6.1.1.12: aspartate-tRNA ligase
This is an abbreviated version!
For detailed information about aspartate-tRNA ligase, go to the full flat file.
Word Map on EC 6.1.1.12
-
6.1.1.12
-
synthetases
-
aminoacyl-trna
-
aminoacylation
-
aspartylation
-
asparaginyl-trna
-
anticodon
-
leukoencephalopathy
-
trnaasn
-
aarss
-
amidotransferase
-
aspartyl-adenylate
-
microcin
-
asparaginylation
-
asp-trnaasn
-
glnrs
-
gatcabs
-
anticodon-binding
-
glutaminyl-trna
-
misacylated
-
mischarged
-
transamidation
-
nondiscriminating
-
lysyl-trna
-
argrs
-
trnaphe
-
leurs
-
medicine
-
glutaminylation
-
pharmacology
- 6.1.1.12
- synthetases
- aminoacyl-trna
- aminoacylation
-
aspartylation
-
asparaginyl-trna
-
anticodon
- leukoencephalopathy
- trnaasn
-
aarss
-
amidotransferase
-
aspartyl-adenylate
-
microcin
-
asparaginylation
- asp-trnaasn
- glnrs
- gatcabs
-
anticodon-binding
- glutaminyl-trna
-
misacylated
-
mischarged
-
transamidation
-
nondiscriminating
- lysyl-trna
- argrs
- trnaphe
- leurs
- medicine
-
glutaminylation
- pharmacology
Reaction
Synonyms
Antigen T5, AsnRS, Asp-RS, ASPA, Aspartate--tRNA ligase, Aspartic acid translase, Aspartyl ribonucleate synthetase, Aspartyl ribonucleic synthetase, aspartyl ribonuleic synthetase, Aspartyl-transfer ribonucleic acid synthetase, Aspartyl-transfer RNA synthetase, Aspartyl-tRNA synthetase, AspRS, AspS, Bt cyt-AspRS, cytoplasmic aspartyl-tRNA synthetase, D-AspRS, DARS2, discriminating aspartyl-tRNA synthetase, discriminating AspRS, DRS, Drs2, Ec AspRS, HS cyt-AspRS, Hs mt-AspRS, hsAspRS, IBI1, mAspRS, mitochondrial aspartyl-tRNA synthetase, mmAspRS, mt-AspRS, non-discriminating aspartyl-tRNA synthetase, non-discriminating AspRS, Pa AspRS, Synthetase, aspartyl-transfer ribonucleate, Tb-AspRS1, Tb-AspRS2, TK0492
ECTree
6.1.1.12 aspartate-tRNA ligaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 6.1.1.12 - aspartate-tRNA 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 + 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 + tRNAAspA73
AMP + diphosphate + L-aspartyl-tRNAAspA73
-
-
-
-
?
adenosine 5’-[beta,gamma-imido]-triphosphate + L-Asp
AMP-Asp + imidodiphosphate
-
-
-
?
adenosine 5’-[beta,gamma-imido]-triphosphate + L-Asp
AMP-Asp + imidodiphosphate
-
-
-
?
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
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
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
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
about half as effective as tRNAAsp
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsp
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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
-
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
Escherichia coli B / ATCC 11303
-
-
-
?
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
-
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
-
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
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
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
discriminating AspRS1 and non-discriminating AspRS2
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
Thermus thermophilus or Escherichia coli tRNA
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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
-
-
-
?
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
?
-
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
?
-
-
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
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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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aspartate-dependent ATP-diphosphate exchange
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?
additional information
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erroneous binding of Asn by the enzyme is highly improbable, determination of binding energy
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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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Thermus thermophilus contains two AspRSs: the discriminating AspRS1 which aspartylates only tRNAAsp and the non-discriminating AspRS2 which aspartylates tRNAAsn as efficiently as tRNAAsp
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additional information
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Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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aspartate-dependent ATP-diphosphate exchange
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?
additional information
?
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Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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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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Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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Thermus thermophilus contains two AspRSs: the discriminating AspRS1 which aspartylates only tRNAAsp and the non-discriminating AspRS2 which aspartylates tRNAAsn as efficiently as tRNAAsp
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?
additional information
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enzyme can also utilize 2-aminomalonic acid and threo-3-hydroxyaspartic acid in ATP-diphosphate exchange
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