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
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aminoacylation
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asparaginyl-trna
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amidotransferase
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trnaasp
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synthetases
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aminoacyl-trna
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asp-trnaasp
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transamidation
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gatcabs
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trna-dependent
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mischarged
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anticodon-binding
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asprss
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non-discriminating
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misacylated
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transamidosome
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glutaminyl-trna
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microcin
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kodakaraensis
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gln-trnagln
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asp-trna
- 6.1.1.23
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aspartylation
- aminoacylation
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asparaginyl-trna
-
amidotransferase
- trnaasp
- synthetases
- aminoacyl-trna
- asp-trnaasp
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transamidation
- gatcabs
-
trna-dependent
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mischarged
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anticodon-binding
- asprss
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non-discriminating
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misacylated
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transamidosome
- glutaminyl-trna
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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
Advanced search results
Engineering
Engineering on EC 6.1.1.23 - aspartate-tRNAAsn ligase
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H28Q
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wild-type enzyme shows a slight preference to tRNAAsn over tRNAAsp. Mutation H28Q leads to a reverse tRNA preference
H77K/H28Q
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wild-type enzyme shows a slight preference to tRNAAsn over tRNAAsp. Mutation P77K/H28Q leads to a reverse tRNA preference
P77K
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wild-type enzyme shows a slight preference to tRNAAsn over tRNAAsp. Mutation P77K leads to a reverse tRNA preference and a 3fold increase in specificity for tRNAASp over tRNAAsn
H26A
site-directed mutagenesis, mutation the amino acid located in the AspRS anticodon binding domain limits the specificity of this nondiscriminating enzyme towards tRNAAsn, altered tRNA substrate specificity compared to the wild-type enzyme, overview
H26A/P84A
site-directed mutagenesis, mutation the amino acid located in the AspRS anticodon binding domain limits the specificity of this nondiscriminating enzyme towards tRNAAsn, altered tRNA substrate specificity compared to the wild-type enzyme, overview
H26A/P84K
site-directed mutagenesis, mutation the amino acid located in the AspRS anticodon binding domain limits the specificity of this nondiscriminating enzyme towards tRNAAsn, altered tRNA substrate specificity compared to the wild-type enzyme, overview
H26Q
site-directed mutagenesis, mutation the amino acid located in the AspRS anticodon binding domain limits the specificity of this nondiscriminating enzyme towards tRNAAsn, altered tRNA substrate specificity compared to the wild-type enzyme, overview
H26Q/P84A
site-directed mutagenesis, mutation the amino acid located in the AspRS anticodon binding domain limits the specificity of this nondiscriminating enzyme towards tRNAAsn, altered tRNA substrate specificity compared to the wild-type enzyme, overview
H26Q/P84K
site-directed mutagenesis, mutation the amino acid located in the AspRS anticodon binding domain limits the specificity of this nondiscriminating enzyme towards tRNAAsn, altered tRNA substrate specificity compared to the wild-type enzyme, overview
P84A
site-directed mutagenesis, mutation the amino acid located in the AspRS anticodon binding domain limits the specificity of this nondiscriminating enzyme towards tRNAAsn, altered tRNA substrate specificity compared to the wild-type enzyme, overview
P84K
site-directed mutagenesis, mutation the amino acid located in the AspRS anticodon binding domain limits the specificity of this nondiscriminating enzyme towards tRNAAsn, altered tRNA substrate specificity compared to the wild-type enzyme, overview
H26A
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site-directed mutagenesis, mutation the amino acid located in the AspRS anticodon binding domain limits the specificity of this nondiscriminating enzyme towards tRNAAsn, altered tRNA substrate specificity compared to the wild-type enzyme, overview
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H26Q
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site-directed mutagenesis, mutation the amino acid located in the AspRS anticodon binding domain limits the specificity of this nondiscriminating enzyme towards tRNAAsn, altered tRNA substrate specificity compared to the wild-type enzyme, overview
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H26Q/P84A
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site-directed mutagenesis, mutation the amino acid located in the AspRS anticodon binding domain limits the specificity of this nondiscriminating enzyme towards tRNAAsn, altered tRNA substrate specificity compared to the wild-type enzyme, overview
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P84A
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site-directed mutagenesis, mutation the amino acid located in the AspRS anticodon binding domain limits the specificity of this nondiscriminating enzyme towards tRNAAsn, altered tRNA substrate specificity compared to the wild-type enzyme, overview
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P84K
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site-directed mutagenesis, mutation the amino acid located in the AspRS anticodon binding domain limits the specificity of this nondiscriminating enzyme towards tRNAAsn, altered tRNA substrate specificity compared to the wild-type enzyme, overview
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L81N
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site-directed mutagenesis, the mutation in the anticodon binding domain doubles the kcat for tRNAAsn as compared to the wild-type enzyme
L81N/L86M
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site-directed mutagenesis, the mutation in the anticodon binding domain alters the tRNA specificity as compared to the wild-type enzyme, the L81N/L86M mutant does not follow Michaelis-Menten kinetics
L86M
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site-directed mutagenesis, the mutation in the anticodon binding domain alters the tRNA specificity as compared to the wild-type enzyme
G83K
H31L
additional information
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aspartylation reaction of the mutant enzyme is 55% as fast as the wild-type enzyme
G83K
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site-directed mutagenesis, the mutation increases the specificity of tRNAAsp charging over that of tRNAAsn by 4.2fold
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aspartylation reaction of the mutant enzyme is 84% as fast as the wild-type enzyme
H31L
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aspartylation reaction of the mutant enzyme is 92% as fast as the wild-type enzyme
H31L
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site-directed mutagenesis, the mutation increases the specificity of tRNAAsp charging over that of tRNAAsn by 3.5fold
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mutations in the anticodon binding domain of Helicobacter pylori ND-AspRS, e.g. at L81, L86, N82, and M87, reduce this enzymes ability to misacylate tRNAAsn and enhance tRNAAsp specificity, in a manner that correlates with the toxicity of the enzyme in Escherichia coli, overview
additional information
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naturylla occuring gene DARS2 mutant phenotype, overview
additional information
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AspRS overexpression leads deprivation of the gene's 5'-untranslated region, that is essential for directing mRNA recognition by the protein and initiating the retro-inhibition process, but does not lead to increased tRNAAsn and/or tRNAGlu misaspartylation or the logical consecutive post-translational stress