6.1.1.7: alanine-tRNA ligase
This is an abbreviated version!
For detailed information about alanine-tRNA ligase, go to the full flat file.
Word Map on EC 6.1.1.7
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6.1.1.7
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aminoacylation
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synthetases
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aminoacyl-trna
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leukodystrophy
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alanylation
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mischarged
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aarss
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leukoencephalopathy
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mistranslation
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tmrnas
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charcot-marie-tooth
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noncognate
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thrrs
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threonyl-trna
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minihelix
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seryl-trna
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anti-pl-12
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valrs
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misactivation
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microhelix
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ilers
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trans-translation
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molecular biology
- 6.1.1.7
- aminoacylation
- synthetases
- aminoacyl-trna
- leukodystrophy
-
alanylation
-
mischarged
-
aarss
- leukoencephalopathy
-
mistranslation
- tmrnas
- charcot-marie-tooth
-
noncognate
- thrrs
- threonyl-trna
- minihelix
- seryl-trna
-
anti-pl-12
- valrs
-
misactivation
- microhelix
- ilers
-
trans-translation
- molecular biology
Reaction
Synonyms
AARS2, Ala-tRNA synthetase, ALA1, ALA2, Alanine transfer RNA synthetase, Alanine translase, Alanine tRNA synthetase, Alanine--tRNA ligase, Alanine-transfer RNA ligase, alanine-tRNA ligase, alanyl tRNA ligase, Alanyl-transfer ribonucleate synthetase, Alanyl-transfer ribonucleic acid synthetase, Alanyl-transfer RNA synthetase, alanyl-tRNA ligase, alanyl-tRNA synthase, Alanyl-tRNA synthetase, alanyltRNA synthetase, AlaRS, mitochondrial alanyl-tRNA synthetase, More, mtAlaRS, MurM, MurN, Synthase, alanyl-transfer ribonucleate
ECTree
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Subunits
Subunits on EC 6.1.1.7 - alanine-tRNA ligase
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dimer
monomer
tetramer
additional information
monomer
1 * 18152, crystal structure analysis, two-domain structure consisting of seven antiparallel beta-sheets and six helices
monomer
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1 * 18152, crystal structure analysis, two-domain structure consisting of seven antiparallel beta-sheets and six helices
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AlaRS consists of four parts: an N-terminal aminoacylation active-site domain, a tRNA-recognition module, an editing domain and a C-terminal oligomerization domain
additional information
the enzyme is constituted by three domains with an evolutionarily conserved modular arrangement: the N-terminal aminoacylation domain, the editing domain and the C-terminal domain (C-Ala). Enzyme secondary structure prediction, overview
additional information
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the enzyme is constituted by three domains with an evolutionarily conserved modular arrangement: the N-terminal aminoacylation domain, the editing domain and the C-terminal domain (C-Ala). Enzyme secondary structure prediction, overview
additional information
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the enzyme is constituted by three domains with an evolutionarily conserved modular arrangement: the N-terminal aminoacylation domain, the editing domain and the C-terminal domain (C-Ala). Enzyme secondary structure prediction, overview
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additional information
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decameric association complex in which dimeric AlaRS is the predominant species at 25°C
additional information
alanyl-tRNA synthetase exists as a dimer in its native form and the C-terminal coiled-coil part plays an important role in the dimerization process. Dimerization is one of the key regulatory factors that is important in the proper folding and stability of Escherichia coli alaRS
additional information
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alanyl-tRNA synthetase exists as a dimer in its native form and the C-terminal coiled-coil part plays an important role in the dimerization process. Dimerization is one of the key regulatory factors that is important in the proper folding and stability of Escherichia coli alaRS
additional information
an isolated appended C-terminal domain (C-Ala), consisting of the C-terminal 757968 amino acids, forms dimers as well as monomers, gel filtration
additional information
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an isolated appended C-terminal domain (C-Ala), consisting of the C-terminal 757968 amino acids, forms dimers as well as monomers, gel filtration