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adenosine 5-[beta,gamma-imido]-triphosphate + L-Asp
AMP-Asp + imidodiphosphate
AMP-Asp + diphosphate
ATP + L-Asp
ATP + 2-aminomalonic acid + tRNAAsp
?
-
-
-
-
?
ATP + Asp + tRNAAsn
AMP + diphosphate + aspartyl-tRNAAsn
discriminating AspRS gains the ability to form Asp-tRNAAsn in vitro when the W26H or K85P changes are introduced independently or in combination
-
-
?
ATP + Asp + tRNAAsp
AMP + diphosphate + aspartyl-tRNAAsp
-
-
-
?
ATP + D-aspartate + tRNAAsp
AMP + diphosphate + D-aspartyl-tRNAAsp
aspartyl-tRNA synthetase can misacylate tRNAAsp with D-aspartate instead of its usual substrate, L-Asp, substrate specificity and molecular dynamics simulations, overview
-
-
?
ATP + L-Asp + tRNAAsp
AMP + diphosphate + aspartyl-tRNAAsp
-
low reaction with mutant tRNAAsp with A instead of G at position 73 (tRNAAspA73)
-
-
?
ATP + L-asparagine + tRNAAsp
AMP + diphosphate + L-asparaginyl-tRNAAsp
-
-
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsn
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsp
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + aspartyl-tRNAAsp
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
ATP + L-aspartate + tRNAAspA73
AMP + diphosphate + L-aspartyl-tRNAAspA73
-
-
-
-
?
ATP + threo-3-hydroxyaspartic acid + tRNAAsp
?
-
-
-
-
?
GTP + L-aspartate + tRNAAsp
GMP + diphosphate + L-aspartyl-tRNAAsp
UTP + L-aspartate + tRNAAsp
UMP + diphosphate + L-aspartyl-tRNAAsp
additional information
?
-
adenosine 5-[beta,gamma-imido]-triphosphate + L-Asp
AMP-Asp + imidodiphosphate
-
-
-
?
adenosine 5-[beta,gamma-imido]-triphosphate + L-Asp
AMP-Asp + imidodiphosphate
-
-
-
?
AMP-Asp + diphosphate
ATP + L-Asp
-
-
-
?
AMP-Asp + diphosphate
ATP + L-Asp
-
-
-
?
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 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
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsn
-
-
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsn
-
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
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsn
wild-type enzyme shows no activity with tRNAAsn. Mutant enzymes W26H, K85P and W26H/K85P are active with tRNAAsn
-
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsn
-
-
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsn
-
the archaeal AspRS2 enzyme is nondiscriminating, which means that it forms Asp-tRNAAsp and Asp-tRNAAsn
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsn
-
non-discriminating AspRS2
-
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsn
-
non-discriminating AspRS2, recombinantly produced tRNAAsn
-
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsn
-
non-discriminating AspRS2
-
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsp
about half as effective as tRNAAsp
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsp
about have as effective as tRNAAsp
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsp
about half as effective as tRNAAsp
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsp
about have as effective as 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
-
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
-
-
?
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
-
-
-
?
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
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
-
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
-
conformational changes and conformational stability upon tRNA and adenylate binding
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
-
wild-type Escherichia coli tRNAAsp and some recombinant acceptor stem mutants from Saccharomyces cerevisiae, overview
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
-
protein-RNA recognition between the enzyme and tRNA is highly specific and essential for cell viability
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
-
specific amino acid binding by the enzyme is required for correct translation of the genetic code
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
aspartyl-tRNA synthetase can misacylate tRNAAsp with D-aspartate instead of its usual substrate, L-Asp, substrate specificity and molecular dynamics simulations, overview
-
-
?
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
-
no activity with tRNAAsn
-
-
?
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
-
-
-
?
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
-
-
-
-
?
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
-
-
-
?
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
-
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 + 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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
specificty of tRNA recognition by the enzyme is primarily ensured by the tRNA identity determinants, the discriminator base G37, four bases in the anticodon loop G34, U35, C36, and C38, and G10-U25 base pair in the core region of the tRNA, substrate specificity of wild-type and truncated mutant enzymes, overview
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
tRNA undergoes large conformational changes upon binding to the enzyme, specific charging of amino acid resdiue on tRNA, accurate recognition by the enzyme is achieved through sequence and structural signalling
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
-
specific amino acid binding by the enzyme is required for correct translation of the genetic code
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
the N-terminal extension of each AspRS subunit plays a crucial role in anchoring the tRNA-like motifs of the mRNA on the synthetase
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
-
the yeast AspRS not only binds and aminoacylates tRNAAsp but also binds its yeast mRNA and initiates retro-inhibition of its expression, overview
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
-
the yeast enzyme also binds its own mRNA and autoinhibits itself
-
-
?
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
-
-
-
-
?
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
no activity with tRNAAsn
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
wild-type enzyme shows no activity with tRNAAsn
-
-
?
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
-
-
-
?
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
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
Thermus thermophilus or Escherichia coli tRNA
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
Thermus thermophilus or Eschrichia coli tRNA
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
-
specific amino acid binding by the enzyme is required for correct translation of the genetic code
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
-
discriminating AspRS1 and non-discriminating AspRS2
-
-
?
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
-
discriminating AspRS1 and non-discriminating AspRS2
-
-
?
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
Thermus thermophilus or Escherichia coli tRNA
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
Thermus thermophilus or Eschrichia coli tRNA
-
?
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
-
-
-
?
GTP + L-aspartate + tRNAAsp
GMP + diphosphate + L-aspartyl-tRNAAsp
-
-
-
-
?
GTP + L-aspartate + tRNAAsp
GMP + diphosphate + L-aspartyl-tRNAAsp
-
-
-
-
?
GTP + L-aspartate + tRNAAsp
GMP + diphosphate + L-aspartyl-tRNAAsp
-
-
-
?
UTP + L-aspartate + tRNAAsp
UMP + diphosphate + L-aspartyl-tRNAAsp
-
-
-
-
?
UTP + L-aspartate + tRNAAsp
UMP + diphosphate + L-aspartyl-tRNAAsp
-
-
-
-
?
UTP + L-aspartate + tRNAAsp
UMP + diphosphate + L-aspartyl-tRNAAsp
-
-
-
?
additional information
?
-
-
determination of binding free energies
-
?
additional information
?
-
-
erroneous binding of Asn by the enzyme is highly improbable, determination of binding energy
-
?
additional information
?
-
-
no activity with wild-type tRNAAsp and several acceptor stem mutants from Saccharomyces cerevisiae, overview
-
?
additional information
?
-
-
no transfer of lysine on tRNAAsp
-
-
?
additional information
?
-
the co-substrate ATP binds preferentially with three associated Mg2+ cations in an unusual, bent geometry, the Mg2+ cations play a structural role and also participate catalytically in the enzyme reaction, co-binding of the ATP-Mg3+ complex increases the Asp/Asn binding free energy difference, indicating that amino acid discrimination is substrate-assisted, molecular dynamics simulations, overview
-
-
?
additional information
?
-
-
ATP-diphosphate exchange activity of wild-type and mutant enzymes in the presence of Asp or Asn, overview
-
-
?
additional information
?
-
-
no acylation with L-aspartate of tRNAAsn
-
?
additional information
?
-
-
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
-
?
additional information
?
-
-
in vitro transcription-translation activity and inhibition by Microcystin C, overview
-
-
?
additional information
?
-
-
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
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
mutations in the DARS2 gene cause the autosomal recessive disorder leukoencephalopathy with brainstem and spinal cord involvement and lactate elevation, overview
-
-
?
additional information
?
-
-
the enzyme shows no activity with tRNAAsn and tRNAGln
-
-
?
additional information
?
-
-
activity of tRNAAsp mimics
-
?
additional information
?
-
-
erroneous binding of Asn by the enzyme is highly improbable, determination of binding energy
-
?
additional information
?
-
-
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
-
?
additional information
?
-
-
misaspartylation of tRNAAsn and tRNAGlu does not exist in vivo
-
-
?
additional information
?
-
-
increased concentrations of AspRS lead to the accumulation of significant amounts of Asp-tRNAAsn and Asp-tRNAGlu in vitro, but not in vivo. The enzyme does not perform autoaspartylation
-
-
?
additional information
?
-
no acylation with L-aspartate of tRNAAsn
-
?
additional information
?
-
-
no acylation with L-aspartate of tRNAAsn
-
?
additional information
?
-
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
-
?
additional information
?
-
-
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
-
?
additional information
?
-
-
aspartate-dependent ATP-diphosphate exchange
-
-
?
additional information
?
-
-
erroneous binding of Asn by the enzyme is highly improbable, determination of binding energy
-
?
additional information
?
-
-
aspartyl- and asparaginyl-tRNA synthetases have evolved relatively recently from a comon ancestor
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
Thermus thermophilus contains two AspRSs: the discriminating AspRS1 which aspartylates only tRNAAsp and the non-discriminating AspRS2 which aspartylates tRNAAsn as efficiently as tRNAAsp
-
-
?
additional information
?
-
-
aspartate-dependent ATP-diphosphate exchange
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
Thermus thermophilus contains two AspRSs: the discriminating AspRS1 which aspartylates only tRNAAsp and the non-discriminating AspRS2 which aspartylates tRNAAsn as efficiently as tRNAAsp
-
-
?
additional information
?
-
-
enzyme can also utilize 2-aminomalonic acid and threo-3-hydroxyaspartic acid in ATP-diphosphate exchange
-
-
?
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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
?
-
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsn
-
-
-
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsn
-
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
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsn
-
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
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsn
-
the archaeal AspRS2 enzyme is nondiscriminating, which means that it forms Asp-tRNAAsp and Asp-tRNAAsn
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsn
-
non-discriminating AspRS2
-
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsn
-
non-discriminating AspRS2
-
-
?
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
-
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
-
-
?
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
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
-
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
-
protein-RNA recognition between the enzyme and tRNA is highly specific and essential for cell viability
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
-
specific amino acid binding by the enzyme is required for correct translation of the genetic code
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
?
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
-
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
-
specific amino acid binding by the enzyme is required for correct translation of the genetic code
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
-
the yeast AspRS not only binds and aminoacylates tRNAAsp but also binds its yeast mRNA and initiates retro-inhibition of its expression, overview
-
-
?
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
-
-
-
?
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
-
specific amino acid binding by the enzyme is required for correct translation of the genetic code
-
?
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
?
-
-
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
-
?
additional information
?
-
-
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
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
mutations in the DARS2 gene cause the autosomal recessive disorder leukoencephalopathy with brainstem and spinal cord involvement and lactate elevation, overview
-
-
?
additional information
?
-
-
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
-
?
additional information
?
-
-
misaspartylation of tRNAAsn and tRNAGlu does not exist in vivo
-
-
?
additional information
?
-
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
-
?
additional information
?
-
-
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
-
?
additional information
?
-
-
aspartyl- and asparaginyl-tRNA synthetases have evolved relatively recently from a comon ancestor
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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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Apnea
Provocation of aspiration reflexes and their effects on the pattern of cough and reflex apnea in cats.
arginine-trna ligase deficiency
Phenotypes and genotypes of mitochondrial aminoacyl-tRNA synthetase deficiencies from a single neurometabolic clinic.
aspartate-trna ligase deficiency
DARS2 protects against neuroinflammation and apoptotic neuronal loss, but is dispensable for myelin producing cells.
aspartate-trna ligase deficiency
Loss of CLPP alleviates mitochondrial cardiomyopathy without affecting the mammalian UPRmt.
aspartate-trna ligase deficiency
Mitochondrial aspartyl-tRNA synthetase deficiency causes leukoencephalopathy with brain stem and spinal cord involvement and lactate elevation.
aspartate-trna ligase deficiency
Phenotypes and genotypes of mitochondrial aminoacyl-tRNA synthetase deficiencies from a single neurometabolic clinic.
Ataxia
Acetazolamide-responsive exercise-induced episodic ataxia associated with a novel homozygous DARS2 mutation.
Ataxia
DARS2 protects against neuroinflammation and apoptotic neuronal loss, but is dispensable for myelin producing cells.
Ataxia
Next generation sequencing for molecular diagnosis of neurological disorders using ataxias as a model.
Carcinogenesis
Upregulation of DARS2 by HBV promotes hepatocarcinogenesis through the miR-30e-5p/MAPK/NFAT5 pathway.
Carcinoma, Hepatocellular
Upregulation of DARS2 by HBV promotes hepatocarcinogenesis through the miR-30e-5p/MAPK/NFAT5 pathway.
Cardiomyopathies
Loss of CLPP alleviates mitochondrial cardiomyopathy without affecting the mammalian UPRmt.
Cataract
Headache, cataract, and unilateral visual loss: unusual features of DARS2 variants in LBSL.
Cerebellar Ataxia
DARS2 is indispensable for Purkinje cell survival and protects against cerebellar ataxia.
Cough
Excitability and rhythmicity of tracheobronchial cough is altered by aspiration reflex in cats.
Cough
Provocation of aspiration reflexes and their effects on the pattern of cough and reflex apnea in cats.
Epilepsy
Perinatal Manifestations of DARS2-Associated Leukoencephalopathy With Brainstem and Spinal Cord Involvement and Lactate Elevation (LBSL).
Gait Ataxia
Acetazolamide-responsive exercise-induced episodic ataxia associated with a novel homozygous DARS2 mutation.
Hearing Loss
An acoustically evoked short latency negative response in profound hearing loss patients.
Infections
Early-onset leukoencephalopathy due to a homozygous missense mutation in the DARS2 gene.
Infections
The genome and transcriptome of the zoonotic hookworm Ancylostoma ceylanicum identify infection-specific gene families.
Leukoencephalopathies
A human pathology-related mutation prevents import of an aminoacyl-tRNA synthetase into mitochondria.
Leukoencephalopathies
A New DARS2 Mutation Discovered in an Adult Patient.
Leukoencephalopathies
Acetazolamide-responsive exercise-induced episodic ataxia associated with a novel homozygous DARS2 mutation.
Leukoencephalopathies
DARS2 gene clinical spectrum: new ideas regarding an underdiagnosed leukoencephalopathy.
Leukoencephalopathies
DARS2 is indispensable for Purkinje cell survival and protects against cerebellar ataxia.
Leukoencephalopathies
DARS2 mutations in mitochondrial leukoencephalopathy and multiple sclerosis.
Leukoencephalopathies
DARS2 protects against neuroinflammation and apoptotic neuronal loss, but is dispensable for myelin producing cells.
Leukoencephalopathies
Early-onset leukoencephalopathy due to a homozygous missense mutation in the DARS2 gene.
Leukoencephalopathies
Impaired information-processing speed and working memory in leukoencephalopathy with brainstem and spinal cord involvement and elevated lactate (LBSL) and DARS2 mutations: a report of three adult patients.
Leukoencephalopathies
LBSL: Case Series and DARS2 Variant Analysis in Early Severe Forms With Unexpected Presentations.
Leukoencephalopathies
Leukoencephalopathy With Brain Stem and Spinal Cord Involvement and Lactate Elevation (LBSL): A Case With Long-term Follow-up.
Leukoencephalopathies
Leukoencephalopathy with Brain Stem and Spinal Cord Involvement and Lactate Elevation High Outcome Variation between Two Siblings.
Leukoencephalopathies
Leukoencephalopathy with brainstem and spinal cord involvement and lactate elevation (LBSL) with a novel DARS2 mutation and isolated progressive spastic paraparesis.
Leukoencephalopathies
Leukoencephalopathy with brainstem and spinal cord involvement and lactate elevation: clinical and genetic characterization and target for therapy.
Leukoencephalopathies
Leukoencephalopathy With Brainstem and Spinal Cord Involvement and Normal Lactate: A New Mutation in the DARS2 Gene.
Leukoencephalopathies
Leukoencephalopathy with brainstem and spinal cord involvement caused by a novel mutation in the DARS2 gene.
Leukoencephalopathies
Magnetic resonance imaging and genetic investigation of a case of rottweiler leukoencephalomyelopathy.
Leukoencephalopathies
Mitochondrial aspartyl-tRNA synthetase deficiency causes leukoencephalopathy with brain stem and spinal cord involvement and lactate elevation.
Leukoencephalopathies
Mitochondrial dysfunctions in leukoencephalopathy with brainstem and spinal cord involvement and lactate elevation (LBSL).
Leukoencephalopathies
Mitochondrial syndromes with leukoencephalopathies.
Leukoencephalopathies
Mutations in DARS cause hypomyelination with brain stem and spinal cord involvement and leg spasticity.
Leukoencephalopathies
Neurodegenerative disease-associated mutants of a human mitochondrial aminoacyl-tRNA synthetase present individual molecular signatures.
Leukoencephalopathies
Neuronal ablation of mt-AspRS in mice induces immune pathway activation prior to severe and progressive cortical and behavioral disruption.
Leukoencephalopathies
Neuropathology of leukoencephalopathy with brainstem and spinal cord involvement and high lactate caused by a homozygous mutation of DARS2.
Leukoencephalopathies
Perinatal Manifestations of DARS2-Associated Leukoencephalopathy With Brainstem and Spinal Cord Involvement and Lactate Elevation (LBSL).
Leukoencephalopathies
Reply: DARS2 gene clinical spectrum: new ideas regarding an underdiagnosed leukoencephalopathy.
Leukoencephalopathies
Spinal Cord Calcification in an Early-Onset Progressive Leukoencephalopathy.
Leukoencephalopathies
The Leukodystrophies HBSL and LBSL-Correlates and Distinctions.
Leukoencephalopathies
Three human aminoacyl-tRNA synthetases have distinct sub-mitochondrial localizations that are unaffected by disease-associated mutations.
Malaria
Plasmodial aspartyl-tRNA synthetases and peculiarities in Plasmodium falciparum.
Melanoma
Current practice of patient follow-up after potentially curative resection of cutaneous melanoma.
Melanoma
Geographic variation in posttreatment surveillance intensity for patients with cutaneous melanoma.
Melanoma
How surgeon age affects post-treatment surveillance strategies for melanoma patients.
Mitochondrial Diseases
DARS2 protects against neuroinflammation and apoptotic neuronal loss, but is dispensable for myelin producing cells.
Mitochondrial Diseases
Mitochondrial DNA homeostasis is essential for nigrostriatal integrity.
Mitochondrial Diseases
Tissue-Specific Loss of DARS2 Activates Stress Responses Independently of Respiratory Chain Deficiency in the Heart.
Multiple Sclerosis
DARS2 mutations in mitochondrial leukoencephalopathy and multiple sclerosis.
Muscle Spasticity
DARS2 protects against neuroinflammation and apoptotic neuronal loss, but is dispensable for myelin producing cells.
Neoplasms
Using apelin-based synthetic Notch receptors to detect angiogenesis and treat solid tumors.
Nervous System Diseases
Early-onset leukoencephalopathy due to a homozygous missense mutation in the DARS2 gene.
Neurodegenerative Diseases
Three human aminoacyl-tRNA synthetases have distinct sub-mitochondrial localizations that are unaffected by disease-associated mutations.
Neuroinflammatory Diseases
DARS2 is indispensable for Purkinje cell survival and protects against cerebellar ataxia.
Neuroinflammatory Diseases
DARS2 protects against neuroinflammation and apoptotic neuronal loss, but is dispensable for myelin producing cells.
Neuroinflammatory Diseases
Neuronal ablation of mt-AspRS in mice induces immune pathway activation prior to severe and progressive cortical and behavioral disruption.
Otitis Media
Natural insertion of the bro-1 ?-lactamase gene into the gatCAB operon affects Moraxella catarrhalis aspartyl-tRNAAsn amidotransferase activity.
pantoate-beta-alanine ligase (amp-forming) deficiency
Phenotypes and genotypes of mitochondrial aminoacyl-tRNA synthetase deficiencies from a single neurometabolic clinic.
Paraparesis, Spastic
Leukoencephalopathy with brainstem and spinal cord involvement and lactate elevation (LBSL) with a novel DARS2 mutation and isolated progressive spastic paraparesis.
Respiratory Tract Infections
Early-onset leukoencephalopathy due to a homozygous missense mutation in the DARS2 gene.
Shoulder Pain
The Health Status of Informal Waste Collectors in Korea.
Spastic Paraplegia, Hereditary
Compound Heterozygous DARS2 Mutations as a Mimic of Hereditary Spastic Paraplegia.
Tuberculosis
Identification and characterization of aspartyl-tRNA synthetase inhibitors against Mycobacterium tuberculosis by an integrated whole-cell target-based approach.
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A471T
-
mutant enzyme is still able to aminoacylate the native tRNAAsp in vivo at a level sufficient to complement the defective strain CS143
D29N
-
mutant enzyme is still able to aminoacylate the native tRNAAsp in vivo at a level sufficient to complement the defective strain CS143
E118K
-
mutant enzyme is still able to aminoacylate the native tRNAAsp in vivo at a level sufficient to complement the defective strain CS143. 6.5fold increase in aminoacylation rate and 3fold decrease in amino acid activation reaction
E93K
-
mutant enzyme is still able to aminoacylate the native tRNAAsp in vivo at a level sufficient to complement the defective strain CS143
G90S
-
mutant enzyme is still able to aminoacylate the native tRNAAsp in vivo at a level sufficient to complement the defective strain CS143
G90V
-
mutant enzyme is still able to aminoacylate the native tRNAAsp in vivo at a level sufficient to complement the defective strain CS143
K198L/D233E
-
slightly increased binding of Asp, binding of ASn is strongly increased to the level of Asp, no ability to adenylate Asn, molecular dynamic simulation, binding mechansim and free energy
K198L/Q199E/D233E
-
binding of Asp is strongly reduced, no ability to adenylate Asn, molecular dynamic simulation, binding mechansim and free energy
L30F
-
mutant enzyme is still able to aminoacylate the native tRNAAsp in vivo at a level sufficient to complement the defective strain CS143
P555S
-
thermosensitive mutant, resulting in substitution of Pro 555 by Ser. Pro555Ser lowers the stability of the functional configuration of both the acylation and the amino acid activation sites but has no significant effect on substrate binding
R383C
-
mutant enzyme is still able to aminoacylate the native tRNAAsp in vivo at a level sufficient to complement the defective strain CS143
T89I
-
mutant enzyme is still able to aminoacylate the native tRNAAsp in vivo at a level sufficient to complement the defective strain CS143
hDRSDELTA32
-
N-terminal 32-residue truncated form, hDRSDELTA32, with lower thermal stability and ATP-diphosphate exchange activity, but higher aminoacylation activity. Fusion protein of glutathione-S-transferase and hDRSDELTA32 with lower thermal stability
L613F
the mutant shows reduced specific activity compared to the wild type enzyme
L626Q
the mutant shows 43fold decreased specific activity compared to the wild type enzyme
L626V
-
the mutant shows 210fold reduced activity compared to the wild-type enzyme
R58G
the mutant shows an increase in specific activity compared to the wild type enzyme
S45G
a naturally occuring mutation identified in patients suffering leukoencephalopathy with brain stem and spinal cord involvement and lactate elevation. The mutant enzyme is not processed due to nontranslocation of the protein
T136S
the mutant shows an increase in specific activity compared to the wild type enzyme
Asp-DELTA20
-
native recombinant AspRS from rat and the N-terminal truncated derivatives Asp-DELTA20 and AspRS-DELTA36 expressed in yeast. A moderate but significant drop in affinity towards the multisynthetase complex is inferred by the removal of the N-terminal domain. This domain is absolutely required in vivo for association within the multisynthetase structure
D210A
-
central core binding mutant, increased acylation activity, increased dissociation constant
E188A
-
anticodon loop binding mutant, slightly reduced acylation activity, increased dissociation constant
E188A/S239A
-
anticodon-G73 binding mutant, reduced acylation activity, highly increased dissociation constant
E188A/T331A
-
anticodon-G73 binding mutant, highly reduced acylation activity, highly increased dissociation constant
E202A
-
central core binding mutant, slightly increased acylation activity, increased dissociation constant
E327A
-
acceptor arm binding mutant, reduced acylation activity
F127A
-
anticodon loop binding mutant, increased acylation activity, increased dissociation constant
F127A/D210A
-
anticodon binding mutant, reduced acylation activity, highly increased dissociation constant
F127A/E188A
-
anticodon binding mutant, reduced acylation activity, highly increased dissociation constant
F127A/S239A
-
anticodon-G73 binding mutant, reduced acylation activity, highly increased dissociation constant
F127A/T331A
-
anticodon-G73 binding mutant, highly reduced acylation activity, highly increased dissociation constant
F304A
-
terminal A binding mutant, reduced acylation activity
H116G
-
mutants with substituted His residues, His116Gly mutant with a slightly reduced rate of amino acid activation without affecting the other kinetic parameters, His271Gly mutant with completely destroyed activity, His332Gly mutant with 60% decrease in rate of tRNA aminoacylation and no significant changes in the other parameters, His334Gly mutant with 70% decrease in amino acid activation, complete loss of tRNA aspartylation and slightly increased Km for ATP, His271Ala mutant with 25% decrease in the rate of tRNA charging. His334 seems do be part of the active site, while His271 and His332 play an important structural role
H334A
-
acceptor arm binding mutant, highly reduced acylation activity, increased dissociation constant
K142A
-
anticodon loop binding mutant, increased acylation activity, increased dissociation constant
K142A/E188A
-
anticodon binding mutant, reduced acylation activity, highly increased dissociation constant
K155A
-
central core binding mutant, increased acylation activity, increased dissociation constant
K180A
-
anticodon loop binding mutant, slightly increased acylation activity, increased dissociation constant
K293A
-
acceptor arm binding mutant, highly increased acylation activity, increased dissociation constant
K428A
-
acceptor arm binding mutant, increased acylation activity, increased dissociation constant
K553A
-
acceptor arm binding mutant, acylation activity similar to wild-type, increased dissociation constant
N117A
-
anticodon loop binding mutant, increased acylation activity, increased dissociation constant
N227A
-
central core binding mutant, slightly increased acylation activity, increased dissociation constant
N328A
-
acceptor arm binding mutant, reduced acylation activity, increased dissociation constant
N328A/S329A/T331A
-
G73 binding mutant, highly reduced acylation activity, increased dissociation constant
P273G
-
Pro273Gly mutant. Catalytic properties of native and Pro273Gly homodimers or heterodimers of AspRS molecules, confirm the participation of Pro273 in subunit association
Q121A
-
anticodon loop binding mutant, increased acylation activity, increased dissociation constant
Q138A
-
anticodon loop binding mutant, slightly increased acylation activity, increased dissociation constant
Q138A/E188A
-
anticodon binding mutant, reduced acylation activity, highly increased dissociation constant
Q138A/R119A
-
anticodon binding mutant, reduced acylation activity, highly increased dissociation constant
Q300A
-
terminal A binding mutant, reduced acylation activity
R119A
-
anticodon loop binding mutant, increased acylation activity, increased dissociation constant
R119A/E188A
-
anticodon binding mutant, highly reduced acylation activity, highly increased dissociation constant
R485K
-
site-directed mutagenesis, the substitution in the catalytic site completely inhibits aspartylation by impairing ATP binding, this mutant still retains the capacity to be modified and shows the same pattern as wild-type AspRS on the two-dimensional gel, thus the modifications are not the result of autoaspartylation
S181A
-
anticodon loop binding mutant, increased acylation activity, increased dissociation constant
S280A
-
terminal A binding mutant, reduced acylation activity
S301A
-
terminal A binding mutant, reduced acylation activity, slightly increased dissociation constant
S329A
-
acceptor arm binding mutant, increased acylation activity, increased dissociation constant
S423A
-
acceptor arm binding mutant, reduced acylation activity
T124A
-
anticodon loop binding mutant, slightly reduced acylation activity, increased dissociation constant
T230A
-
central core binding mutant, increased acylation activity, increased dissociation constant
T331A
-
acceptor arm binding mutant, reduced acylation activity, increased dissociation constant
T424A
-
acceptor arm binding mutant, acylation activity similar to the wild-type, increased dissociation constant
K198L
-
exchange of the conserved residue leads to a slightly increased binding of Asp, binding of Asn is strongly increased to the level of Asp, no ability to adenylate Asn, molecular dynamic simulation, binding mechansim and free energy
K198L
-
site-directed mutagenesis, the mutant shows reduced ATP-diphosphate exchange activity compared to the wild-type enzyme
Q199E
site-directed mutagenesis and molecular dynamics simulation of the mutation, reduction in binding free energy in the simulation in agreement with experiment, overview
Q199E
-
site-directed mutagenesis, the mutant shows reduced ATP-diphosphate exchange activity compared to the wild-type enzyme
C152F
-
the mutant shows 14fold reduced activity compared to the wild-type enzyme
C152F
the mutation causes strongly reduced protein levels
D560V
-
the mutant shows 400fold reduced activity compared to the wild-type enzyme
D560V
the mutation causes strongly reduced protein levels, the mutant shows 6fold decreased specific activity compared to the wild type enzyme
Q184K
-
the mutant shows 170fold reduced activity compared to the wild-type enzyme
Q184K
the mutant shows an increase in specific activity compared to the wild type enzyme
Q184K
the mutation causes strongly reduced protein levels
R263Q
-
the mutant shows 260fold reduced activity compared to the wild-type enzyme
R263Q
the mutant shows 135fold decreased specific activity compared to the wild type enzyme
K85P
discriminating AspRS gains the ability to form Asp-tRNAAsn. Mutation impairs the ability to synthesize Asp-trNAASp in vitr, 8fold increase in KM-value for tRNAAsp
K85P
the wild-type enzyme shows no activity with tRNAAsn, the mutant is active with tRNAAsn
W26H
discriminating AspRS gains the ability to form Asp-tRNAAsn. Mutation causes a 1.5fold decrease in overall catalytic efficiency for Asp-tRNAASp synthesis
W26H
the wild-type enzyme shows no activity with tRNAAsn, the mutant is active with tRNAAsn
W26H/K85P
discriminating AspRS gains the ability to form Asp-tRNAAsn
W26H/K85P
the wild-type enzyme shows no activity with tRNAAsn, the mutant is active with tRNAAsn
additional information
-
transplantation of the L45 loop of Escherichia coli AspRS and two residues flanking the loop inside the Escherichia coli lysyl-tRNALys ligase sequence causes a loss of lysyl-tRNALys ligase capacity to aminoacylate tRNALys. The chimeric enzyme acquires the capacity to charge tRNAAsp with lysine
additional information
-
enzyme deficiency leads to autosomal recessive disease leukoencephalopathy with brain stem and spinal cord involvement and lactate elevation, i.e. LBSL, often manifesting in early childhood, affected individuals develop slowly progressive cerebellar ataxia, spasticity and dorsal column dysfunction, sometimes with a mild cognitive deficit or decline, phenotype, mutational analysis, overview
additional information
-
a male patient with two mutations heterogenous in the DARS2 gene, shows cerebellar, pyramidal and dorsal column dysfunctions and specific magnetic resonance imaging and characteristic magnetic resonance spectroscopy abnormalities, leukoencephalopathy with brain stem and spinal cord involvement, phenotype, overview
additional information
-
two deletion mutations in the DARS2 gene cause the autosomal recessive disorder leukoencephalopathy with brainstem and spinal cord involvement and lactate elevation. determination of cerebellar, pyramidal and dorsal column dysfunctions and abnormalities, e.g. in in the superior cerebellar peduncles, the intraparenchymal trajectories of the trigeminal nerves, the pyramidal tracts, and the medial lemniscus, by resonance imaging, MRI, and magnetic resonance spectroscopy, MRS, phenotype, overview
additional information
the RNA binding motif is mutated, from 70KKKEKKAKK78 to 70QEEREEGQM78
additional information
-
the RNA binding motif is mutated, from 70KKKEKKAKK78 to 70QEEREEGQM78
additional information
-
mutant enzyme with a deletion of 34 amino acids from its N-terminus does not associate within the complex from Chinese hamster ovary cells. A chimeric enzyme made of the amino-terminal moiety of rat liver aspartyl-tRNA synthetase fused to the catalytic domain of yeast lysyl-tRNA synthetase, expressed in Lys-101 cells (a Chinese hamster ovary cell line with a temperature-sensitive lysyl-tRNA synthetase) does not associate within the multisynthetase complex and cannot restore normal growth of mutant cells
additional information
-
two truncated forms lacking 20 or 36 amino acid residues from their amino-terminal polypeptide extension, expressed in Saccharomyces cerevisiae, are less stable than wild-type enzyme
additional information
-
C-terminal and N-terminal truncated forms. On the C-terminal side, very limited modifications readily affect the enzyme properties. The N-terminal sequence up to amino acid 70 is dispensable for activity, domains beyond amino acid 70 have increasing catalytic importance
additional information
-
truncated form that has lost the first 50-64 residues, with full retention of both the activity and the dimeric structure
additional information
-
construction of several N-terminal deletion mutants with altered mRNA binding properties, overview
additional information
-
cooperativity analysis of the G73 and anticodon binding interactions, overview, effect of mutations on cell growth
additional information
-
proteomic analysis of mutant cells in comparison to wild-type cells
additional information
-
wild-type discriminating enzyme is engineered to a non-discriminating mutant by site-directed mutagenesis, a L1 loop exchange
additional information
-
construction of 7 mutants for crystallization
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Escherichia coli (P21889)
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Escherichia coli, Escherichia coli TG1
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Post-translational modifications guard yeast from misaspartylation
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Thermococcus kodakarensis (Q52428)
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Homo sapiens (Q6PI48), Homo sapiens
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Brugia malayi
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Escherichia coli, Homo sapiens (Q6PI48), Homo sapiens
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Homo sapiens (P14868), Homo sapiens
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Songsiriritthigul, C.; Suebka, S.; Chen, C.J.; Fuengfuloy, P.; Chuawong, P.
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Helicobacter pylori (P56459), Helicobacter pylori ATCC 700392 (P56459)
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Released selective pressure on a structural domain gives new insights on the functional relaxation of mitochondrial aspartyl-tRNA synthetase
Biochimie
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Homo sapiens, Mus musculus
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Mycoplasma pneumoniae
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Arabidopsis thaliana
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Biochemical and structural characterization of mycobacterial aspartyl-tRNA synthetase AspS, a promising TB drug target
PLoS ONE
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Mycolicibacterium smegmatis, Mycobacterium tuberculosis (P9WFW3), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WFW3)
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