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ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsn
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + aspartyl-tRNAAsp
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
additional information
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ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsn
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ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsn
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the archaeal AspRS enzyme is nondiscriminating, which means that it forms Asp-tRNAAsp and Asp-tRNAAsn, which is the intermediate in AsntRNAAsn generation by ASp-tRNAAsn amidotransferase, in contrary bacterial enzymes are discriminating ones
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ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsn
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the archaeal AspRS2 enzyme is discriminating, which means that it forms only Asp-tRNAAsp and not Asp-tRNAAsn, the L1 loop exchange mutant is rendered non-dicriminating
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ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsn
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the archaeal AspRS2 enzyme is nondiscriminating, which means that it forms Asp-tRNAAsp and Asp-tRNAAsn
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ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsn
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non-discriminating AspRS2
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ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsn
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non-discriminating AspRS2
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ATP + L-aspartate + tRNAAsp
AMP + diphosphate + aspartyl-tRNAAsp
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ATP + L-aspartate + tRNAAsp
AMP + diphosphate + aspartyl-tRNAAsp
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ATP + L-aspartate + tRNAAsp
AMP + diphosphate + aspartyl-tRNAAsp
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ATP + L-aspartate + tRNAAsp
AMP + diphosphate + aspartyl-tRNAAsp
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enzyme deficiency or mutation is involved in development of autosomal recessive disease leukoencephalopathy with brain stem and spinal cord involvement and lactate elevation, i.e. LBSL, often manifesting in early childhood, overview
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ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
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ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
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ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
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ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
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ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
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ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
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ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
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ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
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protein-RNA recognition between the enzyme and tRNA is highly specific and essential for cell viability
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ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
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specific amino acid binding by the enzyme is required for correct translation of the genetic code
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ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
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ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
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ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
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ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
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ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
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ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
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ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
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ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
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ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
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ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
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ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
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ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
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ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
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ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
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ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
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ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
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ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
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ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
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ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
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ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
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ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
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ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
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ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
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ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
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ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
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ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
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specific amino acid binding by the enzyme is required for correct translation of the genetic code
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ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
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the yeast AspRS not only binds and aminoacylates tRNAAsp but also binds its yeast mRNA and initiates retro-inhibition of its expression, overview
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ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
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ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
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ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
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ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
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ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
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ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
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ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
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ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
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ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
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ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
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ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
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specific amino acid binding by the enzyme is required for correct translation of the genetic code
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?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
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ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
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ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
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additional information
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no acylation with L-aspartate of tRNAAsn, enzyme is discriminating, because it forms Asn-tRNAAsn by direct aminoacylation, not via the intermediate of Asp-tRNAAsn, and it contains no Asp-tRNAAsn amidotransferase
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additional information
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the N-terminal extension of the enzyme is involved in the transfer of Asp-tRNAAsp to elongation factor alpha1, the structural switch model supports the direct transfer mechanism
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additional information
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AspRS mediates stimulation of lysyl-tRNA synthetase, KRShe, with 40% stimulation when eight fold excess of AspRS is present. The non-synthetase protein from the multi-synthetase complex p38 inhibits the AspRS-mediated stimulation
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additional information
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mutations in the DARS2 gene cause the autosomal recessive disorder leukoencephalopathy with brainstem and spinal cord involvement and lactate elevation, overview
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additional information
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the enzyme also binds to its mRNA via its N-terminal extension of 70 amino acid residues and the anticodon-binding module, which has a regulatory function on the expression of the enzyme
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additional information
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misaspartylation of tRNAAsn and tRNAGlu does not exist in vivo
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additional information
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no acylation with L-aspartate of tRNAAsn, enzyme is discriminating, because it forms Asn-tRNAAsn by direct aminoacylation, not via the intermediate of Asp-tRNAAsn, and it contains no Asp-tRNAAsn amidotransferase
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additional information
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no acylation with L-aspartate of tRNAAsn, enzyme is discriminating, because it forms Asn-tRNAAsn by direct aminoacylation, not via the intermediate of Asp-tRNAAsn, and it contains no Asp-tRNAAsn amidotransferase
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additional information
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aspartyl- and asparaginyl-tRNA synthetases have evolved relatively recently from a comon ancestor
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additional information
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in Thermus thermophilus Asn-tRNAAsn is formed indirectly via a two-step pathway whereby tRNAAsn is mischarged with Asp that will subsequently be amidated into Asn by an amidotransferase.The non-discriminating aspartyl-tRNA synthetase, the trimeric GatCAB tRNA-dependent amidotransferase and the tRNAAsn promoting this pathway assemble into a ribonucleoprotein particle termed transamidosome, analysis of the mechanism of Asn-tRNAAsn formation by the transamidosome, overview
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additional information
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in Thermus thermophilus Asn-tRNAAsn is formed indirectly via a two-step pathway whereby tRNAAsn is mischarged with Asp that will subsequently be amidated into Asn by an amidotransferase.The non-discriminating aspartyl-tRNA synthetase, the trimeric GatCAB tRNA-dependent amidotransferase and the tRNAAsn promoting this pathway assemble into a ribonucleoprotein particle termed transamidosome, analysis of the mechanism of Asn-tRNAAsn formation by the transamidosome, overview
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