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ATP + alanine + tRNAAla
?
ATP + glycine + tRNAAla
AMP + diphosphate + glycyl-tRNAAla
-
-
-
?
ATP + L-alanine + dual specific tRNAPhe
AMP + diphosphate + L-alanyl-tRNAPhe
-
effects of deoxynucleotide substitutions in the tRNAPhe substrate on the enzyme activity, overview
-
?
ATP + L-alanine + dual specific tRNAPhe(17)
AMP + diphosphate + L-alanyl-tRNAPhe(17)
-
site-specific modification leads to deoxynucleotide substituted yeast tRNA substrate, the backbone is interrupted on the 3'-side of nucleotide 17
-
?
ATP + L-alanine + dual specific tRNAPhe(38)
AMP + diphosphate + L-alanyl-tRNAPhe(38)
-
site-specific modification leads to deoxynucleotide substituted yeast tRNA substrate, the backbone is interrupted on the 3'-side of nucleotide 38
-
?
ATP + L-alanine + dual specific tRNAPhe(57)
AMP + diphosphate + L-alanyl-tRNAPhe(57)
-
site-specific modification leads to deoxynucleotide substituted yeast tRNA substrate, the backbone is interrupted on the 3'-side of nucleotide 57
-
?
ATP + L-alanine + liver tRNA
?
-
-
-
-
?
ATP + L-alanine + tmRNA
AMP + diphosphate + L-alanyl-tmRNA
ATP + L-alanine + tRNA
?
-
-
-
-
?
ATP + L-alanine + tRNAAla
AMP + diphosphate + L-alanyl-tRNAAla
ATP + L-alanine + tRNAPhe(17)
?
-
-
-
-
?
ATP + L-alanine + tRNAPhe(38)
?
-
-
-
-
?
ATP + L-alanine + tRNAPhe(57)
?
-
-
-
-
?
ATP + L-alanine + tRNAPyl
AMP + diphosphate + L-alanyl-tRNAPyl
-
-
-
-
?
ATP + L-serine + tRNAAla
AMP + diphosphate + L-seryl-tRNAAla
-
-
-
?
ATP + lipid II L-alanine + tRNAAla
?
-
-
-
-
?
ATP + lipid II L-serine + tRNAAla
?
-
-
-
-
?
additional information
?
-
ATP + alanine + tRNAAla
?
-
key role in protein biosynthesis
-
-
?
ATP + alanine + tRNAAla
?
-
key role in protein biosynthesis
-
-
?
ATP + L-alanine + tmRNA
AMP + diphosphate + L-alanyl-tmRNA
-
transfer messenger RNA, 75fold reduced activity compared to cognate tRNAAla
-
?
ATP + L-alanine + tmRNA
AMP + diphosphate + L-alanyl-tmRNA
-
recombinant transfer messenger RNA substrate from Thermus thermophilus expressed in Escherichia coli
-
?
ATP + L-alanine + tmRNA
AMP + diphosphate + L-alanyl-tmRNA
-
recombinant transfer messenger RNA substrate from Thermus thermophilus expressed in Escherichia coli
-
?
ATP + L-alanine + tRNAAla
AMP + diphosphate + L-alanyl-tRNAAla
-
-
-
-
?
ATP + L-alanine + tRNAAla
AMP + diphosphate + L-alanyl-tRNAAla
-
the aminoacylation reaction takes place in two steps catalyzed by the same active site: the synthesis of an aminoacyladenylate as an activated intermediate from the amino acid and ATP and the transfer of the aminoacyl moiety to the 3'-terminus of the cognate tRNA to yield the aminoacyl-tRNA, the synthetic active site of AlaRS misrecognizes noncognate glycine and serine as well as recognizing the cognate alanine and produces GlytRNAAla and Ser-tRNAAla, the editing domain hydrolyzes the incorrect products GlytRNAAla and Ser-tRNAAla and thus contributes to accurate aminoacylation, three tRNA isoacceptors, tRNAAla1, tRNA and tRNAAla3
-
-
?
ATP + L-alanine + tRNAAla
AMP + diphosphate + L-alanyl-tRNAAla
-
-
-
-
?
ATP + L-alanine + tRNAAla
AMP + diphosphate + L-alanyl-tRNAAla
-
-
-
-
?
ATP + L-alanine + tRNAAla
AMP + diphosphate + L-alanyl-tRNAAla
-
-
-
?
ATP + L-alanine + tRNAAla
AMP + diphosphate + L-alanyl-tRNAAla
-
-
-
?
ATP + L-alanine + tRNAAla
AMP + diphosphate + L-alanyl-tRNAAla
-
-
-
?
ATP + L-alanine + tRNAAla
AMP + diphosphate + L-alanyl-tRNAAla
-
-
?
ATP + L-alanine + tRNAAla
AMP + diphosphate + L-alanyl-tRNAAla
-
-
?
ATP + L-alanine + tRNAAla
AMP + diphosphate + L-alanyl-tRNAAla
-
-
-
?
ATP + L-alanine + tRNAAla
AMP + diphosphate + L-alanyl-tRNAAla
-
-
-
?
ATP + L-alanine + tRNAAla
AMP + diphosphate + L-alanyl-tRNAAla
-
-
-
?
ATP + L-alanine + tRNAAla
AMP + diphosphate + L-alanyl-tRNAAla
-
-
-
?
ATP + L-alanine + tRNAAla
AMP + diphosphate + L-alanyl-tRNAAla
-
-
-
?
ATP + L-alanine + tRNAAla
AMP + diphosphate + L-alanyl-tRNAAla
-
-
-
?
ATP + L-alanine + tRNAAla
AMP + diphosphate + L-alanyl-tRNAAla
-
-
-
?
ATP + L-alanine + tRNAAla
AMP + diphosphate + L-alanyl-tRNAAla
-
-
-
?
ATP + L-alanine + tRNAAla
AMP + diphosphate + L-alanyl-tRNAAla
-
-
-
?
ATP + L-alanine + tRNAAla
AMP + diphosphate + L-alanyl-tRNAAla
-
-
-
?
ATP + L-alanine + tRNAAla
AMP + diphosphate + L-alanyl-tRNAAla
-
-
-
-
?
ATP + L-alanine + tRNAAla
AMP + diphosphate + L-alanyl-tRNAAla
-
-
-
?
ATP + L-alanine + tRNAAla
AMP + diphosphate + L-alanyl-tRNAAla
-
-
-
-
?
ATP + L-alanine + tRNAAla
AMP + diphosphate + L-alanyl-tRNAAla
-
2-step reaction
-
?
ATP + L-alanine + tRNAAla
AMP + diphosphate + L-alanyl-tRNAAla
-
wild-type and mutant Escherichia coli tRNAAla substrates, enzyme interacts with 2'-hydroxyls in the acceptor stem of the tRNA substrate
-
?
ATP + L-alanine + tRNAAla
AMP + diphosphate + L-alanyl-tRNAAla
-
a two-step reaction, class II synthetases are rate-limited by a step prior to aminoacyl transfer
-
-
?
ATP + L-alanine + tRNAAla
AMP + diphosphate + L-alanyl-tRNAAla
-
-
-
?
ATP + L-alanine + tRNAAla
AMP + diphosphate + L-alanyl-tRNAAla
-
-
?
ATP + L-alanine + tRNAAla
AMP + diphosphate + L-alanyl-tRNAAla
-
-
-
?
ATP + L-alanine + tRNAAla
AMP + diphosphate + L-alanyl-tRNAAla
-
-
-
?
ATP + L-alanine + tRNAAla
AMP + diphosphate + L-alanyl-tRNAAla
-
-
-
?
ATP + L-alanine + tRNAAla
AMP + diphosphate + L-alanyl-tRNAAla
AlaRS hydrolyzes mischarged tRNA by the catalytic zinc ion in the editing domain, modeling, overview
-
-
?
ATP + L-alanine + tRNAAla
AMP + diphosphate + L-alanyl-tRNAAla
-
-
-
?
ATP + L-alanine + tRNAAla
AMP + diphosphate + L-alanyl-tRNAAla
AlaRS hydrolyzes mischarged tRNA by the catalytic zinc ion in the editing domain, modeling, overview
-
-
?
ATP + L-alanine + tRNAAla
AMP + diphosphate + L-alanyl-tRNAAla
-
-
-
?
ATP + L-alanine + tRNAAla
AMP + diphosphate + L-alanyl-tRNAAla
-
-
-
?
ATP + L-alanine + tRNAAla
AMP + diphosphate + L-alanyl-tRNAAla
-
-
-
?
ATP + L-alanine + tRNAAla
AMP + diphosphate + L-alanyl-tRNAAla
-
-
-
?
ATP + L-alanine + tRNAAla
AMP + diphosphate + L-alanyl-tRNAAla
-
-
-
?
ATP + L-alanine + tRNAAla
AMP + diphosphate + L-alanyl-tRNAAla
-
-
-
-
?
ATP + L-alanine + tRNAAla
AMP + diphosphate + L-alanyl-tRNAAla
-
-
-
?
ATP + L-alanine + tRNAAla
AMP + diphosphate + L-alanyl-tRNAAla
-
-
-
-
?
ATP + L-alanine + tRNAAla
AMP + diphosphate + L-alanyl-tRNAAla
-
marked specificity for ATP. ADP, GTP, ITP, CTP and UTP are inactive
-
?
ATP + L-alanine + tRNAAla
AMP + diphosphate + L-alanyl-tRNAAla
-
-
-
?
ATP + L-alanine + tRNAAla
AMP + diphosphate + L-alanyl-tRNAAla
-
-
?
ATP + L-alanine + tRNAAla
AMP + diphosphate + L-alanyl-tRNAAla
-
-
-
?
ATP + L-alanine + tRNAAla
AMP + diphosphate + L-alanyl-tRNAAla
-
-
?
additional information
?
-
-
aminoacylates 9-base pair RNA duplexes whose sequences are based on the acceptor stems of either E. coli or human alanine tRNAs
-
-
?
additional information
?
-
-
alanine dependent ATP-diphosphate exchange: alanine + ATP + enzyme /alanine-AMP-enzyme + diphosphate
-
-
?
additional information
?
-
-
alanine dependent ATP-diphosphate exchange: alanine + ATP + enzyme /alanine-AMP-enzyme + diphosphate
-
-
?
additional information
?
-
-
enzyme contains a second active site which prevents mistranslation (mistaking Ser or Gly for Ala) and which is specially designed for hydrolytic editing
-
-
?
additional information
?
-
-
analysis of the deacylation activities of the wild type and five different Escherichia coli AlaRS editing site substitution mutants using the free-standing Pyrococcus horikoshii AlaX editing domain complexed with serine as a model and both Ser-tRNAAla and Ala-tRNAAla as substrates, overview
-
-
?
additional information
?
-
-
aminoacylates 9-base pair RNA duplexes whose sequences are based on the acceptor stems of either E. coli or human alanine tRNAs
-
-
?
additional information
?
-
recombinant mutant human appended C-terminal domain (C-Ala) shows strong binding to DNA cellulose, but not to cellulose alone
-
-
?
additional information
?
-
-
recombinant mutant human appended C-terminal domain (C-Ala) shows strong binding to DNA cellulose, but not to cellulose alone
-
-
?
additional information
?
-
-
synthesis of alanyl hydroxamate with high concentrations of hydroxylamine
-
-
?
additional information
?
-
-
alanine dependent ATP-diphosphate exchange: alanine + ATP + enzyme /alanine-AMP-enzyme + diphosphate
-
-
?
additional information
?
-
alanine dependent ATP-diphosphate exchange: alanine + ATP + enzyme /alanine-AMP-enzyme + diphosphate
-
-
?
additional information
?
-
-
alanine dependent ATP-diphosphate exchange: alanine + ATP + enzyme /alanine-AMP-enzyme + diphosphate
-
-
?
additional information
?
-
alanine dependent ATP-diphosphate exchange: alanine + ATP + enzyme /alanine-AMP-enzyme + diphosphate
-
-
?
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Ataxia
Alanyl-tRNA Synthetase 2 (AARS2)-Related Ataxia Without Leukoencephalopathy.
Ataxia
Editing-defective tRNA synthetase causes protein misfolding and neurodegeneration.
Brain Diseases
Deficient activity of alanyl-tRNA synthetase underlies an autosomal recessive syndrome of progressive microcephaly, hypomyelination, and epileptic encephalopathy.
Brain Diseases
Loss-of-function alanyl-tRNA synthetase mutations cause an autosomal-recessive early-onset epileptic encephalopathy with persistent myelination defect.
CADASIL
Novel Alanyl-tRNA Synthetase 2 Pathogenic Variants in Leukodystrophies.
Cardiomyopathies
A novel compound heterozygous mutation in AARS2 gene (c.965?G?>?A, p.R322H; c.334?G?>?C, p.G112R) identified in a Chinese patient with leukodystrophy involved in brain and spinal cord.
Cardiomyopathies
Exome sequencing identifies mitochondrial alanyl-tRNA synthetase mutations in infantile mitochondrial cardiomyopathy.
Cardiomyopathies
Expansion of the clinical spectrum associated with AARS2-related disorders.
Cardiomyopathies
Instability of the mitochondrial alanyl-tRNA synthetase underlies fatal infantile-onset cardiomyopathy.
Cardiomyopathies
Novel AARS2 gene mutation producing leukodystrophy: a case report.
Cardiomyopathies
Retinopathy and optic atrophy: Expanding the phenotypic spectrum of pathogenic variants in the AARS2 gene.
Cardiomyopathies
Siblings with lethal primary pulmonary hypoplasia and compound heterozygous variants in the AARS2 gene: further delineation of the phenotypic spectrum.
Cardiomyopathies
Structural modeling of tissue-specific mitochondrial alanyl-tRNA synthetase (AARS2) defects predicts differential effects on aminoacylation.
Cardiomyopathies
Thymidine kinase 2 and alanyl-tRNA synthetase 2 deficiencies cause lethal mitochondrial cardiomyopathy: case reports and review of the literature.
Cardiomyopathies
Use of whole-exome sequencing to determine the genetic basis of multiple mitochondrial respiratory chain complex deficiencies.
Cardiomyopathy, Dilated
Recessive Inheritance of a Rare Variant in the Nuclear Mitochondrial Gene for AARS2 in Late Onset Dilated Cardiomyopathy.
Cardiomyopathy, Hypertrophic
Thymidine kinase 2 and alanyl-tRNA synthetase 2 deficiencies cause lethal mitochondrial cardiomyopathy: case reports and review of the literature.
Cerebellar Ataxia
Alanyl-tRNA Synthetase 2 (AARS2)-Related Ataxia Without Leukoencephalopathy.
Charcot-Marie-Tooth Disease
A major determinant for binding and aminoacylation of tRNA(Ala) in cytoplasmic Alanyl-tRNA synthetase is mutated in dominant axonal Charcot-Marie-Tooth disease.
Charcot-Marie-Tooth Disease
A recurrent loss-of-function alanyl-tRNA synthetase (AARS?) mutation in patients with Charcot-Marie-Tooth disease type 2N (CMT2N).
Charcot-Marie-Tooth Disease
Deficient activity of alanyl-tRNA synthetase underlies an autosomal recessive syndrome of progressive microcephaly, hypomyelination, and epileptic encephalopathy.
Deafness
Use of whole-exome sequencing to determine the genetic basis of multiple mitochondrial respiratory chain complex deficiencies.
Dementia
Alanyl-tRNA Synthetase 2-Related Dementia with Selective Bilateral Frontal Cystic Leukoencephalopathy.
Dementia
Analysis of frontotemporal dementia, amyotrophic lateral sclerosis, and other dementia-related genes in 107 Korean patients with frontotemporal dementia.
Dyskinesias
Surgical alar base management with a personal technique: the tightening alar base suture.
Genetic Diseases, Inborn
Case report: 'AARS2 leukodystrophy'.
Genetic Diseases, Inborn
Novel Alanyl-tRNA Synthetase 2 Pathogenic Variants in Leukodystrophies.
Heart Diseases
Case report: 'AARS2 leukodystrophy'.
Heart Failure
Thymidine kinase 2 and alanyl-tRNA synthetase 2 deficiencies cause lethal mitochondrial cardiomyopathy: case reports and review of the literature.
Idiopathic Pulmonary Fibrosis
Autoantibody to alanyl-tRNA synthetase in patients with idiopathic pulmonary fibrosis.
Leukoencephalopathies
AARS2 Compound Heterozygous Variants in a Case of Adult-Onset Leukoencephalopathy With Axonal Spheroids and Pigmented Glia.
Leukoencephalopathies
AARS2 leukoencephalopathy: A new variant of mitochondrial encephalomyopathy.
Leukoencephalopathies
AARS2-related ovarioleukodystrophy: Clinical and neuroimaging features of three new cases.
Leukoencephalopathies
Alanyl-tRNA Synthetase 2 (AARS2)-Related Ataxia Without Leukoencephalopathy.
Leukoencephalopathies
Alanyl-tRNA Synthetase 2-Related Dementia with Selective Bilateral Frontal Cystic Leukoencephalopathy.
Leukoencephalopathies
An adolescence-onset male leukoencephalopathy with remarkable cerebellar atrophy and novel compound heterozygous AARS2 gene mutations: a case report.
Leukoencephalopathies
Analysis of Mutations in AARS2 in a Series of CSF1R-Negative Patients With Adult-Onset Leukoencephalopathy With Axonal Spheroids and Pigmented Glia.
Leukoencephalopathies
Expansion of the clinical spectrum associated with AARS2-related disorders.
Leukoencephalopathies
New AARS2 Mutations in Two Siblings With Tremor, Downbeat Nystagmus, and Primary Amenorrhea: A Benign Phenotype Without Leukoencephalopathy.
Leukoencephalopathies
Novel AARS2 gene mutation producing leukodystrophy: a case report.
Leukoencephalopathies
Novel Alanyl-tRNA Synthetase 2 Pathogenic Variants in Leukodystrophies.
Leukoencephalopathies
Practical approach to the diagnosis of adult-onset leukodystrophies: an updated guide in the genomic era.
Leukoencephalopathies
Redefining the phenotype of ALSP and
Leukoencephalopathies
Siblings with lethal primary pulmonary hypoplasia and compound heterozygous variants in the AARS2 gene: further delineation of the phenotypic spectrum.
Leukoencephalopathies
Structural modeling of tissue-specific mitochondrial alanyl-tRNA synthetase (AARS2) defects predicts differential effects on aminoacylation.
Lung Diseases, Interstitial
Anti-Synthetase Syndrome-Related Interstitial Lung Disease With Anti-PL-12 Antibodies.
Microcephaly
Deficient activity of alanyl-tRNA synthetase underlies an autosomal recessive syndrome of progressive microcephaly, hypomyelination, and epileptic encephalopathy.
Microcephaly
Impact of alanyl-tRNA synthetase editing deficiency in yeast.
Mitochondrial Diseases
Exome sequencing identifies mitochondrial alanyl-tRNA synthetase mutations in infantile mitochondrial cardiomyopathy.
Mitochondrial Diseases
Use of whole-exome sequencing to determine the genetic basis of multiple mitochondrial respiratory chain complex deficiencies.
Mitochondrial Encephalomyopathies
AARS2 leukoencephalopathy: A new variant of mitochondrial encephalomyopathy.
Muscular Dystrophies, Limb-Girdle
Case report: 'AARS2 leukodystrophy'.
Myocardial Infarction
[tRNA and aminoacyl-tRNA synthetases from the liver of rabbits in experimental myocardial infarction]
Myocardial Ischemia
[Seasonal differences in activity of tRNA and aminoacyl-tRNA synthetases of rabbit liver in myocardial ischemia]
Myositis
Anti-Synthetase Syndrome-Related Interstitial Lung Disease With Anti-PL-12 Antibodies.
Myositis
Autoantibodies against alanyl-tRNA synthetase and tRNAAla coexist and are associated with myositis.
Myositis
Pulmonary Pathologic Manifestations of Anti-Alanyl-tRNA Synthetase (Anti-PL-12)-Related Inflammatory Myopathy.
Myositis
RENAL, HEPATIC AND IMMUNE FUNCTION INDICES IN PATIENTS WITH DUCHENNE MUSCULAR DYSTROPHY.
Nervous System Diseases
Deficient activity of alanyl-tRNA synthetase underlies an autosomal recessive syndrome of progressive microcephaly, hypomyelination, and epileptic encephalopathy.
Neurodegenerative Diseases
Substrate specificity and catalysis by the editing active site of Alanyl-tRNA synthetase from Escherichia coli.
Neurodegenerative Diseases
The uniqueness of AlaRS and its human disease connections.
Optic Atrophy
Retinopathy and optic atrophy: Expanding the phenotypic spectrum of pathogenic variants in the AARS2 gene.
Polymyositis
Polymyositis and molecular mimicry, a mechanism of autoimmunity.
thymidine kinase deficiency
Thymidine kinase 2 and alanyl-tRNA synthetase 2 deficiencies cause lethal mitochondrial cardiomyopathy: case reports and review of the literature.
Tremor
New AARS2 Mutations in Two Siblings With Tremor, Downbeat Nystagmus, and Primary Amenorrhea: A Benign Phenotype Without Leukoencephalopathy.
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evolution
the enzyme belongs to the class IIa aminoacyl-tRNA synthestase family
evolution
the enzyme belongs to the class IIa aminoacyl-tRNA synthestase family. Divergent alanyl-tRNA synthetase genes of Vanderwaltozyma polyspora descended from a common ancestor through whole-genome duplication followed by asymmetric evolution. Cytoplasmic and mitochondrial forms of a eukaryotic aminoacyl-tRNA synthetase (aaRS) are generally encoded by two distinct nuclear genes, one of eukaryotic origin and the other of mitochondrial origin. In most known yeasts, only the mitochondrial-origin alanyl-tRNA synthetase (AlaRS) gene is retained and plays a dual-functional role. In contrast, the yeast Tetrapisispora phaffii possesses two significantly diverged AlaRS gene homologues, one encoding the cytoplasmic form and the other its mitochondrial counterpart. Phylogenetic relationships of yeast AlaRSs, overview
evolution
the enzyme belongs to the class IIa aminoacyl-tRNA synthestase family. Divergent alanyl-tRNA synthetase genes of Vanderwaltozyma polyspora descended from a common ancestor through whole-genome duplication followed by asymmetric evolution. Cytoplasmic and mitochondrial forms of a eukaryotic aminoacyl-tRNA synthetase (aaRS) are generally encoded by two distinct nuclear genes, one of eukaryotic origin and the other of mitochondrial origin. In most known yeasts, only the mitochondrial-origin alanyl-tRNA synthetase (AlaRS) gene is retained and plays a dual-functional role. In contrast, the yeast Vanderwaltozyma polyspora possesses two significantly diverged AlaRS gene homologues, one encoding the cytoplasmic form and the other its mitochondrial counterpart. Clever selection of transcription and translation initiation sites enables the two isoforms to be localized and thus functional in their respective cellular compartments. But the two isoforms can also be stably expressed and function in the reciprocal compartments by insertion or removal of a mitochondrial targeting signal. Synteny and phylogeny analyses reveal that the AlaRS homologues of Vanderwaltozyma polyspora arose from a dual-functional common ancestor through whole-genome duplication (WGD). Moreover, the mitochondrial form has higher synonymous (1.6fold) and nonsynonymous (2.8fold) substitution rates than does its cytoplasmic counterpart, presumably due to a lesser constraint imposed on components of the mitochondrial translational apparatus. Asymmetric evolution confers the divergence between the AlaRS paralogues of Vanderwaltozyma polyspora. Phylogenetic relationships of yeast AlaRSs, overview
evolution
the enzyme belongs to the class IIa aminoacyl-tRNA synthestase family. Divergent alanyl-tRNA synthetase genes of Vanderwaltozyma polyspora descended from a common ancestor through whole-genome duplication followed by asymmetric evolution. Cytoplasmic and mitochondrial forms of a eukaryotic aminoacyl-tRNA synthetase (aaRS) are generally encoded by two distinct nuclear genes, one of eukaryotic origin and the other of mitochondrial origin. In most known yeasts, only the mitochondrial-origin alanyl-tRNA synthetase (AlaRS) gene is retained and plays a dual-functional role. The AlaRS homologues of Saccharomyces cerevisiae arose from a dual-functional common ancestor through whole-genome duplication (WGD), but retains only one copy of the AlaRS gene. Phylogenetic relationships of yeast AlaRSs, overview
evolution
the enzyme belongs to the class IIa aminoacyl-tRNA synthetase family. Divergent alanyl-tRNA synthetase genes of Vanderwaltozyma polyspora descended from a common ancestor through whole-genome duplication followed by asymmetric evolution. Cytoplasmic and mitochondrial forms of a eukaryotic aminoacyl-tRNA synthetase (aaRS) are generally encoded by two distinct nuclear genes, one of eukaryotic origin and the other of mitochondrial origin. In most known yeasts, only the mitochondrial-origin alanyl-tRNA synthetase (AlaRS) gene is retained and plays a dual-functional role. In contrast, the yeast Tetrapisispora phaffii possesses two significantly diverged AlaRS gene homologues, one encoding the cytoplasmic form and the other its mitochondrial counterpart. Phylogenetic relationships of yeast AlaRSs, overview
evolution
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). Alanyl-tRNA synthetases (AlaRSs) belong to class-II aminoacyl-tRNA synthetases
evolution
the sequence of appended C-terminal domain (C-Ala) of enzyme AlaRS diverged widely in the evolutionary progression to humans. During evolution, 19 aaRSs expanded by acquiring novel noncatalytic appended domains, which are absent from bacteria and many lower eukaryotes but confer extracellular and nuclear functions in higher organisms. AlaRS is the single exception, with an appended C-terminal domain (C-Ala) that is conserved from prokaryotes to humans but with a wide sequence divergence. In human cells, C-Ala is also a splice variant of AlaRS. Crystal structures of two forms of human C-Ala, and small-angle X-ray scattering of AlaRS, show that the large sequence divergence of human C-Ala reshaped C-Ala in a way that changed the global architecture of AlaRS. This reshaping removed the role of C-Ala in prokaryotes for docking tRNA and instead repurposed it to form a dimer interface presenting a DNA-binding groove. This groove cannot form with the bacterial ortholog. Direct DNA binding by human C-Ala, but not by bacterial C-Ala. Instead of acquiring a special appended domain, a new AlaRS architecture has benn created by diversifying a preexisting domain
evolution
-
the enzyme belongs to the class IIa aminoacyl-tRNA synthestase family. Divergent alanyl-tRNA synthetase genes of Vanderwaltozyma polyspora descended from a common ancestor through whole-genome duplication followed by asymmetric evolution. Cytoplasmic and mitochondrial forms of a eukaryotic aminoacyl-tRNA synthetase (aaRS) are generally encoded by two distinct nuclear genes, one of eukaryotic origin and the other of mitochondrial origin. In most known yeasts, only the mitochondrial-origin alanyl-tRNA synthetase (AlaRS) gene is retained and plays a dual-functional role. In contrast, the yeast Vanderwaltozyma polyspora possesses two significantly diverged AlaRS gene homologues, one encoding the cytoplasmic form and the other its mitochondrial counterpart. Clever selection of transcription and translation initiation sites enables the two isoforms to be localized and thus functional in their respective cellular compartments. But the two isoforms can also be stably expressed and function in the reciprocal compartments by insertion or removal of a mitochondrial targeting signal. Synteny and phylogeny analyses reveal that the AlaRS homologues of Vanderwaltozyma polyspora arose from a dual-functional common ancestor through whole-genome duplication (WGD). Moreover, the mitochondrial form has higher synonymous (1.6fold) and nonsynonymous (2.8fold) substitution rates than does its cytoplasmic counterpart, presumably due to a lesser constraint imposed on components of the mitochondrial translational apparatus. Asymmetric evolution confers the divergence between the AlaRS paralogues of Vanderwaltozyma polyspora. Phylogenetic relationships of yeast AlaRSs, overview
-
evolution
-
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). Alanyl-tRNA synthetases (AlaRSs) belong to class-II aminoacyl-tRNA synthetases
-
malfunction
enzyme mutations are associated with infantile mitochondrial cardiomyopathy
malfunction
importance of the mtARS proteins for mitochondrial pathophysiology since nearly every nuclear gene for mtARS (out of 19) is recognized as a disease gene for mitochondrial disease. Mutations in the AARS2 gene for mitochondrial alanyl-tRNA synthetase (mtAlaRS) is observed both in patients with infantile-onset cardiomyopathy and in patients with childhood to adulthood-onset leukoencephalopathy. The cardiomyopathy phenotype results from a single allele, causing an amino acid change R592W in the editing domain of AARS2, whereas the leukodystrophy mutations are located in other domains of the synthetase. All mutations reduce the aminoacylation activity of the synthetase, because all mtAlaRS domains contribute to tRNA binding for aminoacylation. The cardiomyopathy mutations severely compromise aminoacylation whereas partial activity is retained by the mutation combinations found in the leukodystrophy patients. Molecular basis of the distinct tissue-specific phenotypic outcomes of enzyme mutantions, structure analysis and homology modeling, overview
physiological function
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the relatively modest specificity of the AlaRS editing domain may provide a rationale for the widespread phylogenetic distribution of AlaX free-standing editing domains, thereby contributing a further mechanism to lower concentrations of misacylated tRNAAla
physiological function
alanyl-tRNA synthetases (AlaRSs) play an essential role in the early events of protein synthesis by catalyzing the conjugation of amino acids to their cognate transfer RNAs. The C-terminal domain, C-Ala, plays an essential role in enzyme activity
physiological function
the accuracy of mitochondrial protein synthesis is dependent on the coordinated action of nuclear-encoded mitochondrial aminoacyl-tRNA synthetases (mtARSs) and the mitochondrial DNA-encoded tRNAs. The mitochondrial alanyl-tRNA synthetase (mtAlaRS) differs from the other mtARSs because in addition to the aminoacylation domain, it has a conserved editing domain for deacylating tRNAs that have been mischarged within correct amino acids
physiological function
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alanyl-tRNA synthetases (AlaRSs) play an essential role in the early events of protein synthesis by catalyzing the conjugation of amino acids to their cognate transfer RNAs. The C-terminal domain, C-Ala, plays an essential role in enzyme activity
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additional information
enzyme structure modeling, analysis of the contact surface between linker safety belt, and beta-barrel of the editing domain in modeled human mitochondrial AlaRS, overview
additional information
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enzyme structure modeling, analysis of the contact surface between linker safety belt, and beta-barrel of the editing domain in modeled human mitochondrial AlaRS, overview
additional information
the near complete NMR resonance assignment of the 122 amino acid C-Ala domain from Bizionia argentinensis is determined, enzyme structure homology modeling using the X-ray structure of Aquifex aeolicus AlaRS C-Ala domain
additional information
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the near complete NMR resonance assignment of the 122 amino acid C-Ala domain from Bizionia argentinensis is determined, enzyme structure homology modeling using the X-ray structure of Aquifex aeolicus AlaRS C-Ala domain
additional information
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the near complete NMR resonance assignment of the 122 amino acid C-Ala domain from Bizionia argentinensis is determined, enzyme structure homology modeling using the X-ray structure of Aquifex aeolicus AlaRS C-Ala domain
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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
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
-
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
-
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
-
site-directed mutagenesis, the mutant shows reduced deacylation rates of tRNAAla compared to the wild-type enzyme
L73A
-
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/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
C666A/Q584H
-
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
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mutagenesis of the AlaRS editing active site
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
-
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
-
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
-
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
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deletion mutants with reduced aminoacylation efficiency, expressed in Escherichia coli strain BL21
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(deltaDE3) cells
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expressed in Escherichia coli BL21DE3star cells
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expressed in HEK-293T cells
expression in Escherichia coli
expression in Escherichia coli strain BL21
expression in Pichia sp.
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expression of the full-length AlaRS, of the N-terminal fragment lacking the C-terminal oligomerization domain, residues 1-739, and of the C-terminal oligomerization domain of AlaRS, residues 737-906, in Escherichia coli strain BL21
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gene ALA1, DNA and amino acid sequence determination and analysis, mitochondrial and cytoplasmic isozymes are encoded by a single nuclear gene ALA1, through alternative use of inframe successive ACG triplets and a downstream AUG triplet, overview, despite participation of the non-AUG-initiated leader peptide in mitochondrial localization, the leader peptide per se cannot target a cytoplasmic passenger protein into mitochondria under normal conditions, functional mapping
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gene ALA1, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression of His6-tagged wild-type and chimeric fusion enzymes
gene ALA1, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression of His6-tagged wild-type and chimeric fusion enzymes, recombinant expression of GFP-tagged isozyme ALA1 in Saccharomyces cerevisiae strain INVSc1
gene ALA2, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression of His6-tagged wild-type and chimeric fusion enzymes
gene ALA2, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression of His6-tagged wild-type and chimeric fusion enzymes, recombinant expression of GFP-tagged isozyme ALA2 in Saccharomyces cerevisiae strain INVSc1
gene alaS, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of His6-tagged full-length enzyme and C-terminal domain C-Ala in Escherichia coli strain BL21(DE3)
gene alaS, DNA sequence determination and analysis, phylogenetic origin
gene alaS, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
gene alaS, sequence comparisons, recombinant expression of a C-Ala construct consisting of the C-terminal 757-968 amino acids
gene cdc64, DNA sequence determination and analysis, gene maps to a locus between met7 and prt1 on chromosome XV, gene derepresses gcn4 expression, the cdc64-1 mutant strain can be complemented by expression of the wild-type enzyme
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gene PH0574, expression in Escherichia coli strain BL21
recombinant MurN is expressed and purified as MBP fusion protein in Escherichia coli
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temperature-sensitve mutant tsET12
-
-
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
gene ALA2, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression of His6-tagged wild-type and chimeric fusion enzymes
gene ALA2, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression of His6-tagged wild-type and chimeric fusion enzymes
gene alaS, DNA sequence determination and analysis, phylogenetic origin
gene alaS, DNA sequence determination and analysis, phylogenetic origin
gene alaS, DNA sequence determination and analysis, phylogenetic origin
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Substrate specificity and catalysis by the editing active site of alanyl-tRNA synthetase from Escherichia coli
Biochemistry
50
1474-1482
2011
Escherichia coli
brenda
Goetz, A.; Tyynismaa, H.; Euro, L.; Ellonen, P.; Hyoetylaeinen, T.; Ojala, T.; Haemaelaeinen, R.H.; Tommiska, J.; Raivio, T.; Oresic, M.; Karikoski, R.; Tammela, O.; Simola, K.O.; Paetau, A.; Tyni, T.; Suomalainen, A.
Exome sequencing identifies mitochondrial alanyl-tRNA synthetase mutations in infantile mitochondrial cardiomyopathy
Am. J. Hum. Genet.
88
635-642
2011
Homo sapiens (Q5JTZ9), Homo sapiens
brenda
Dignam, J.D.; Guo, J.; Griffith, W.P.; Garbett, N.C.; Holloway, A.; Mueser, T.
Allosteric interaction of nucleotides and tRNA(Ala) with E. coli alanyl-tRNA synthetase
Biochemistry
50
9886-9900
2011
Escherichia coli
brenda
Smal, C.; Zanzoni, S.; DOnofrio, M.; Molinari, H.; Cicero, D.O.; Assfalg, M.
1H, 15N and 13C chemical shift assignments of the C-Ala domain of the alanyl-tRNA synthetase of the psychrophilic bacterium Bizionia argentinensis sp. nov
Biomol. NMR Assign.
8
415-418
2013
Bizionia argentinensis, Bizionia argentinensis JUB59
brenda
Banerjee, B.; Banerjee, R.
Guanidine hydrochloride mediated denaturation of E. coli alanyl-tRNA Synthetase: identification of an inactive dimeric intermediate
Protein J.
33
119-127
2014
Escherichia coli
brenda
Smal, C.; Zanzoni, S.; D'Onofrio, M.; Molinari, H.; Cicero, D.; Assfalg, M.
1H, 15N and 13C chemical shift assignments of the C-Ala domain of the alanyl-tRNA synthetase of the psychrophilic bacterium Bizionia argentinensis sp. nov
Biomol. NMR Assign.
8
415-418
2014
Bizionia argentinensis (G2EA49), Bizionia argentinensis, Bizionia argentinensis JUB59 (G2EA49)
brenda
Euro, L.; Konovalova, S.; Asin-Cayuela, J.; Tulinius, M.; Griffin, H.; Horvath, R.; Taylor, R.W.; Chinnery, P.F.; Schara, U.; Thorburn, D.R.; Suomalainen, A.; Chihade, J.; Tyynismaa, H.
Structural modeling of tissue-specific mitochondrial alanyl-tRNA synthetase (AARS2) defects predicts differential effects on aminoacylation
Front. Genet.
6
21
2015
Homo sapiens (Q5JTZ9), Homo sapiens
brenda
Banerjee, B.; Banerjee, R.
Urea unfolding study of E. coli alanyl-tRNA synthetase and its monomeric variants proves the role of C-terminal domain in stability
J. Amino Acids
2015
805681
2015
Escherichia coli (P00957), Escherichia coli
brenda
Chang, C.P.; Chang, C.Y.; Lee, Y.H.; Lin, Y.S.; Wang, C.C.
Divergent alanyl-tRNA synthetase genes of Vanderwaltozyma polyspora descended from a common ancestor through whole-genome duplication followed by asymmetric evolution
Mol. Cell. Biol.
35
2242-2253
2015
Vanderwaltozyma polyspora (A7TPK2), Vanderwaltozyma polyspora (A7TRK4), Vanderwaltozyma polyspora, Tetrapisispora phaffii (G8BWM7), Tetrapisispora phaffii (G8C0Z7), Saccharomyces cerevisiae (P40825), Saccharomyces cerevisiae, Vanderwaltozyma polyspora ATCC 22028 / DSM 70294 (A7TPK2), Vanderwaltozyma polyspora ATCC 22028 / DSM 70294 (A7TRK4)
brenda
Sun, L.; Song, Y.; Blocquel, D.; Yang, X.L.; Schimmel, P.
Two crystal structures reveal design for repurposing the C-Ala domain of human AlaRS
Proc. Natl. Acad. Sci. USA
113
14300-14305
2016
Homo sapiens (Q5JTZ9), Homo sapiens
brenda