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
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alanylation
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mischarged
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aarss
- leukoencephalopathy
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mistranslation
- tmrnas
- charcot-marie-tooth
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noncognate
- thrrs
- threonyl-trna
- minihelix
- seryl-trna
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anti-pl-12
- valrs
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misactivation
- microhelix
- ilers
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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
6.1.1.7 alanine-tRNA ligaseAdvanced search results
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results (Engineering
Engineering on EC 6.1.1.7 - alanine-tRNA ligase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C290S
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mutant enzymes with replacement of Cys residues, Cys76Ser, Cys290Ser, Cys412Ser, Cys665Ser. Mutation of Cys665 to serine induces a 120-fold decrease in catalytic efficiency
C665S
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mutant enzymes with replacement of Cys residues, Cys76Ser, Cys290Ser, Cys412Ser, Cys665Ser. Mutation of Cys665 to serine induces a 120-fold decrease in catalytic efficiency
C666A
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site-directed mutagenesis, the mutant shows reduced deacylation rates of tRNAAla compared to the wild-type enzyme
C666A/Q584H
C76S
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mutant enzymes with replacement of Cys residues, Cys76Ser, Cys290Ser, Cys412Ser, Cys665Ser. Mutation of Cys665 to serine induces a 120-fold decrease in catalytic efficiency
D235A
no improvement in the discrimination between alanine and serine
D235E
no improvement in the discrimination between alanine and serine
D235N
no improvement in the discrimination between alanine and serine
D235Q
no improvement in the discrimination between alanine and serine
DELTA1-437
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mutant protein containing a deleted aminoacylation domain: mutant protein is fully active for clearance of Ser-tRNAAla but it is inactive deacylate Ser-tRNAAla
DELTA1-437/731-875
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mutant protein containing a deleted aminoacylation domain: mutant protein is inactive for clearance of Ser-tRNAAla. Using RNA-binding assays, it is shown that the inactivity of the mutant correlates with a lack of binding of tRNAAla. However, at much higher concentrations, mutant is able of specifically deacylating misacylated tRNAAla. Thus, the catalytic site for editing is not disrupted instead, the reduction in editing activity results from a loss of affinity for tRNA
DELTA1-437/R693K
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a region important for tRNA-specificity is further localized to a predicted strand-loop-strand motif within the region 438-875. Arg 693 is highly conserved. Mutant R693K has relaxed specificity for tRNAThr, and deacylated Ser-tRNAThr. Thus, the AlaRS editing domain shares a second, independent way to recognize tRNAAla
E664A
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site-directed mutagenesis, the mutant shows reduced deacylation rates of tRNAAla compared to the wild-type enzyme
G237A
mutation G237A introduces bulk into the alanine-binding pocket, with little other change in the pocket or the surrounding atoms. Shrinking of the alanine-binding pocket sharply raises the Km for alanine but does not greatly perturb the Km for serine
G674D
site-directed mutagenesis, a point mutation in the C-terminal domain, the mutation produces a monomeric variant with a fivefold reduced aminoacylation activity compared to the wild-type enzyme
I667E
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site-directed mutagenesis, the mutant shows reduced deacylation rates of tRNAAla compared to the wild-type enzyme
L73A
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mutant enzymes with replacement of Lys73 with Gln, Asn, Ala or Glu show reduction in catalytic efficiency in aminoacylation assay. Glu substitution causes a 5-fold decrease in affinity for alanine
L73E
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mutant enzymes with replacement of Lys73 with Gln, Asn, Ala or Glu show reduction in catalytic efficiency in aminoacylation assay. Glu substitution causes a 5-fold decrease in affinity for alanine
L73N
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mutant enzymes with replacement of Lys73 with Gln, Asn, Ala or Glu show reduction in catalytic efficiency in aminoacylation assay. Glu substitution causes a 5-fold decrease in affinity for alanine
L73Q
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mutant enzymes with replacement of Lys73 with Gln, Asn, Ala or Glu show reduction in catalytic efficiency in aminoacylation assay. Glu substitution causes a 5-fold decrease in affinity for alanine
Q584N
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site-directed mutagenesis, the mutant shows reduced deacylation rates of tRNAAla compared to the wild-type enzyme
T567G
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site-directed mutagenesis, the mutant shows reduced deacylation rates of tRNAAla compared to the wild-type enzyme
A77V
naturally occuring mutation of a catalytic residue. the mutant likely affects alanine binding resulting in either totally inactive enzyme or with little aminoacylation activity due to decreased affinity to alanine
E405K
naturally occuring mutation of a structural residue within the tRNA recognition subdomain of the aminoacylation domain, the mutation leads to a partly reduced rate of tRNA aminoacylation due to structural instability in the tRNA recognition fold
F50C
naturally occuring mutation, leads to reduced rate of aminoacylation due to instability of alanine- and ATP-binding sites and impaired alanyl-adenylate formation
G965R
naturally occuring mutation predicted to impair protein folding and stability resulting in loss of aminoacylation activity
L155R
the mutation is associated with infantile mitochondrial cardiomyopathy
R199C
naturally occuring mutation of a catalytic residue involved in ATP binding, the mutantion leads to reduced rate of tRNA aminoacylation due to affected ATP-binding and impaired alanyl-adenylate formation
R592W
R592W/A961V
naturally occuring lethal mutation R592W in gene AARS2 causing infantile cardiomyopathy, mutation A961V is predicted to impair protein folding and stability resulting in loss of aminoacylation activity
R592W/C218L
naturally occuring lethal mutation R592W in gene AARS2 causing infantile cardiomyopathy, truncated mutant
R592W/L155R
naturally occuring lethal mutation R592W in gene AARS2 causing infantile cardiomyopathy, mutation L155R is predicted to impair protein folding and stability resulting in loss of aminoacylation activity
R592W/R329H
naturally occuring lethal mutation R592W in gene AARS2 causing infantile cardiomyopathy, mutation R329H is predicted to impair protein folding and stability resulting in loss of aminoacylation activity
R592W/Y539C
naturally occuring lethal mutation R592W in gene AARS2 causing infantile cardiomyopathy. The Y539C mutation causes a dramatic decrease of aminoacylation rate due to impaired tRNA binding and positioning of the 3'-end within the active site
additional information
C666A/Q584H
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aminoacylation activity is unchanged from that of wild-type. In contrast to the wild-type protein mutant protein mischarges Ser onto tRNAAla. Consistent with this mischarging, deacylation of Ser-tRNA Ala by the mutant protein is undetecable. Mutant protein is sensitive to high concentrations of serine
C666A/Q584H
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Serine toxicity, experienced by a strain harboring an C666A/Q584H editing-defective alanyl-tRNA synthetase mutant, is rescued by an AlaXp-encoding transgene from Methanosarcina mazei. AlaXp is a free-standing editing domain homolog of AlaRS. Rescue is dependent on amino acid residues in AlaXp that are needed for its in vitro catalytic activity
R592W
the mutation is associated with infantile mitochondrial cardiomyopathy
R592W
a naturally occuring lethal mutation in the editing domain of AARS2 causing a cardiomyopathy phenotype, homology modeling of the AARS2 missense mutant, overview. The AARS2 cardiomyopathy mutation R592W is a common founder mutation and carried by all the identified patients with the severe infantile-onset phenotype
additional information
expression of truncated forms AlaRS-DELTAC, comprising the aminoacylation, tRNA-recognition, and editing domains, and AlaRS-C, comprising the dimerization domain
additional information
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expression of truncated forms AlaRS-DELTAC, comprising the aminoacylation, tRNA-recognition, and editing domains, and AlaRS-C, comprising the dimerization domain
additional information
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engineering of the enzyme by introduction of a mutation that compensates for a deletion
additional information
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K12 strain KL386 that carries the gene on a recombinant pBR322 plasmid
additional information
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the needed tRNA interaction energy is further localized to non-specific RNA-binding determinants located in the region between amino acids 808 and 875
additional information
a truncated enzyme comparising the N-terminal 700 amino acids forms a monomeric protein possessing similar aminoacylation activity like the wild-type enzyme, and construction of N461 truncated enzyme. Aminoacylation activity assay after refolding from denatured state reveals that the monomeric mutants are unable to regain their activity, whereas the dimeric full-length alaRS gets back similar activity as the native enzyme
additional information
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a truncated enzyme comparising the N-terminal 700 amino acids forms a monomeric protein possessing similar aminoacylation activity like the wild-type enzyme, and construction of N461 truncated enzyme. Aminoacylation activity assay after refolding from denatured state reveals that the monomeric mutants are unable to regain their activity, whereas the dimeric full-length alaRS gets back similar activity as the native enzyme
additional information
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engineering of the enzyme by introduction of a mutation that compensates for a deletion
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additional information
construction of an isolated appended C-terminal domain (C-Ala) consisting of the C-terminal 757968 amino acids, the 23 kDa protein forms dimers as well as monomers, and locates in the nucleus
additional information
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construction of an isolated appended C-terminal domain (C-Ala) consisting of the C-terminal 757968 amino acids, the 23 kDa protein forms dimers as well as monomers, and locates in the nucleus
additional information
patient haplotypes around the AARS2 mutation, some patients show heterozygous mutations R592W/L155R, R592W/R329H, R592W/A961V, R592W/C218L, or R592W/Y539C, but the same pehnotype as homozygous R592W mutants. Mapping and function predictions of AARS2 mutations associated with cardiomyopathy and leukodystrophy
additional information
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patient haplotypes around the AARS2 mutation, some patients show heterozygous mutations R592W/L155R, R592W/R329H, R592W/A961V, R592W/C218L, or R592W/Y539C, but the same pehnotype as homozygous R592W mutants. Mapping and function predictions of AARS2 mutations associated with cardiomyopathy and leukodystrophy
additional information
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temperature-sensitive mutation cdc64-1 might affect charging of tRNAAla and thereby initiation of cell division, the mutation causes G1 arrest in yeast cells corresponding to a type II Start phenotype, the mutant strain can be complemented by expression of the wild-type enzyme
additional information
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overexpression of the cytoplasmic isozyme enables it to overcome the compartmental barrier and function in the mitochondria as well, but deletion of as few as eight amino acid residues from its amino-terminus eliminates such a potential, the sequence upstream of the first in-frame AUG initiator not only carries an unusual initiation site, but also contributes to the pattern of protein expression and localization
additional information
generation of Saccharomyces cerervisiae ALA1 chimeric fusion proteins with ALA1 and ALA2 from Vanderwaltozyma polyspora and Tetrapisispora phaffii, overview
additional information
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generation of Saccharomyces cerervisiae ALA1 chimeric fusion proteins with ALA1 and ALA2 from Vanderwaltozyma polyspora and Tetrapisispora phaffii, overview
additional information
generation of Tetrapisispora phaffii ALA1 and ALA2 chimeric fusion proteins with ALA1 from Saccharomyces cerevisiae and Vanderwaltozyma polyspora ALA1 and ALA2, overview
additional information
generation of Tetrapisispora phaffii ALA1 and ALA2 chimeric fusion proteins with ALA1 from Saccharomyces cerevisiae and Vanderwaltozyma polyspora ALA1 and ALA2, overview
additional information
generation of Vanderwaltozyma polyspora ALA1 and ALA2 chimeric fusion proteins with ALA1 from Saccharomyces cerevisiae and Tetrapisispora phaffii, overview
additional information
generation of Vanderwaltozyma polyspora ALA1 and ALA2 chimeric fusion proteins with ALA1 from Saccharomyces cerevisiae and Tetrapisispora phaffii, overview
additional information
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generation of Vanderwaltozyma polyspora ALA1 and ALA2 chimeric fusion proteins with ALA1 from Saccharomyces cerevisiae and Tetrapisispora phaffii, overview
additional information
Vanderwaltozyma polyspora ATCC 22028 / DSM 70294
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generation of Vanderwaltozyma polyspora ALA1 and ALA2 chimeric fusion proteins with ALA1 from Saccharomyces cerevisiae and Tetrapisispora phaffii, overview
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