6.1.1.23: aspartate-tRNAAsn ligase
This is an abbreviated version!
For detailed information about aspartate-tRNAAsn ligase, go to the full flat file.
Word Map on EC 6.1.1.23
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6.1.1.23
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aspartylation
-
aminoacylation
-
asparaginyl-trna
-
amidotransferase
-
trnaasp
-
synthetases
-
aminoacyl-trna
-
asp-trnaasp
-
transamidation
-
gatcabs
-
trna-dependent
-
mischarged
-
anticodon-binding
-
asprss
-
non-discriminating
-
misacylated
-
transamidosome
-
glutaminyl-trna
-
microcin
-
kodakaraensis
-
gln-trnagln
-
asp-trna
- 6.1.1.23
-
aspartylation
- aminoacylation
-
asparaginyl-trna
-
amidotransferase
- trnaasp
- synthetases
- aminoacyl-trna
- asp-trnaasp
-
transamidation
- gatcabs
-
trna-dependent
-
mischarged
-
anticodon-binding
- asprss
-
non-discriminating
-
misacylated
-
transamidosome
- glutaminyl-trna
-
microcin
- kodakaraensis
- gln-trnagln
- asp-trna
Reaction
Synonyms
aspartate tRNA synthetase, Aspartic acid translase, Aspartyl ribonucleic synthetase, aspartyl tRNA synthetase, aspartyl-transfer ribonucleate synthetase, Aspartyl-transfer ribonucleic acid synthetase, Aspartyl-transfer RNA synthetase, Aspartyl-tRNA synthetase, AspRS, EC 6.1.1.12, More, ND-AspRS, non-discriminating aspartyl-tRNA synthetase, nondicriminating AspRS, nondiscriminating aspartyl-tRNA synthetase, nondiscriminating AspRS, Synthetase, aspartyl-transfer ribonucleate
ECTree
6.1.1.23 aspartate-tRNAAsn ligaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 6.1.1.23 - aspartate-tRNAAsn ligase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + Asp-tRNAAsn
-
only the enzyme AspRS2 aspartylates tRNAAsn
-
-
?
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
Staphylococcus aureus FPR3757
-
-
-
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsn
-
-
-
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsn
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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
Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539
-
-
-
-
?
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
Staphylococcus aureus FPR3757
-
-
-
-
?
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
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-
?
