-type enzyme shows a slight preference to tRNAAsn over tRNAAsp
-
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsn
Halalkalibacterium halodurans
about 20% activity compared to tRNAAsp
-
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsn
-
-
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsn
-
-
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsn
-
-
-
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsn
-
the product L-aspartyl-tRNAAsn is transamidated by amidotransferase to form Asn-tRNAAsn. Synthesis of Asn-tRNA via the indirect pathway
-
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsn
-
two residues in the anticodon recognition domain of the aspartyl-tRNA synthetase, H31 and G83, are individually implicated in the recognition of tRNAAsn
-
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsn
-
-
-
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsn
-
-
-
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsn
-
-
-
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsn
-
Thermus thermophilus deprived of asparagine synthetase snthesizes Asn on tRNAAsn via a tRNA-dependent pathway involving a nondiscriminating aspartyl-tRNA synthetase that charges Asp onto tRNAAsn prior to conversion of the Asp to Asn by GatCAB
-
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsn
-
ND-AspRSKtRNAAsn complex and of the transamidosome and mechanism of transamidation, overview. A scaffold tRNAAsn mediates stability and integrity of the complex
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + Asp-tRNAAsp
-
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + Asp-tRNAAsp
-
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + Asp-tRNAAsp
-
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + Asp-tRNAAsp
-
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + aspartyl-tRNAAsp
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + aspartyl-tRNAAsp
in vivo expressed Halobacterium salinarum tRNAAsp
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + aspartyl-tRNAAsp
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + aspartyl-tRNAAsp
-
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + aspartyl-tRNAAsp
-
recombinantly produced tRNA substrate
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + aspartyl-tRNAAsp
-
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + aspartyl-tRNAAsp
-
tRNA substrate from Escherichia coli
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + aspartyl-tRNAAsp
-
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
100% activity
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
100% activity
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
-
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
-
100% activity
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
-
aspartyl-tRNA synthetase requires a conserved proline, P77, in the anticodon-binding loop for tRNA(Asn) recognition in vivo. Wild-type enzyme shows a slight preference to tRNAAsn over tRNAAsp
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
Halalkalibacterium halodurans
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
Halalkalibacterium halodurans
100% activity
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
-
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
-
-
-
-
?
ATP + L-aspartate + tRNAAsx
AMP + diphosphate + L-aspartyl-tRNAAsx
-
preparation of recombinant tRNA substrates from Pseudomonas aeruginosa and Saccharomyces cerevisiae, overview, activity with two variants C36U and C38U of yeast tRNAAsp
-
-
?
ATP + L-aspartate + tRNAAsx
AMP + diphosphate + L-aspartyl-tRNAAsx
-
-
-
-
?
additional information
?
-
the enzyme shows no activity with tRNAGln
-
-
?
additional information
?
-
the enzyme shows no activity with tRNAGln
-
-
?
additional information
?
-
-
the enzyme shows no activity with tRNAGln
-
-
?
additional information
?
-
AspRS must perform two sequential reactions. The first reaction is the formation of aspartyladenylate from the free amino acid and ATP, releasing diphosphate. The second reaction is the displacement of the adenylate moiety by the 3'-OH of the terminal adenosine of the tRNAAsp acceptor arm, yielding the covalently linked Asp-tRNAAsp. The active site must therefore bind the two initial reactants, Asp and ATP, and also provide access for the properly positioned acceptor stem of a bound tRNA molecule
-
-
?
additional information
?
-
Halalkalibacterium halodurans
the enzyme shows no activity with tRNAGln
-
-
?
additional information
?
-
the tRNA-dependent transamidation pathway is the essential route for Asn-tRNAAsn formation in organisms that lack an asparaginyl-tRNA synthetase. This pathway relies on ND-AspRS, an enzyme with relaxed tRNA specificity, to form Asp-tRNAAsn, the misacylated tRNA is then converted to Asn-tRNAAsn by the action of an Asp-tRNAAsn amidotransferase, EC 6.3.5.6
-
-
?
additional information
?
-
-
the tRNA-dependent transamidation pathway is the essential route for Asn-tRNAAsn formation in organisms that lack an asparaginyl-tRNA synthetase. This pathway relies on ND-AspRS, an enzyme with relaxed tRNA specificity, to form Asp-tRNAAsn, the misacylated tRNA is then converted to Asn-tRNAAsn by the action of an Asp-tRNAAsn amidotransferase, EC 6.3.5.6
-
-
?
additional information
?
-
the Halobacterium salinarum enzyme is unable to use Escherichia coli tRNA as substrate
-
-
?
additional information
?
-
-
the Halobacterium salinarum enzyme is unable to use Escherichia coli tRNA as substrate
-
-
?
additional information
?
-
the tRNA-dependent transamidation pathway is the essential route for Asn-tRNAAsn formation in organisms that lack an asparaginyl-tRNA synthetase. This pathway relies on ND-AspRS, an enzyme with relaxed tRNA specificity, to form Asp-tRNAAsn, the misacylated tRNA is then converted to Asn-tRNAAsn by the action of an Asp-tRNAAsn amidotransferase, EC 6.3.5.6
-
-
?
additional information
?
-
the Halobacterium salinarum enzyme is unable to use Escherichia coli tRNA as substrate
-
-
?
additional information
?
-
-
in bacteria that lack AsnRS, AspRS is nondiscriminating 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, EC 6.3.5.6, increasing tRNAAsp specificity in an ND-AspRS diminishes in vivo toxicity
-
-
?
additional information
?
-
-
tRNA anticodon binding site structures, overview, Helicobacter pylori AspRS is a nondiscriminating enzyme that aminoacylates both tRNAAsp and tRNAAsn, ND-AspRS is 1.7times more efficient at aminoacylating tRNAAsp over tRNAAsn
-
-
?
additional information
?
-
-
mutations in the DARS2 gene lead to Leukoencephalopathy with brainstem and spinal cord involvement and lactate elevation as a disorder with an autosomal recessive mode of inheritance, the phenotype includes cerebellar, pyramidal and dorsal column dysfunctions, overview
-
-
?
additional information
?
-
-
two residues in the anticodon recognition domain of the enzyme are individually implicated in the recognition of tRNAAsn, nondiscriminating AspRSs possess a histidine at position 31 and usually a glycine at position 83, whereas discriminating AspRSs, EC 6.1.1.12, possess a leucine at position 31 and a residue other than a glycine at position 83
-
-
?
additional information
?
-
-
the enzyme is downregulated at the post-transcriptional level in a complex retro-inhibition mechanism, the cell equilibrates cellular concentrations of tRNAAsp, AspRS, and its encoding mRNA to hinder AspRS accumulation and avoid misacylation of heterologous tRNAs, proteomic analysis, overview
-
-
?
additional information
?
-
-
the purified protein has the ability to catalyze the aspartylation of hydroxylamine through an aspartyl-AMP intermediate
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + Asp + tRNAAsn
AMP + diphosphate + aspartyl-tRNAAsn
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + aspartyl-tRNAAsn
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsn
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + Asp-tRNAAsp
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + aspartyl-tRNAAsp
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
ATP + L-aspartate + tRNAAsx
AMP + diphosphate + L-aspartyl-tRNAAsx
-
-
-
-
?
additional information
?
-
ATP + Asp + tRNAAsn
AMP + diphosphate + aspartyl-tRNAAsn
-
while large amounts pf Asp-tRNAAsn are detrimental to Escherichia coli with trypA34 missense mutation, a smaller amount supports protein synthesis and allows the formation of up to 38% of the wild-type level of missense-suppressed tryptophan synthetase
-
-
?
ATP + Asp + tRNAAsn
AMP + diphosphate + aspartyl-tRNAAsn
-
while large amounts pf Asp-tRNAAsn are detrimental to Escherichia coli with trypA34 missense mutation, a smaller amount supports protein synthesis and allows the formation of up to 38% of the wild-type level of missense-suppressed tryptophan synthetase
-
-
?
ATP + Asp + tRNAAsn
AMP + diphosphate + aspartyl-tRNAAsn
-
while large amounts of Asp-tRNAAsn are detrimental to Escherichia coli with trypA34 missense mutation, a smaller amount supports protein synthesis and allows the formation of up to 38% of the wild-type level of missense-suppressed tryptophan synthetase
-
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + aspartyl-tRNAAsn
reaction via transamidation mechanism
-
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + aspartyl-tRNAAsn
reaction via transamidation mechanism
-
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + aspartyl-tRNAAsn
-
-
-
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + aspartyl-tRNAAsn
-
-
-
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + aspartyl-tRNAAsn
-
-
-
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + aspartyl-tRNAAsn
-
dual activity of the ND-AspRS since an asparaginyl-tRNA synthetase is missing in Sulfolobus tokodaii strain 7
-
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsn
-
-
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsn
-
-
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsn
-
-
-
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsn
-
the product L-aspartyl-tRNAAsn is transamidated by amidotransferase to form Asn-tRNAAsn. Synthesis of Asn-tRNA via the indirect pathway
-
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsn
-
-
-
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsn
-
Thermus thermophilus deprived of asparagine synthetase snthesizes Asn on tRNAAsn via a tRNA-dependent pathway involving a nondiscriminating aspartyl-tRNA synthetase that charges Asp onto tRNAAsn prior to conversion of the Asp to Asn by GatCAB
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + Asp-tRNAAsp
-
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + Asp-tRNAAsp
-
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + Asp-tRNAAsp
-
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + Asp-tRNAAsp
-
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + aspartyl-tRNAAsp
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + aspartyl-tRNAAsp
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + aspartyl-tRNAAsp
-
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + aspartyl-tRNAAsp
-
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + aspartyl-tRNAAsp
-
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
-
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
Halalkalibacterium halodurans
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
-
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
-
-
-
-
?
additional information
?
-
AspRS must perform two sequential reactions. The first reaction is the formation of aspartyladenylate from the free amino acid and ATP, releasing diphosphate. The second reaction is the displacement of the adenylate moiety by the 3'-OH of the terminal adenosine of the tRNAAsp acceptor arm, yielding the covalently linked Asp-tRNAAsp. The active site must therefore bind the two initial reactants, Asp and ATP, and also provide access for the properly positioned acceptor stem of a bound tRNA molecule
-
-
?
additional information
?
-
the tRNA-dependent transamidation pathway is the essential route for Asn-tRNAAsn formation in organisms that lack an asparaginyl-tRNA synthetase. This pathway relies on ND-AspRS, an enzyme with relaxed tRNA specificity, to form Asp-tRNAAsn, the misacylated tRNA is then converted to Asn-tRNAAsn by the action of an Asp-tRNAAsn amidotransferase, EC 6.3.5.6
-
-
?
additional information
?
-
-
the tRNA-dependent transamidation pathway is the essential route for Asn-tRNAAsn formation in organisms that lack an asparaginyl-tRNA synthetase. This pathway relies on ND-AspRS, an enzyme with relaxed tRNA specificity, to form Asp-tRNAAsn, the misacylated tRNA is then converted to Asn-tRNAAsn by the action of an Asp-tRNAAsn amidotransferase, EC 6.3.5.6
-
-
?
additional information
?
-
the tRNA-dependent transamidation pathway is the essential route for Asn-tRNAAsn formation in organisms that lack an asparaginyl-tRNA synthetase. This pathway relies on ND-AspRS, an enzyme with relaxed tRNA specificity, to form Asp-tRNAAsn, the misacylated tRNA is then converted to Asn-tRNAAsn by the action of an Asp-tRNAAsn amidotransferase, EC 6.3.5.6
-
-
?
additional information
?
-
-
in bacteria that lack AsnRS, AspRS is nondiscriminating 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, EC 6.3.5.6, increasing tRNAAsp specificity in an ND-AspRS diminishes in vivo toxicity
-
-
?
additional information
?
-
-
mutations in the DARS2 gene lead to Leukoencephalopathy with brainstem and spinal cord involvement and lactate elevation as a disorder with an autosomal recessive mode of inheritance, the phenotype includes cerebellar, pyramidal and dorsal column dysfunctions, overview
-
-
?
additional information
?
-
-
the enzyme is downregulated at the post-transcriptional level in a complex retro-inhibition mechanism, the cell equilibrates cellular concentrations of tRNAAsp, AspRS, and its encoding mRNA to hinder AspRS accumulation and avoid misacylation of heterologous tRNAs, proteomic analysis, overview
-
-
?
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.
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.
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.
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.
H28Q
-
wild-type enzyme shows a slight preference to tRNAAsn over tRNAAsp. Mutation H28Q leads to a reverse tRNA preference
H77K/H28Q
-
wild-type enzyme shows a slight preference to tRNAAsn over tRNAAsp. Mutation P77K/H28Q leads to a reverse tRNA preference
P77K
-
wild-type enzyme shows a slight preference to tRNAAsn over tRNAAsp. Mutation P77K leads to a reverse tRNA preference and a 3fold increase in specificity for tRNAASp over tRNAAsn
H26A
site-directed mutagenesis, mutation the amino acid located in the AspRS anticodon binding domain limits the specificity of this nondiscriminating enzyme towards tRNAAsn, altered tRNA substrate specificity compared to the wild-type enzyme, overview
H26A/P84A
site-directed mutagenesis, mutation the amino acid located in the AspRS anticodon binding domain limits the specificity of this nondiscriminating enzyme towards tRNAAsn, altered tRNA substrate specificity compared to the wild-type enzyme, overview
H26A/P84K
site-directed mutagenesis, mutation the amino acid located in the AspRS anticodon binding domain limits the specificity of this nondiscriminating enzyme towards tRNAAsn, altered tRNA substrate specificity compared to the wild-type enzyme, overview
H26Q
site-directed mutagenesis, mutation the amino acid located in the AspRS anticodon binding domain limits the specificity of this nondiscriminating enzyme towards tRNAAsn, altered tRNA substrate specificity compared to the wild-type enzyme, overview
H26Q/P84A
site-directed mutagenesis, mutation the amino acid located in the AspRS anticodon binding domain limits the specificity of this nondiscriminating enzyme towards tRNAAsn, altered tRNA substrate specificity compared to the wild-type enzyme, overview
H26Q/P84K
site-directed mutagenesis, mutation the amino acid located in the AspRS anticodon binding domain limits the specificity of this nondiscriminating enzyme towards tRNAAsn, altered tRNA substrate specificity compared to the wild-type enzyme, overview
P84A
site-directed mutagenesis, mutation the amino acid located in the AspRS anticodon binding domain limits the specificity of this nondiscriminating enzyme towards tRNAAsn, altered tRNA substrate specificity compared to the wild-type enzyme, overview
P84K
site-directed mutagenesis, mutation the amino acid located in the AspRS anticodon binding domain limits the specificity of this nondiscriminating enzyme towards tRNAAsn, altered tRNA substrate specificity compared to the wild-type enzyme, overview
H26A
-
site-directed mutagenesis, mutation the amino acid located in the AspRS anticodon binding domain limits the specificity of this nondiscriminating enzyme towards tRNAAsn, altered tRNA substrate specificity compared to the wild-type enzyme, overview
-
H26Q
-
site-directed mutagenesis, mutation the amino acid located in the AspRS anticodon binding domain limits the specificity of this nondiscriminating enzyme towards tRNAAsn, altered tRNA substrate specificity compared to the wild-type enzyme, overview
-
H26Q/P84A
-
site-directed mutagenesis, mutation the amino acid located in the AspRS anticodon binding domain limits the specificity of this nondiscriminating enzyme towards tRNAAsn, altered tRNA substrate specificity compared to the wild-type enzyme, overview
-
P84A
-
site-directed mutagenesis, mutation the amino acid located in the AspRS anticodon binding domain limits the specificity of this nondiscriminating enzyme towards tRNAAsn, altered tRNA substrate specificity compared to the wild-type enzyme, overview
-
P84K
-
site-directed mutagenesis, mutation the amino acid located in the AspRS anticodon binding domain limits the specificity of this nondiscriminating enzyme towards tRNAAsn, altered tRNA substrate specificity compared to the wild-type enzyme, overview
-
L81N
-
site-directed mutagenesis, the mutation in the anticodon binding domain doubles the kcat for tRNAAsn as compared to the wild-type enzyme
L81N/L86M
-
site-directed mutagenesis, the mutation in the anticodon binding domain alters the tRNA specificity as compared to the wild-type enzyme, the L81N/L86M mutant does not follow Michaelis-Menten kinetics
L86M
-
site-directed mutagenesis, the mutation in the anticodon binding domain alters the tRNA specificity as compared to the wild-type enzyme
R485K
-
a catalytic site mutant
G83K
-
aspartylation reaction of the mutant enzyme is 55% as fast as the wild-type enzyme
G83K
-
site-directed mutagenesis, the mutation increases the specificity of tRNAAsp charging over that of tRNAAsn by 4.2fold
H31L
-
aspartylation reaction of the mutant enzyme is 84% as fast as the wild-type enzyme
H31L
-
aspartylation reaction of the mutant enzyme is 92% as fast as the wild-type enzyme
H31L
-
site-directed mutagenesis, the mutation increases the specificity of tRNAAsp charging over that of tRNAAsn by 3.5fold
additional information
-
mutations in the anticodon binding domain of Helicobacter pylori ND-AspRS, e.g. at L81, L86, N82, and M87, reduce this enzymes ability to misacylate tRNAAsn and enhance tRNAAsp specificity, in a manner that correlates with the toxicity of the enzyme in Escherichia coli, overview
additional information
-
naturylla occuring gene DARS2 mutant phenotype, overview
additional information
-
AspRS overexpression leads deprivation of the gene's 5'-untranslated region, that is essential for directing mRNA recognition by the protein and initiating the retro-inhibition process, but does not lead to increased tRNAAsn and/or tRNAGlu misaspartylation or the logical consecutive post-translational stress
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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
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12838-12843
1998
Deinococcus radiodurans
brenda
Schmitt, E.; Moulinier, L.; Fujiwara, S.; Imanaka, T.; Thierry, J.C.; Moras, D.
Crystal structure of aspartyl-tRNA synthetase from Pyrococcus kodakaraensis KOD: archaeon specificity and catalytic mechanism of adenylate formation
EMBO J.
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Thermococcus kodakarensis
brenda
Becker, H.D.; Roy, H.; Moulinier, L.; Mazauric, M.H.; Keith, G.; Kern, D.
Thermus thermophilus contains an eubacterial and an archaebacterial aspartyl-tRNA synthetase
Biochemistry
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Thermus thermophilus
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
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Methanothermobacter thermautotrophicus (O26328), Methanothermobacter thermautotrophicus, Methanothermobacter thermautotrophicus DSM 1053 (O26328)
brenda
Min, B.; Kitabatake, M.; Polycarpo, C.; Pelaschier, J.; Raczniak, G.; Ruan, B.; Kobayashi, H.; Namgoong, S.; Soll, D.
Protein synthesis in Escherichia coli with mischarged tRNA
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2003
Chlamydia trachomatis, Deinococcus radiodurans, Halobacterium salinarum
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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.
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2004
Pseudomonas aeruginosa
brenda
Bernard, D.; Akochy, P.M.; Beaulieu, D.; Lapointe, J.; Roy, P.H.
Two residues in the anticodon recognition domain of the aspartyl-tRNA synthetase from Pseudomonas aeruginosa are individually implicated in the recognition of tRNAAsn
J. Bacteriol.
188
269-274
2006
Pseudomonas aeruginosa
brenda
Feng, L.; Yuan, J.; Toogood, H.; Tumbula-Hansen, D.; Soll, D.
Aspartyl-tRNA synthetase requires a conserved proline in the anticodon-binding loop for tRNA(Asn) recognition in vivo
J. Biol. Chem.
280
20638-20641
2005
Deinococcus radiodurans
brenda
Sato, Y.; Maeda, Y.; Shimizu, S.; Hossain, M.T.; Ubukata, S.; Suzuki, K.; Sekiguchi, T.; Takenaka, A.
Structure of the nondiscriminating aspartyl-tRNA synthetase from the crenarchaeon Sulfolobus tokodaii strain 7 reveals the recognition mechanism for two different tRNA anticodons
Acta Crystallogr. Sect. D
63
1042-1047
2007
no activity in Sulfolobus tokodaii, Sulfurisphaera tokodaii, no activity in Sulfolobus tokodaii 7
brenda
Suzuki, K.; Sato, Y.; Maeda, Y.; Shimizu, S.; Hossain, M.T.; Ubukata, S.; Sekiguchi, T.; Takenaka, A.
Crystallization and preliminary X-ray crystallographic study of a putative aspartyl-tRNA synthetase from the crenarchaeon Sulfolobus tokodaii strain 7
Acta Crystallogr. Sect. F
63
608-612
2007
no activity in Sulfolobus tokodaii, no activity in Sulfolobus tokodaii 7, Sulfurisphaera tokodaii
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
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
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 (O07683), Halobacterium salinarum, Halobacterium salinarum NRC 1 (O07683)
brenda
Kazakov, T.; Vondenhoff, G.H.; Datsenko, K.A.; Novikova, M.; Metlitskaya, A.; Wanner, B.L.; Severinov, K.
Escherichia coli peptidase A, B, or N can process translation inhibitor microcin C
J. Bacteriol.
190
2607-2610
2008
Escherichia coli
brenda
Uluc, K.; Baskan, O.; Yildirim, K.A.; Ozsahin, S.; Koseoglu, M.; Isak, B.; Scheper, G.C.; Gunal, D.I.; van der Knaap, M.S.
Leukoencephalopathy with brain stem and spinal cord involvement and high lactate: a genetically proven case with distinct MRI findings
J. Neurol. Sci.
273
118-122
2008
Homo sapiens
brenda
Ryckelynck, M.; A Paulus, C.; Frugier, M.
Post-translational modifications guard yeast from misaspartylation
Biochemistry
47
12476-12482
2008
Saccharomyces cerevisiae
brenda
Bailly, M.; Blaise, M.; Lorber, B.; Thirup, S.; Kern, D.
Isolation, crystallization and preliminary X-ray analysis of the transamidosome, a ribonucleoprotein involved in asparagine formation
Acta Crystallogr. Sect. F
65
577-581
2009
Thermus thermophilus
brenda
Merritt, E.A.; Arakaki, T.L.; Larson, E.T.; Kelley, A.; Mueller, N.; Napuli, A.J.; Zhang, L.; Deditta, G.; Luft, J.; Verlinde, C.L.; Fan, E.; Zucker, F.; Buckner, F.S.; Van Voorhis, W.C.; Hol, W.G.
Crystal structure of the aspartyl-tRNA synthetase from Entamoeba histolytica
Mol. Biochem. Parasitol.
169
95-100
2010
Entamoeba histolytica (C4LZN0)
brenda
Blaise, M.; Bailly, M.; Frechin, M.; Behrens, M.A.; Fischer, F.; Oliveira, C.L.; Becker, H.D.; Pedersen, J.S.; Thirup, S.; Kern, D.
Crystal structure of a transfer-ribonucleoprotein particle that promotes asparagine formation
EMBO J.
29
3118-3129
2010
Thermus thermophilus
brenda
Akochy, P.M.; Lapointe, J.; Roy, P.H.
Natural insertion of the bro-1 beta-lactamase gene into the gatCAB operon affects Moraxella catarrhalis aspartyl-tRNA(Asn) amidotransferase activity
Microbiology
158
2363-2371
2012
Moraxella catarrhalis
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
Helicobacter pylori
brenda
Mladenova, S.R.; Stein, K.R.; Bartlett, L.; Sheppard, K.
Relaxed tRNA specificity of the Staphylococcus aureus aspartyl-tRNA synthetase enables RNA-dependent asparagine biosynthesis
FEBS Lett.
588
1808-1812
2014
Staphylococcus aureus, Staphylococcus aureus FPR3757
brenda
Nair, N.; Raff, H.; Islam, M.T.; Feen, M.; Garofalo, D.M.; Sheppard, K.
The Bacillus subtilis and Bacillus halodurans aspartyl-tRNA synthetases retain recognition of tRNAAsn
J. Mol. Biol.
428
618-630
2016
Borreliella burgdorferi, Bacillus subtilis (O32038), Halalkalibacterium halodurans (Q9KDG1), Bacillus subtilis 168 (O32038)
brenda
Alperstein, A.; Ulrich, B.; Garofalo, D.M.; Dreisbach, R.; Raff, H.; Sheppard, K.
The predatory bacterium Bdellovibrio bacteriovorus aspartyl-tRNA synthetase recognizes tRNAAsn as a substrate
PLoS ONE
9
e110842
2014
Bdellovibrio bacteriovorus (Q6MI59), Bdellovibrio bacteriovorus HD100 (Q6MI59)
brenda
Suzuki, T.; Nakamura, A.; Kato, K.; Sll, D.; Tanaka, I.; Sheppard, K.; Yao, M.
Structure of the Pseudomonas aeruginosa transamidosome reveals unique aspects of bacterial tRNA-dependent asparagine biosynthesis
Proc. Natl. Acad. Sci. USA
112
382-387
2015
Pseudomonas aeruginosa
brenda