RNA, Transfer, Ala: A transfer RNA which is specific for carrying alanine to sites on the ribosomes in preparation for protein synthesis.Alanine-tRNA Ligase: An enzyme that activates alanine with its specific transfer RNA. EC 6.1.1.7.RNA Ligase (ATP): An enzyme that catalyzes the conversion of linear RNA to a circular form by the transfer of the 5'-phosphate to the 3'-hydroxyl terminus. It also catalyzes the covalent joining of two polyribonucleotides in phosphodiester linkage. EC 6.5.1.3.Polynucleotide Ligases: Catalyze the joining of preformed ribonucleotides or deoxyribonucleotides in phosphodiester linkage during genetic processes. EC 6.5.1.Polynucleotide 5'-Hydroxyl-Kinase: An enzyme that catalyzes the transfer of a phosphate group to the 5'-terminal hydroxyl groups of DNA and RNA. EC 2.7.1.78.RNA, Transfer: The small RNA molecules, 73-80 nucleotides long, that function during translation (TRANSLATION, GENETIC) to align AMINO ACIDS at the RIBOSOMES in a sequence determined by the mRNA (RNA, MESSENGER). There are about 30 different transfer RNAs. Each recognizes a specific CODON set on the mRNA through its own ANTICODON and as aminoacyl tRNAs (RNA, TRANSFER, AMINO ACYL), each carries a specific amino acid to the ribosome to add to the elongating peptide chains.Alanine: A non-essential amino acid that occurs in high levels in its free state in plasma. It is produced from pyruvate by transamination. It is involved in sugar and acid metabolism, increases IMMUNITY, and provides energy for muscle tissue, BRAIN, and the CENTRAL NERVOUS SYSTEM.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Amino Acyl-tRNA Synthetases: A subclass of enzymes that aminoacylate AMINO ACID-SPECIFIC TRANSFER RNA with their corresponding AMINO ACIDS.RNA Splicing: The ultimate exclusion of nonsense sequences or intervening sequences (introns) before the final RNA transcript is sent to the cytoplasm.Basic-Leucine Zipper Transcription Factors: A large superfamily of transcription factors that contain a region rich in BASIC AMINO ACID residues followed by a LEUCINE ZIPPER domain.Saccharomyces cerevisiae: A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement.tRNA Methyltransferases: Enzymes that catalyze the S-adenosyl-L-methionine-dependent methylation of ribonucleotide bases within a transfer RNA molecule. EC 2.1.1.Molecular Sequence Data: Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.Escherichia coli: A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.Ubiquitin-Protein Ligases: A diverse class of enzymes that interact with UBIQUITIN-CONJUGATING ENZYMES and ubiquitination-specific protein substrates. Each member of this enzyme group has its own distinct specificity for a substrate and ubiquitin-conjugating enzyme. Ubiquitin-protein ligases exist as both monomeric proteins multiprotein complexes.Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.Alanine Transaminase: An enzyme that catalyzes the conversion of L-alanine and 2-oxoglutarate to pyruvate and L-glutamate. (From Enzyme Nomenclature, 1992) EC 2.6.1.2.Anticodon: The sequential set of three nucleotides in TRANSFER RNA that interacts with its complement in MESSENGER RNA, the CODON, during translation in the ribosome.DNA Ligases: Poly(deoxyribonucleotide):poly(deoxyribonucleotide)ligases. Enzymes that catalyze the joining of preformed deoxyribonucleotides in phosphodiester linkage during genetic processes during repair of a single-stranded break in duplex DNA. The class includes both EC 6.5.1.1 (ATP) and EC 6.5.1.2 (NAD).Alanine Racemase: A pyridoxal-phosphate protein that reversibly catalyzes the conversion of L-alanine to D-alanine. EC 5.1.1.1.RNA, Transfer, Amino Acid-Specific: A group of transfer RNAs which are specific for carrying each one of the 20 amino acids to the ribosome in preparation for protein synthesis.RNA, Transfer, Amino Acyl: Intermediates in protein biosynthesis. The compounds are formed from amino acids, ATP and transfer RNA, a reaction catalyzed by aminoacyl tRNA synthetase. They are key compounds in the genetic translation process.RNA, Transfer, Ser: A transfer RNA which is specific for carrying serine to sites on the ribosomes in preparation for protein synthesis.Nucleic Acid Conformation: The spatial arrangement of the atoms of a nucleic acid or polynucleotide that results in its characteristic 3-dimensional shape.Ubiquitination: The act of ligating UBIQUITINS to PROTEINS to form ubiquitin-protein ligase complexes to label proteins for transport to the PROTEASOME ENDOPEPTIDASE COMPLEX where proteolysis occurs.RNA, Transfer, Phe: A transfer RNA which is specific for carrying phenylalanine to sites on the ribosomes in preparation for protein synthesis.Ubiquitin-Protein Ligase Complexes: Complexes of enzymes that catalyze the covalent attachment of UBIQUITIN to other proteins by forming a peptide bond between the C-terminal GLYCINE of UBIQUITIN and the alpha-amino groups of LYSINE residues in the protein. The complexes play an important role in mediating the selective-degradation of short-lived and abnormal proteins. The complex of enzymes can be broken down into three components that involve activation of ubiquitin (UBIQUITIN-ACTIVATING ENZYMES), conjugation of ubiquitin to the ligase complex (UBIQUITIN-CONJUGATING ENZYMES), and ligation of ubiquitin to the substrate protein (UBIQUITIN-PROTEIN LIGASES).RNA, Transfer, Trp: A transfer RNA which is specific for carrying tryptophan to sites on the ribosomes in preparation for protein synthesis.Mutation: Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.Cullin Proteins: A family of structurally related proteins that were originally discovered for their role in cell-cycle regulation in CAENORHABDITIS ELEGANS. They play important roles in regulation of the CELL CYCLE and as components of UBIQUITIN-PROTEIN LIGASES.Alanine Dehydrogenase: An NAD-dependent enzyme that catalyzes the reversible DEAMINATION of L-ALANINE to PYRUVATE and AMMONIA. The enzyme is needed for growth when ALANINE is the sole CARBON or NITROGEN source. It may also play a role in CELL WALL synthesis because L-ALANINE is an important constituent of the PEPTIDOGLYCAN layer.RNA, Transfer, Arg: A transfer RNA which is specific for carrying arginine to sites on the ribosomes in preparation for protein synthesis.Ligases: A class of enzymes that catalyze the formation of a bond between two substrate molecules, coupled with the hydrolysis of a pyrophosphate bond in ATP or a similar energy donor. (Dorland, 28th ed) EC 6.RNA, Transfer, Met: A transfer RNA which is specific for carrying methionine to sites on the ribosomes. During initiation of protein synthesis, tRNA(f)Met in prokaryotic cells and tRNA(i)Met in eukaryotic cells binds to the start codon (CODON, INITIATOR).RNA, Transfer, Gly: A transfer RNA which is specific for carrying glycine to sites on the ribosomes in preparation for protein synthesis.Ubiquitin: A highly conserved 76-amino acid peptide universally found in eukaryotic cells that functions as a marker for intracellular PROTEIN TRANSPORT and degradation. Ubiquitin becomes activated through a series of complicated steps and forms an isopeptide bond to lysine residues of specific proteins within the cell. These "ubiquitinated" proteins can be recognized and degraded by proteosomes or be transported to specific compartments within the cell.RNA, Transfer, Ile: A transfer RNA which is specific for carrying isoleucine to sites on the ribosomes in preparation for protein synthesis.Glutamate-Cysteine Ligase: One of the enzymes active in the gamma-glutamyl cycle. It catalyzes the synthesis of gamma-glutamylcysteine from glutamate and cysteine in the presence of ATP with the formation of ADP and orthophosphate. EC 6.3.2.2.RNA, Transfer, Glu: A transfer RNA which is specific for carrying glutamic acid to sites on the ribosomes in preparation for protein synthesis.RNA, Transfer, Asp: A transfer RNA which is specific for carrying aspartic acid to sites on the ribosomes in preparation for protein synthesis.RNA, Transfer, Val: A transfer RNA which is specific for carrying valine to sites on the ribosomes in preparation for protein synthesis.RNA, Transfer, Gln: A transfer RNA which is specific for carrying glutamine to sites on the ribosomes in preparation for protein synthesis.RNA, Transfer, Pro: A transfer RNA which is specific for carrying proline to sites on the ribosomes in preparation for protein synthesis.Protein Binding: The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.RNA, Transfer, His: A transfer RNA which is specific for carrying histidine to sites on the ribosomes in preparation for protein synthesis.

tRNA synthetase mutants of Escherichia coli K-12 are resistant to the gyrase inhibitor novobiocin. (1/81)

In previous studies we demonstrated that mutations in the genes cysB, cysE, and cls (nov) affect resistance of Escherichia coli to novobiocin (J. Rakonjac, M. Milic, and D. J. Savic, Mol. Gen. Genet. 228:307-311, 1991; R. Ivanisevic, M. Milic, D. Ajdic, J. Rakonjac, and D. J. Savic, J. Bacteriol. 177:1766-1771, 1995). In this work we expand this list with mutations in rpoN (the gene for RNA polymerase subunit sigma54) and the tRNA synthetase genes alaS, argS, ileS, and leuS. Similarly to resistance to the penicillin antibiotic mecillinam, resistance to novobiocin of tRNA synthetase mutants appears to depend upon the RelA-mediated stringent response. However, at this point the overlapping pathways of mecillinam and novobiocin resistance diverge. Under conditions of stringent response induction, either by the presence of tRNA synthetase mutations or by constitutive production of RelA protein, inactivation of the cls gene diminishes resistance to novobiocin but not to mecillinam.  (+info)

SmpB, a unique RNA-binding protein essential for the peptide-tagging activity of SsrA (tmRNA). (2/81)

In bacteria, SsrA RNA recognizes ribosomes stalled on defective messages and acts as a tRNA and mRNA to mediate the addition of a short peptide tag to the C-terminus of the partially synthesized nascent polypeptide chain. The SsrA-tagged protein is then degraded by C-terminal-specific proteases. SmpB, a unique RNA-binding protein that is conserved throughout the bacterial kingdom, is shown here to be an essential component of the SsrA quality-control system. Deletion of the smpB gene in Escherichia coli results in the same phenotypes observed in ssrA-defective cells, including a variety of phage development defects and the failure to tag proteins translated from defective mRNAs. Purified SmpB binds specifically and with high affinity to SsrA RNA and is required for stable association of SsrA with ribosomes in vivo. Formation of an SmpB-SsrA complex appears to be critical in mediating SsrA activity after aminoacylation with alanine but prior to the transpeptidation reaction that couples this alanine to the nascent chain. SsrA RNA is present at wild-type levels in the smpB mutant arguing against a model of SsrA action that involves direct competition for transcription factors.  (+info)

Single-nucleotide polymorphisms can cause different structural folds of mRNA. (3/81)

Single-nucleotide polymorphisms (SNPs) are the most common type of genetic variation in man. Genes containing one or more SNPs can give rise to two or more allelic forms of mRNAs. These mRNA variants may possess different biological functions as a result of differences in primary or higher order structures that interact with other cellular components. Here we report the observation of marked differences in mRNA secondary structure associated with SNPs in the coding regions of two human mRNAs: alanyl tRNA synthetase and replication protein A, 70-kDa subunit (RPA70). Enzymatic probing of SNP-containing allelic fragments of the mRNAs revealed pronounced allelic differences in cleavage pattern at sites 14 or 18 nt away from the SNP, suggesting that a single-nucleotide variation can give rise to different mRNA folds. By using phosphorothioate oligodeoxyribonucleotides complementary to the region of different allelic structures in the RPA70 mRNA, but not extending to the SNP itself, we find that the SNP exerts an allele-specific effect on the accessibility of its flanking site in the endogenous human RPA70 mRNA. This further supports the allele-specific structural features identified by enzymatic probing. These results demonstrate the contribution of common genetic variation to structural diversity of mRNA and suggest a broader role than previously thought for the effects of SNPs on mRNA structure and, ultimately, biological function.  (+info)

CDC64 encodes cytoplasmic alanyl-tRNA synthetase, Ala1p, of Saccharomyces cerevisiae. (4/81)

The cdc64-1 mutation causes G(1) arrest in Saccharomyces cerevisiae corresponding to a type II Start phenotype. We report that CDC64 encodes Ala1p, an alanyl-tRNA synthetase. Thus, cdc64-1 might affect charging of tRNA(Ala) and thereby initiation of cell division.  (+info)

Identification of discriminator base atomic groups that modulate the alanine aminoacylation reaction. (5/81)

Specific aminoacylation of tRNAs involves activation of an amino acid with ATP followed by amino acid transfer to the tRNA. Previous work showed that the transfer of alanine from Escherichia coli alanyl-tRNA synthetase to a cognate RNA minihelix involves a transition state sensitive to changes in the tRNA acceptor stem. Specifically, the "discriminator" base at position 73 of minihelix(Ala) is a critical determinant of the transfer step of aminoacylation. This single-stranded nucleotide has previously been shown by solution NMR to be stacked predominantly onto G(1) of the first base pair of the alanine acceptor stem helix. In this work, RNA duplex(Ala) variants were prepared to investigate the role of specific discriminator base atomic groups in aminoacylation catalytic efficiency. Results indicate that the purine structure appears to be important for stabilization of the transition state and that major groove elements are more critical than those located in the minor groove. This result is in accordance with the predicted orientation of a class II synthetase at the end of the acceptor helix. In particular, substitution of the exocyclic amino group of A(73) with a keto-oxygen resulted in negative discrimination at this site. Taken together, these new results are consistent with the involvement of major groove atomic groups of the discriminator base in the formation of the transition state for the amino acid transfer step.  (+info)

Expression of Arabidopsis thaliana mitochondrial alanyl-tRNA synthetase is not sufficient to trigger mitochondrial import of tRNAAla in yeast. (6/81)

It has often been suggested that precursors to mitochondrial aminoacyl-tRNA synthetases are likely carriers for mitochondrial import of tRNAs in those organisms where this process occurs. In plants, it has been shown that mutation of U(70) to C(70) in Arabidopsis thaliana tRNA(Ala)(UGC) blocks aminoacylation and also prevents import of the tRNA into mitochondria. This suggests that interaction of tRNA(Ala) with alanyl-tRNA synthetase (AlaRS) is necessary for import to occur. To test whether this interaction is sufficient to drive import, we co-expressed A. thaliana tRNA(Ala)(UGC) and the precursor to the A. thaliana mitochondrial AlaRS in Saccharomyces cerevisiae. The A. thaliana enzyme and its cognate tRNA were correctly expressed in yeast in vivo. However, although the plant AlaRS was efficiently imported into mitochondria in the transformed strains, we found no evidence for import of the A. thaliana tRNA(Ala) nor of the endogenous cytosolic tRNA(Ala) isoacceptors. We conclude that at least one other factor besides the mitochondrial AlaRS precursor must be involved in mitochondrial import of tRNA(Ala) in plants.  (+info)

Importance of discriminator base stacking interactions: molecular dynamics analysis of A73 microhelix(Ala) variants. (7/81)

Transfer of alanine from Escherichia coli alanyl-tRNA synthetase (AlaRS) to RNA minihelices that mimic the amino acid acceptor stem of tRNA(Ala) has been shown, by analysis of variant minihelix aminoacylation activities, to involve a transition state sensitive to changes in the 'discriminator' base at position 73. Solution NMR has indicated that this single-stranded nucleotide is predominantly stacked onto G1 of the first base pair of the alanine acceptor stem helix. We report the activity of a new variant with the adenine at position 73 substituted by its non-polar isostere 4-methylindole (M). Despite lacking N7, this analog is well tolerated by AlaRS. Molecular dynamics (MD) simulations show that the M substitution improves position 73 base stacking over G1, as measured by a stacking lifetime analysis. Additional MD simulations of wild-type microhelix(Ala) and six variants reveal a positive correlation between N73 base stacking propensity over G1 and aminoacylation activity. For the two DeltaN7 variants simulated we found that the propensity to stack over G1 was similar to the analogous variants that contain N7 and we conclude that the decrease in aminoacylation efficiency observed upon deletion of N7 is likely due to loss of a direct stabilizing interaction with the synthetase.  (+info)

Origin of mitochondria in relation to evolutionary history of eukaryotic alanyl-tRNA synthetase. (8/81)

The origin of the eukaryotic cell remains an unsolved question. Numerous experimental and phylogenetic observations support the symbiotic origin of the modern eukaryotic cell, with its nucleus and (typically) mitochondria. Incorporation of mitochondria has been proposed to precede development of the nucleus, but it is still unclear whether mitochondria were initially part of basal eukaryotes. Data on alanyl-tRNA synthetase from an early eukaryote and other sources are presented and analyzed here. These data are consistent with the notion that mitochondrial genesis did not significantly precede nucleus formation. Moreover, the data raise the possibility that diplomonads are primary amitochondriates that radiated from the eukaryotic lineage before mitochondria became fully integrated as a cellular organelle.  (+info)

*Alanine-tRNA ligase

... alanine-transfer RNA ligase, alanine transfer RNA synthetase, alanine tRNA synthetase, alanine translase, alanyl-transfer ... In enzymology, an alanine-tRNA ligase (EC 6.1.1.7) is an enzyme that catalyzes the chemical reaction ATP + L-alanine + tRNAAla ... L-alanine, and tRNA(Ala), whereas its 3 products are AMP, diphosphate, and L-alanyl-tRNA(Ala). This enzyme belongs to the ... The systematic name of this enzyme class is L-alanine:tRNAAla ligase (AMP-forming). Other names in common use include alanyl- ...

*AARS2

Alanyl-tRNA synthetase, mitochondrial, also known as alanine-tRNA ligase (AlaRS) or alanyl-tRNA synthetase 2 (AARS2), is an ... alanyl-tRNA synthetase 2". Bonnefond L, Fender A, Rudinger-Thirion J, Giegé R, Florentz C, Sissler M (March 2005). "Toward the ... "Toward the full set of human mitochondrial aminoacyl-tRNA synthetases: characterization of AspRS and TyrRS". Biochemistry. 44 ( ... "Exome sequencing identifies mitochondrial alanyl-tRNA synthetase mutations in infantile mitochondrial cardiomyopathy". American ...

*Aspartate-tRNA(Asn) ligase

This enzyme participates in alanine and asparagine metabolism. Ibba, M.; Söll, D. (2000). "Aminoacyl-tRNA synthesis". Annu. Rev ... Aspartate---tRNAAsn ligase (EC 6.1.1.23, nondiscriminating aspartyl-tRNA synthetase) is an enzyme with systematic name L- ... When this enzyme acts on tRNAAsp, it catalyses the same reaction as EC 6.1.1.12, aspartate---tRNA ligase. It has, however, ... This enzyme belongs to the family of ligases, to be specific those forming carbon-oxygen bonds in aminoacyl-tRNA and related ...

*Aspartate-tRNA ligase

This enzyme participates in alanine and aspartate metabolism and aminoacyl-trna biosynthesis. As of late 2007, 10 structures ... In enzymology, an aspartate-tRNA ligase (EC 6.1.1.12) is an enzyme that catalyzes the chemical reaction ATP + L-aspartate + ... and L-aspartyl-tRNA(Asp). This enzyme belongs to the family of ligases, to be specific those forming carbon-oxygen bonds in ... aminoacyl-tRNA and related compounds. The systematic name of this enzyme class is L-aspartate:tRNAAsp ligase (AMP-forming). ...

*D-alanine-poly(phosphoribitol) ligase

This enzyme belongs to the family of ligases, to be specific those forming carbon-oxygen bonds in aminoacyl-tRNA and related ... D-alanine: membrane acceptor ligase, D-alanine-D-alanyl carrier protein ligase, D-alanine-membrane acceptor ligase, and D- ... In enzymology, a D-alanine-poly(phosphoribitol) ligase (EC 6.1.1.13) is an enzyme that catalyzes the chemical reaction ATP + D- ... The systematic name of this enzyme class is D-alanine:poly(phosphoribitol) ligase (AMP-forming). Other names in common use ...

*List of EC numbers (EC 6)

... leucine-tRNA ligase EC 6.1.1.5: isoleucine-tRNA ligase EC 6.1.1.6: lysine-tRNA ligase EC 6.1.1.7: alanine-tRNA ligase EC 6.1. ... valine-tRNA ligase EC 6.1.1.10: methionine-tRNA ligase EC 6.1.1.11: serine-tRNA ligase EC 6.1.1.12: aspartate-tRNA ligase EC ... glycine-tRNA ligase EC 6.1.1.15: proline-tRNA ligase EC 6.1.1.16: cysteine-tRNA ligase EC 6.1.1.17: glutamate-tRNA ligase EC ... glutamine-tRNA ligase EC 6.1.1.19: arginine-tRNA ligase EC 6.1.1.20: phenylalanine-tRNA ligase EC 6.1.1.21: histidine-tRNA ...

*List of MeSH codes (D08)

... alanine-tRNA ligase MeSH D08.811.464.263.200.100 --- arginine-tRNA ligase MeSH D08.811.464.263.200.150 --- aspartate-tRNA ... isoleucine-trna ligase MeSH D08.811.464.263.200.500 --- leucine-trna ligase MeSH D08.811.464.263.200.550 --- lysine-trna ligase ... tyrosine-tRNA ligase MeSH D08.811.464.263.200.950 --- valine-tRNA ligase MeSH D08.811.464.267.500 --- coenzyme a ligases MeSH ... glutamate-trna ligase MeSH D08.811.464.263.200.350 --- glycine-trna ligase MeSH D08.811.464.263.200.400 --- histidine-trna ...

*Transfer-messenger RNA

... including the acceptor stem with elements like those in alanine tRNA that promote its aminoacylation by alanine-tRNA ligase. It ... The standard bacterial tmRNA consists of a tRNA(Ala)-like domain (allowing addition of a non-encoded alanine to mRNAs that ... the tmRNA can be charged by alanyl-tRNA synthetase with alanine. CLPP Ribosome Messenger RNA Keiler KC (2008). "Biology of ... With the exception of the N-terminal alanine, which comes from the 3' end of tmRNA itself, this tag sequence was traced to a ...

*Asparaginyl-tRNA synthase (glutamine-hydrolysing)

L-glutamine amido-ligase (ADP-forming). This enzyme participates in glutamate metabolism and alanine and aspartate metabolism. ... This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds carbon-nitrogen ligases with ... aspartyl-tRNA(Asn), and L-glutamine, whereas its 4 products are ADP, phosphate, asparaginyl-tRNA(Asn), and L-glutamate. ... The systematic name of this enzyme class is aspartyl-tRNAAsn:L-glutamine amido-ligase (ADP-forming). Other names in common use ...

*List of EC numbers (EC 4)

3-chloro-D-alanine dehydrochlorinase EC 4.5.1.3: dichloromethane dehalogenase EC 4.5.1.4: L-2-amino-4-chloropent-4-enoate ... TRNA-intron endonuclease EC 4.99.1.1: ferrochelatase EC 4.99.1.2: alkylmercury lyase EC 4.99.1.3: sirohydrochlorin ... heme ligase "Enzyme: 4.1.2.8". Kyoto Encyclopedia of Genes and Genomes. Retrieved 2017-04-07. European Bioinformatics Institute ...

*Artificial gene synthesis

Synthesis of the first complete gene, a yeast tRNA, was demonstrated by Har Gobind Khorana and coworkers in 1972. Synthesis of ... Total synthesis of the structural gene for an alanine transfer ribonucleic acid from yeast". J. Mol. Biol. 72 (2): 209-217. doi ... To improve specificity of oligonucleotide annealing, the synthesis step relies on a set of thermostable DNA ligase and ... At least in the case of E. coli, protein expression is maximized by predominantly using codons corresponding to tRNA that ...

*Chemical biology

In one example of this, an RNA ligase was created from a zinc finger scaffold after 17 rounds of directed evolution. This new ... such as alanine, that cannot be phosphorylated. While this approach has been successful in some cases, mutations are permanent ... an established technique in which one can insert an unnatural amino acid into a peptide sequence by charging synthetic tRNA ...

*List of EC numbers (EC 3)

N-formylmethionylaminoacyl-tRNA deformylase EC 3.5.1.28: N-acetylmuramoyl-L-alanine amidase EC 3.5.1.29: 2-(acetamidomethylene) ... glutamate-ammonia ligase) hydrolase EC 3.1.4.16: 2',3'-cyclic-nucleotide 2'-phosphodiesterase EC 3.1.4.17: 3',5'-cyclic- ... acylmuramoyl-alanine carboxypeptidase. Now EC 3.5.1.28, N-acetylmuramoyl-L-alanine amidase EC 3.4.17.8: muramoylpentapeptide ... Now EC 3.5.1.28, N-acetylmuramoyl-L-alanine amidase EC 3.4.19.11: gamma-D-Glutamyl-meso-diaminopimelate peptidase EC 3.4.19.12 ...

*List of EC numbers (EC 2)

D-alanine 2-hydroxymethyltransferase EC 2.1.2.8: deoxycytidylate 5-hydroxymethyltransferase EC 2.1.2.9: methionyl-tRNA ... protein ligase EC 2.7.7.64: UTP-monosaccharide-1-phosphate uridylyltransferase EC 2.7.7.65: diguanylate cyclase EC 2.7.7.66: ... tRNA (cytosine-5-)-methyltransferase EC 2.1.1.30: deleted EC 2.1.1.31: tRNA (guanine-N1-)-methyltransferase EC 2.1.1.32: tRNA ( ... tRNA guanosine-2'-O-methyltransferase EC 2.1.1.35: tRNA (uracil-5-)-methyltransferase EC 2.1.1.36: tRNA (adenine-N1-)- ...

*Chromosome 2 (human)

Ubiquitin ligase PLGLB2: Plasminogen-related protein B POLR1A: DNA-directed RNA polymerase I subunit RPA1 PREPL: Prolyl ... "genetype trna"[Properties] OR "genetype scrna"[Properties] OR "genetype snrna"[Properties] OR "genetype snorna"[Properties]) ... alanine-glyoxylate aminotransferase (oxalosis I; hyperoxaluria I; glycolicaciduria; serine-pyruvate aminotransferase) ALS2: ... encoding protein Neuralized E3 ubiquitin protein ligase 3 NCL: Nucleolin NR4A2: nuclear receptor subfamily 4, group A, member 2 ...
Recognition of tRNAs by alanyl-tRNA synthetases and FemXWv. (A) Sequence of the tRNAAla acceptor stem. The bases essential for formation of UDP-MurNAc-hexapepti
Sato, K, "A mammalian cell mutant with an altered alanyl-trna synthetase. Abstr." (1976). Subject Strain Bibliography 1976. 2737 ...
An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs, has no observable editing activity on tRNAs charged with cognate L-amino acid (PubMed:10383414, PubMed:4292198, PubMed:10918062, PubMed:24302572, PubMed:27224426). Edits mischarged glycyl-tRNA(Ala) more efficiently than AlaRS (PubMed:28362257). Acts via tRNA-based rather than protein-based catalysis (PubMed:24302572, PubMed:27224426, PubMed:28362257). Rejects correctly charged L-amino acid-tRNAs from its binding site rather than specifically recognizing incorrectly charged D-amino acid-tRNAs (PubMed:27224426). Hydrolyzes correctly charged, achiral, glycyl-tRNA(Gly); GTP-bound EF-Tu (tested with T.thermophilus EF-Tu AC Q5SHN6) protects charged glycyl-tRNA(Gly) from hydrolysis, while increasing Dtd levels or inactivating EF-Tu decreases protection (PubMed:27224426). Hydrolyzes mischarged glycyl-tRNA(Ala) (but not seryl-tRNA(Ala)) even in the presence of EF-Tu, edits about 4-fold better than the editing domain of AlaRS (PubMed
With the advent of a growing number of Aquificales genome sequences in public databases, we have re-analyzed this group of bacteria thriving in extreme environments. The Aquificales share the feature of a small, compact genome with a reduced number of protein and ncRNA genes. The genes for tRNAs are reduced to a minimum but retain the capacity to decode all types of codons, and rRNA genes are confined to 2-3 copies each. Several classical ncRNAs are present, such as SRP RNA, tmRNA, 6S RNA, RNase P RNA (except for all Aquificaceae) and riboswitch candidates in some Aquificales. Furthermore, by combining in silico analysis with dRNA-seq data of A. aeolicus, we were able to predict nearly 100 novel ncRNA candidates, some of which might be specific to the Aquificales. Finally, CRISPR systems of bacterial immunity were identified.. Re-annotation of protein genes using BacProt revealed novel proteins with unknown function, some of which might turn out to be specific to the Aquificales as well. On ...
Browse Item # PL-3223, PL-3223, BisGMA in the PL Industries catalog including Item #,Item Name,Description,Functionality,Color (APHA),Viscosity @ 25 ºC (cps),Toxic Substance Control Act List,Index of Refraction,Inhibitor
Results The study cohort included 65 female and 29 male ASS patients (77 anti Jo-1, 7 anti-PL-7 and 10 anti-PL-12) with median age at diagnosis of 49 years. At the end of the study period 62 of the patients were alive and 32 (34%) had died. At the time of the follow-up PFT, 90/94 patients were on immunosuppressive therapy. The median time from baseline to follow up PFT was 61 months, but differed between the living and deceased subsets (Table). In the total cohort, there were no significant differences in PFT values from baseline to follow-up; FVC -0.008 (p,0.933), FEV1 0.061 (p,0.369) and DLCO -0.312 (p,0.208). Subset analyses showed that the deceased patients, except for FVC at baseline, had consistently lower PFT values than the living patients (Table).We also observed a reduction in mean FVC and FEV1 values from baseline to follow-up in the deceased group, but not in the living group (Table). ...
Glycyl-tRNA synthetase (GARS) is one of 37 nuclear encoded amino acyl tRNA synthetases that function to attach amino acids onto their respective tRNA for protein translation.44 Since the discovery of GARS as a cause of dHMNV and CMT2D, mutations in three other amino acyl tRNAs have been identified as causes of intermediate CMT (DI-CMTC) (YARS, tyrosyl-tRNA synthetase),45 CMT2N (AARS, alanyl-tRNA synthetase)46 and autosomal recessive CMT2 (RI-CMTB) (KARS, lysyl-tRNA synthetase).47. In 2003, four different GARS mutations were discovered in five families with upper-limb predominant distal motor neuropathy (dHMNV or CMT2D).10 Six additional familial and sporadic cases of dHMN owing to GARS mutations have been reported.48-51 In an extended phenotype/genotype study of the original five families, 75% of affected family members presented in the second decade of life, with the majority functioning independently 40 years after disease onset.52 In one patient, weakness began in the lower limbs, ...
K14218 tRNA-Ala; tRNA Ala K14218 tRNA-Ala; tRNA Ala K14218 tRNA-Ala; tRNA Ala K14218 tRNA-Ala; tRNA Ala K14218 tRNA-Ala; tRNA Ala K14218 tRNA-Ala; tRNA Ala K14218 tRNA-Ala; tRNA Ala K14219 tRNA-Arg; tRNA Arg K14219 tRNA-Arg; tRNA Arg K14219 tRNA-Arg; tRNA Arg K14219 tRNA-Arg; tRNA Arg K14219 tRNA-Arg; tRNA Arg K14219 tRNA-Arg; tRNA Arg K14219 tRNA-Arg; tRNA Arg K14219 tRNA-Arg; tRNA Arg K14219 tRNA-Arg; tRNA Arg K14220 tRNA-Asn; tRNA Asn K14220 tRNA-Asn; tRNA Asn K14220 tRNA-Asn; tRNA Asn K14220 tRNA-Asn; tRNA Asn K14220 tRNA-Asn; tRNA Asn K14221 tRNA-Asp; tRNA Asp K14221 tRNA-Asp; tRNA Asp K14221 tRNA-Asp; tRNA Asp K14221 tRNA-Asp; tRNA Asp K14221 tRNA-Asp; tRNA Asp K14221 tRNA-Asp; tRNA Asp K14221 tRNA-Asp; tRNA Asp K14222 tRNA-Cys; tRNA Cys K14222 tRNA-Cys; tRNA Cys K14223 tRNA-Gln; tRNA Gln K14223 tRNA-Gln; tRNA Gln K14223 tRNA-Gln; tRNA Gln K14223 tRNA-Gln; tRNA Gln K14224 tRNA-Glu; tRNA Glu K14224 tRNA-Glu; tRNA Glu K14224 tRNA-Glu; tRNA Glu K14224 tRNA-Glu; tRNA Glu K14224 tRNA-Glu; tRNA ...
Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
July 15 2017 Issue The semi-monthly AARS online Hot Topics Newsletter is an exclusive AARS member benefit! You dont need to spend countless hours perusing your typical online sources when you have this! Stay informed today by becoming an AARS member and receiving the Hot Topics!
Mouse monoclonal valyl tRNA synthetase antibody [VARSA7E6] validated for WB, Dot and tested in Human. Immunogen corresponding to recombinant fragment
K14218 tRNA-Ala; tRNA Ala K14218 tRNA-Ala; tRNA Ala K14218 tRNA-Ala; tRNA Ala K14219 tRNA-Arg; tRNA Arg K14219 tRNA-Arg; tRNA Arg K14219 tRNA-Arg; tRNA Arg K14219 tRNA-Arg; tRNA Arg K14220 tRNA-Asn; tRNA Asn K14220 tRNA-Asn; tRNA Asn K14220 tRNA-Asn; tRNA Asn K14221 tRNA-Asp; tRNA Asp K14221 tRNA-Asp; tRNA Asp K14221 tRNA-Asp; tRNA Asp K14222 tRNA-Cys; tRNA Cys K14223 tRNA-Gln; tRNA Gln K14224 tRNA-Glu; tRNA Glu K14224 tRNA-Glu; tRNA Glu K14224 tRNA-Glu; tRNA Glu K14224 tRNA-Glu; tRNA Glu K14225 tRNA-Gly; tRNA Gly K14225 tRNA-Gly; tRNA Gly K14225 tRNA-Gly; tRNA Gly K14225 tRNA-Gly; tRNA Gly K14225 tRNA-Gly; tRNA Gly K14225 tRNA-Gly; tRNA Gly K14225 tRNA-Gly; tRNA Gly K14226 tRNA-His; tRNA His K14226 tRNA-His; tRNA His K14227 tRNA-Ile; tRNA Ile K14228 tRNA-Leu; tRNA Leu K14228 tRNA-Leu; tRNA Leu K14228 tRNA-Leu; tRNA Leu K14228 tRNA-Leu; tRNA Leu K14228 tRNA-Leu; tRNA Leu K14228 tRNA-Leu; tRNA Leu K14228 tRNA-Leu; tRNA Leu K14229 tRNA-Lys; tRNA Lys K14229 tRNA-Lys; tRNA Lys K14230 tRNA-Met; tRNA ...
It has been less than half a century since Robert W. Holley et al. used 140 kg of commercial bakers yeast to characterize the first noncoding RNA (ncRNA), alanine tRNA. Now, 48 years later, advanceme
Tryptophanyl tRNA synthetase兔单克隆抗体[EPR3423](ab109213)可与小鼠, 大鼠, 人样本反应并经WB, IHC, Flow Cyt实验严格验证。所有产品均提供质保服务,中国75%以上现货。
Rabbit polyclonal Glutamyl Prolyl tRNA synthetase antibody validated for WB, IHC and tested in Human. With 4 independent reviews. Immunogen corresponding to…
Mouse Monoclonal Anti-Tryptophanyl tRNA synthetase Antibody (3A12) [PE]. Validated: WB, ELISA, ICC/IF, IP. Tested Reactivity: Human. 100% Guaranteed.
Mouse Monoclonal Anti-Seryl tRNA synthetase Antibody (1H4) [DyLight 488]. Validated: WB, ELISA, ICC/IF, IHC, IHC-P. Tested Reactivity: Human. 100% Guaranteed.
Looking for online definition of Aars in the Medical Dictionary? Aars explanation free. What is Aars? Meaning of Aars medical term. What does Aars mean?
January 18, 2018 Issue The semi-monthly AARS online Hot Topics Newsletter is an exclusive AARS member benefit! We encourage you to invite your colleagues and patients to get active in the American Acne & Rosacea Society!
Pay less for Polaroid PL-9002-00 - Genuine - FREE Delivery - Reliable Z-Axis Adhesive 3D Printer Sheets. Reliable delivery. Every time!
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Tyrosyl tRNA synthetase兔多克隆抗体(ab31535)可与小鼠, 人样本反应并经WB, IP, ICC/IF实验严格验证。所有产品均提供质保服务,中国75%以上现货。
OBJECTIVE Serological testing for myositis-specific or associated autoantibodies [myositis-specific antibody (MSA) and myositis-associated antibody (MAA)] is useful for the diagnosis of idiopathic inflammatory myopathies (IIMs). However, available assays are neither standardized nor validated. The objective is to evaluate the accuracy of a commercial line blot assay for myositis diagnosis. METHODS IgG antibodies against Jo-1, PL-7, PL-12, PM/Scl, Ku, Mi-2 and Ro52 antigens were detected by a line blot and in-house RNA immunoprecipitation or immunoblot. We tested sera from 208 IIM patients, 50 healthy subjects and 180 control patients (11 non-autoimmune myopathy, 23 muscular dystrophy, 11 UCTD, 68 SLE, 36 SSc, 22 SS and 9 arthropathy). RESULTS MSAs or MAAs were detected in 98 (47%) out of the 208 IIM patients by line blot: anti-Jo-1 in 43 (21%), anti-PL-7 or anti-PL-12 in 8 (4%), anti-Mi-2 in 9 (4%), anti-PM/Scl in 9 (4%), anti-Ku in 10 (5%) and anti-Ro52 in 49 (24%). Overall specificity was: 100%
Residues 32 to 482 (E-value = 1.5e-16) place NG1489 in the tRNA-synt_2 family which is described as tRNA synthetases class II (D, K and N) (PF00152 ...
Reaktivität: Rind (Kuh), Human, Maus. 6 verschiedene HARS ELISA Kits vergleichen. Alle direkt auf antikoerper-online.de bestellbar!
Ultrasonic Pulse Velocity/Echo Testing of Concrete, Rock, Wood and Ceramics with Pundit PL-200/PE (Subtitles available in 11 languages) Proceqs Pundit PL-200
QARS, DARS, KARS. The current publication by Zhang and collaborators give us an interesting refresher course on basic molecular biology, particularly a section of the cellular machinery that I didnt believe to be relevant to human genetic epilepsies - tRNAs. In humans the amino acids are attached to the tRNAs through 37 different forms of tRNA synthetases, 17 of them only present in mitochondria. The names of the tRNA synthetases is derived from the specific amino acid symbol, followed by the suffix -ARS. Amongst the various tRNA synthetases implicated in human disease, two disease-related aaRS occur in a functional complex with QARS, the multisynthetase complex. These two aaRS are KARS and DARS. The KARS gene coding for the lysine tRNA synthetase has been found to be mutated in a particular form of Charcot-Marie-Tooth disease and, separately from this, nonsyndromic hearing loss. Mutations in the DARS gene coding for the asparate tRNA synthetase cause an inherited white matter disorder with leg ...
POLSKA GRUPA NARODOWA IAMLStowarzyszenie Bibliotekarzy Polskich Sekcja Bibliotek Muzycznych al. Niepodległości 213 PL-02-086 WarszawaemailwebsiteFacebookBranch members:President:Hanna Bias (Biblioteka Główna Akademii Muzycznej im. Karola Szymanowskiego w Katowicach)

Leucyl‐tRNA synthetase from the ancestral bacterium Aquifex aeolicus contains relics of synthetase evolution | The EMBO JournalLeucyl‐tRNA synthetase from the ancestral bacterium Aquifex aeolicus contains relics of synthetase evolution | The EMBO Journal

Chen JF, Li T, Wang ED, Wang YL (2001) Effect of alanine‐293 replacement on the activity, ATP binding, and editing of ... ligase, RNasin (ribonuclease inhibitor), isopropyl β‐d‐thiogalactoside (IPTG), and all restriction endonucleases were obtained ... Deacylation of different mischarged tRNAs (E.c tRNA1,2, E. coli tRNA1Leu or tRNA2Leu; A.a tRNA, A. aeolicus tRNALeu) by Aa‐CP1 ... tRNAGAGLeu, E. coli [3H]Ile‐tRNACAG1Leu, and E. coli [3H]Ile‐tRNAGAG2Leu. The hydrolytic editing of Ile‐tRNALeu by αβ‐LeuRS and ...
more infohttp://emboj.embopress.org/content/24/7/1430.share

herenciageneticayenfermedad: NCI Drug Dictionary - National Cancer Institute | D-1herenciageneticayenfermedad: NCI Drug Dictionary - National Cancer Institute | D-1

L-alanine racemase and D-alanine:D-alanine ligase, thereby impairing peptidoglycan formation necessary for bacterial cell wall ... In bacteria, demeclocycline binds reversibly to the 30S ribosomal subunit and blocks the binding of aminoacyl-tRNA to the A- ... glutamate-cysteine ligase catalytic subunit (Gclc) and glutamate-cysteine ligase regulatory subunit (Gclm); this also increases ... An analogue of the amino acid D-alanine with broad-spectrum antibiotic and glycinergic activities. D-cycloserine interferes ...
more infohttps://herenciageneticayenfermedad.blogspot.com/2017/06/nci-drug-dictionary-national-cancer_2.html

Alanine-tRNA ligase - WikipediaAlanine-tRNA ligase - Wikipedia

... alanine-transfer RNA ligase, alanine transfer RNA synthetase, alanine tRNA synthetase, alanine translase, alanyl-transfer ... In enzymology, an alanine-tRNA ligase (EC 6.1.1.7) is an enzyme that catalyzes the chemical reaction ATP + L-alanine + tRNAAla ... L-alanine, and tRNA(Ala), whereas its 3 products are AMP, diphosphate, and L-alanyl-tRNA(Ala). This enzyme belongs to the ... The systematic name of this enzyme class is L-alanine:tRNAAla ligase (AMP-forming). Other names in common use include alanyl- ...
more infohttps://en.wikipedia.org/wiki/Alanine%E2%80%94tRNA_ligase

alaS - Alanine--tRNA ligase - Helicobacter pylori (strain Shi470) - alaS gene & proteinalaS - Alanine--tRNA ligase - Helicobacter pylori (strain Shi470) - alaS gene & protein

... alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly ... charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. ... Catalyzes the attachment of alanine to tRNA(Ala) in a two-step ... IPR018162 Ala-tRNA-ligase_IIc_anticod-bd. IPR018165 Ala-tRNA-synth_IIc_core. IPR018164 Ala-tRNA-synth_IIc_N. IPR023033 Ala_tRNA ... IPR018162 Ala-tRNA-ligase_IIc_anticod-bd. IPR018165 Ala-tRNA-synth_IIc_core. IPR018164 Ala-tRNA-synth_IIc_N. IPR023033 Ala_tRNA ...
more infohttps://www.uniprot.org/uniprot/B2UV04

alaS - Alanine--tRNA ligase - Nitrosomonas eutropha (strain DSM 101675 / C91) - alaS gene & proteinalaS - Alanine--tRNA ligase - Nitrosomonas eutropha (strain DSM 101675 / C91) - alaS gene & protein

... alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly ... charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. ... Catalyzes the attachment of alanine to tRNA(Ala) in a two-step ... IPR018162 Ala-tRNA-ligase_IIc_anticod-bd. IPR018165 Ala-tRNA-synth_IIc_core. IPR018164 Ala-tRNA-synth_IIc_N. IPR023033 Ala_tRNA ... IPR018162 Ala-tRNA-ligase_IIc_anticod-bd. IPR018165 Ala-tRNA-synth_IIc_core. IPR018164 Ala-tRNA-synth_IIc_N. IPR023033 Ala_tRNA ...
more infohttps://www.uniprot.org/uniprot/Q0AHX2

Recombinant Saccharopolyspora erythraea Alanine--tRNA ligase(alaS) ,partial - CusabioRecombinant Saccharopolyspora erythraea Alanine--tRNA ligase(alaS) ,partial - Cusabio

... tRNA ligase(alaS) ,partial. It is produced in Yeast. High purity. Good price. ... Recombinant Saccharopolyspora erythraea Alanine--tRNA ligase(alaS) ,partial. Recombinant Saccharopolyspora erythraea Alanine-- ... Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction. ... E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This ...
more infohttps://www.cusabio.com/Recombinant-Protein/Recombinant-Saccharopolyspora-erythraea-Alanine-tRNA-ligasealaS-partial-389583.html

AARSD1 Gene - GeneCards | AASD1 Protein | AASD1 AntibodyAARSD1 Gene - GeneCards | AASD1 Protein | AASD1 Antibody

Alanyl-TRNA Synthetase Domain Containing 1, including: function, proteins, disorders, pathways, orthologs, and expression. ... alanine-tRNA ligase activity. IEA. --. Genes that share ontologies with AARSD1: view ... AARSD1 (Alanyl-TRNA Synthetase Domain Containing 1) is a Protein Coding gene. Diseases associated with AARSD1 include Ovary ... Gene Ontology (GO) annotations related to this gene include nucleic acid binding and aminoacyl-tRNA editing activity. An ...
more infohttp://www.genecards.org/cgi-bin/carddisp.pl?gene=AARSD1&rf=/home/genecards/current/website/carddisp.pl

SWISS-MODEL Repository | A2BN65SWISS-MODEL Repository | A2BN65

... tRNA ligase. Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5) ... Alanine--tRNA ligase UniProtKBInterProSTRINGInteractive Modelling. 921 aa; Sequence (Fasta) ... Alanyl-tRNA synthetase, class IIc, N-ter minal. IPR018164PF01411. 693-735. Threonyl/alanyl tRNA synthetase, SAD. IPR012947 ...
more infohttps://swissmodel.expasy.org/repository/uniprot/A2BN65

Mitochondrial Cardiomyopathy disease: Malacards - Research Articles, Drugs, Genes, Clinical TrialsMitochondrial Cardiomyopathy disease: Malacards - Research Articles, Drugs, Genes, Clinical Trials

alanine-tRNA ligase activity. GO:0004813 8.62. AARS AARS2 Jump to section. Aliases & Classifications. Anatomical Context. Drugs ... ligase activity, forming aminoacyl-tRNA and related compounds. GO:0016876 8.96. AARS AARS2 ... Alanyl-TRNA Synthetase 2, Mitochondrial. 17.18. GeneCards inferred via :. Publications (show sections) ... An important gene associated with Mitochondrial Cardiomyopathy is MT-TL2 (Mitochondrially Encoded TRNA Leucine 2 (CUN)), and ...
more infohttp://www.malacards.org/card/mitochondrial_cardiomyopathy

AlaRS Antibody 17394-1-AP  | ProteintechAlaRS Antibody 17394-1-AP | Proteintech

AARS(alanyl-tRNA synthetase) is also named as AlaRS(alanine tRNA ligase 1, cytoplasmic), renal carcinoma antigen NY-REN-42 and ... The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to ... It can interpret the RNA code and attach specific aminoacids to the tRNAs that contain the cognate trinucleotide anticodons. ... cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs(PMID: ...
more infohttps://www.ptglab.com/products/AARS-Antibody-17394-1-AP.htm

Effects of insufficient sleep on circadian rhythmicity and expression amplitude of the human blood transcriptome | PNASEffects of insufficient sleep on circadian rhythmicity and expression amplitude of the human blood transcriptome | PNAS

These genes were associated with functions and processes, such as alanyl-tRNA aminoacylation, alanine-tRNA ligase activity, and ... alanine-tRNA ligase activity (P = 0.0076), and translational elongation (P = 0.037). Biological processes and molecular ... the 688 genes that became circadian after sleep restriction were associated with processes such as alanyl-tRNA aminoacylation ( ...
more infohttp://www.pnas.org/content/110/12/E1132

AARSL (human)AARSL (human)

Alanine--tRNA ligase, mitochondrial Show on y-axis - References (HTP + LTP). References (LTP). References (HTP). ...
more infohttps://www.phosphosite.org/proteinAction.action?id=10108&showAllSites=true

UniProt: W0DH46 9AQUIUniProt: W0DH46 9AQUI

DE RecName: Full=Alanine--tRNA ligase {ECO:0000256,HAMAP-Rule:MF_00036}; DE EC=6.1.1.7 {ECO:0000256,HAMAP-Rule:MF_00036}; DE ... DR HAMAP; MF_00036_B; Ala_tRNA_synth_B; 1. DR InterPro; IPR002318; Ala-tRNA-lgiase_IIc. DR InterPro; IPR018162; Ala-tRNA-ligase ... DR GO; GO:0004813; F:alanine-tRNA ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB- ... DR InterPro; IPR018164; Ala-tRNA-synth_IIc_N. DR InterPro; IPR023033; Ala_tRNA_ligase_euk/bac. DR InterPro; IPR003156; DHHA1_ ...
more infohttps://www.genome.jp/dbget-bin/www_bget?uniprot:W0DH46_9AQUI

AARS Protein | Alanyl t RNA Synthetase | ProSpecAARS Protein | Alanyl t RNA Synthetase | ProSpec

Alanyl-tRNA synthetase Human Recombinant produced in SF9 is a glycosylated, polypeptide chain having a molecular mass of ... Alanyl-tRNA synthetase cytoplasmic, EC 6.1.1.7, Alanine-tRNA ligase, AlaRS, Renal carcinoma antigen NY-REN-42, PL-12, AARS. ... Alanyl-tRNA synthetase is a member of the aminoacyl-tRNA synthetase family, key enzymes of protein biosynthesis which charge ... tRNA molecules with the respective amino acids. This 108 kDa protein is an autoantigen recognized by PL-12 antibodies which ...
more infohttps://www.prospecbio.com/alanyl_t_rna_synthetase_human

Custom and Ready-to-use siRNA - the RNA interference moleculeCustom and Ready-to-use siRNA - the RNA interference molecule

KIAA1270; Alanine--tRNA ligase mitochondrial; Alanyl-tRNA synthetase; AlaRS; alanine--tRNA ligase; mitochondrial; alanyl-tRNA ... ACS1; ACSL2; Long-chain-fatty-acid--CoA ligase 1; Long-chain acyl-CoA synthetase 1; LACS 1; Long-chain-fatty-acid--CoA ligase. ... Acyl-coenzyme A synthetase ACSM3 mitochondrial; Acyl-CoA synthetase medium-chain family member 3; Butyrate--CoA ligase 3; ...
more infohttps://www.mybiosource.com/product.php?name=siRNA

PMID:1563353 - OMPwikiPMID:1563353 - OMPwiki

Alanine-tRNA Ligase; Alleles; Amdinocillin; Arginine-tRNA Ligase; Bacterial Proteins; Carrier Proteins; Cell Division; ... are shown here to be affected in the aminoacyl-tRNA synthetase genes argS and alaS, respectively. Although the argS and alaS ... inactivating the ribosome-associated ppGpp synthetase and preventing ppGpp synthesis in response to aminoacyl-tRNA starvation. ...
more infohttps://microbialphenotypes.org/wiki/index.php/PMID:1563353

KEGG SSDB Best Search Result: gse:GT50 11850KEGG SSDB Best Search Result: gse:GT50 11850

bfw:B5J99_16525 alanine--tRNA ligase K01872 887 109 ( -) 31 0.367 98 -, 1 hje:HacjB3_03220 Urease accessory protein UreD K03190 ... blas:BSY18_1431 alanine--tRNA ligase K01872 887 117 ( -) 33 0.388 98 -, 1 evi:Echvi_3830 PLP-dependent enzyme, glutamate ... kmr:108245162 E3 SUMO-protein ligase EGR2 K12496 443 104 ( -) 30 0.305 82 ,-, 1 lfa:LFA_1259 isopentenyl-adenosine A37 tRNA ... por:APT59_05355 tRNA-2-methylthio-N(6)-dimethylallylade K06168 469 107 ( -) 30 0.327 101 -, 1 ppsl:BJP27_20080 tRNA (N6- ...
more infohttps://www.kegg.jp/ssdb-bin/ssdb_best?org_gene=gse:GT50_11850

KEGG SSDB Best Search Result: tml:GSTUM 00007723001KEGG SSDB Best Search Result: tml:GSTUM 00007723001

nvn:NVIE_030020 alanine--tRNA ligase K01872 909 109 ( 7) 31 0.301 123 -, 3 ptu:PTUN_a1491 release factor glutamine ... nga:Ngar_c24410 alanine--tRNA ligase K01872 907 103 ( -) 29 0.336 116 -, 1 nsl:BOX37_15850 methyltransferase K02493 224 103 ... pbor:BSF38_01221 tRNA (guanine-N(7)-)-methyltransferase K03439 213 108 ( -) 30 0.348 66 -, 1 saci:Sinac_5728 ribosomal protein ... pami:JCM7686_2427 glutamate-ammonia-ligase adenylyltran K00982 948 105 ( -) 30 0.369 84 -, 1 pman:OU5_4581 hypothetical protein ...
more infohttp://www.kegg.jp/ssdb-bin/ssdb_best?org_gene=tml:GSTUM_00007723001

KEGG T00010: BSU27410KEGG T00010: BSU27410

bsu:BSU27410 K01872 alanyl-tRNA synthetase [EC:6.1.1.7] , (RefSeq) alaS; alanine--tRNA ligase (A) ...
more infohttps://www.genome.jp/dbget-bin/www_bget?-f+-n+a+bsu:BSU27410

ABB57749.1 protein (Synechococcus elongatus PCC7942) - STRING interaction networkABB57749.1 protein (Synechococcus elongatus PCC7942) - STRING interaction network

Alanine--tRNA ligase; Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction- alanine is first activated by ... Alanine--tRNA ligase; Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction- alanine is first activated by ... Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain (899 aa) ... Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain ...
more infohttps://string-db.org/network/1140.Synpcc7942_1719

NGR c02330 protein (Sinorhizobium fredii NGR234) - STRING interaction networkNGR c02330 protein (Sinorhizobium fredii NGR234) - STRING interaction network

Alanine--tRNA ligase; Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction- alanine is first activated by ... Alanine--tRNA ligase; Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction- alanine is first activated by ... Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain (887 aa) ... Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain ...
more infohttps://string-db.org/network/394.NGR_c02330

AARS Polyclonal Antibody | EpiGentekAARS Polyclonal Antibody | EpiGentek

... in a two-step reaction alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala ... Background Catalyzes the attachment of alanine to tRNA(Ala) ... Alanine--tRNA ligase, cytoplasmic, Alanyl-tRNA synthetase, AARS ... Recombinant Human Alanine--tRNA ligase, cytoplasmic protein (164-321AA). Storage. Shipped at 4°C. Upon receipt, store at -20°C ... Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and ...
more infohttps://www.epigentek.com/catalog/aars-polyclonal-antibody-p-60790.html

AARS Polyclonal Antibody, Biotin Conjugated | EpiGentekAARS Polyclonal Antibody, Biotin Conjugated | EpiGentek

... in a two-step reaction alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala ... Background Catalyzes the attachment of alanine to tRNA(Ala) ... Alanine--tRNA ligase, cytoplasmic, Alanyl-tRNA synthetase, AARS ... Recombinant Human Alanine--tRNA ligase, cytoplasmic protein (164-321AA). Storage. Shipped at 4°C. Upon receipt, store at -20°C ... Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and ...
more infohttps://www.epigentek.com/catalog/aars-polyclonal-antibody-biotin-conjugated-p-60793.html

Life Sciences  - Science MarketplaceLife Sciences - Science Marketplace

GO annotations related to this gene include alanine-tRNA ligase activity and molecular_function. An important paralo... ... AARSD1 (alanyl-tRNA synthetase domain containing 1) is a protein-coding gene. Diseases associated with AARSD1 include ovarian ...
more infohttp://science-marketplace.org/conferences-calls-for-papers/life-sciences

Pre GI: BLASTP HitsPre GI: BLASTP Hits

alanine--tRNA ligase/alanyl-tRNA synthetase. 0. 908. NC_013769:1739363:1751481. 1751481. 1754183. 2703. Sulfolobus islandicus L ... putative alanine--tRNA ligase (Alanyl-tRNA synthetase). 8e-42. 172. NC_014032:1972623:1986541. 1986541. 1989441. 2901. ... threonyl/alanine--tRNA ligase family protein,tRNA synthetase class II family protein. 5e-12. 73.9. ... alanine--tRNA ligase. 3e-20. 101. NC_015474:538544:555075. 555075. 555716. 642. Pyrococcus sp. NA2 chromosome, complete genome ...
more infohttp://pregi.bi.up.ac.za/pre_gi_blast.php?blast_source_accession=NC_009776&blast_cds_query=NC_009776:157311:171346
  • The single step synthesis of alanine from pyruvate is unique to Coccidians such as Toxoplasma and Neospora among the phylum of Apicomplexa . (llamp.net)
  • L-Alanine is second only to leucine in rate of occurrence, accounting for 7.8% of the primary structure in a sample of 1,150 proteins. (selfdecode.com)
  • An alanine-dependent, ribonuclease-inhibited conversion of adenosine 5'-phosphate to adenosine triphosphate. (wikipedia.org)
  • L-Alanine is found in many foods, some of which are snow crab, persian lime, papaya, and jerusalem artichoke. (foodb.ca)
  • It can interpret the RNA code and attach specific aminoacids to the tRNAs that contain the cognate trinucleotide anticodons. (ptglab.com)