OrganismsChemicals and DrugsPhenomena and ProcessesInformation Science
RNA, Transfer, AlaAlanine-tRNA LigaseRNA Ligase (ATP)Polynucleotide LigasesPolynucleotide 5'-Hydroxyl-KinaseRNA, TransferAlanineBase SequenceAmino Acyl-tRNA SynthetasesRNA SplicingBasic-Leucine Zipper Transcription FactorsSaccharomyces cerevisiaetRNA MethyltransferasesMolecular Sequence DataEscherichia coliUbiquitin-Protein LigasesAmino Acid SequenceAlanine TransaminaseAnticodonDNA LigasesAlanine RacemaseRNA, Transfer, Amino Acid-SpecificRNA, Transfer, Amino AcylRNA, Transfer, SerNucleic Acid ConformationUbiquitinationRNA, Transfer, PheUbiquitin-Protein Ligase ComplexesRNA, Transfer, TrpMutationCullin ProteinsAlanine DehydrogenaseRNA, Transfer, ArgLigasesRNA, Transfer, MetRNA, Transfer, GlyUbiquitinRNA, Transfer, IleGlutamate-Cysteine LigaseRNA, Transfer, GluRNA, Transfer, AspRNA, Transfer, ValRNA, Transfer, GlnRNA, Transfer, ProProtein BindingBinding SitesRNA, Transfer, His
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)

A mammalian cell mutant with an altered alanyl-trna synthetase. Abstr by K SatoA mammalian cell mutant with an altered alanyl-trna synthetase. Abstr by K Sato
Sato, K, A mammalian cell mutant with an altered alanyl-trna synthetase. Abstr. (1976). Subject Strain Bibliography 1976. 2737 ...
https://mouseion.jax.org/ssbb1976/2737/
AARS Polyclonal Antibody | EpiGentekAARS Polyclonal Antibody | EpiGentek
Background The human alanyl-tRNA synthetase (AARS) belongs to a family of tRNA synthases, of the class II enzymes. Class II tRNA synthases evolved early in evolution and are highly conserved. This is reflected by the fact...
https://www.epigentek.com/catalog/aars-polyclonal-antibody-p-81918.html
AARS1 Gene - GeneCards | SYAC Protein | SYAC AntibodyAARS1 Gene - GeneCards | SYAC Protein | SYAC Antibody
Complete information for AARS1 gene (Protein Coding), Alanyl-TRNA Synthetase 1, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
https://www.genecards.org/cgi-bin/carddisp.pl?gene=AARS1
PathBankPathBank
Alanine (L-Alanine) is an α-amino acid that is used for protein biosynthesis. Approximately 8% of human proteins have alanine in their structures. The reductive lamination of pyruvate is effected by alanine transaminase. L-Alanine can be converted to pyruvic acid by alanine aminotransferase 1 reversibly coupled with interconversion of oxoglutaric acid and L-glutamic acid. L-Alanine can also be produced by alanine-glyoxylate transaminase with coupled interconversion of glyoxylate and glycine. L-Alanine will be coupled with alanyl tRNA by alanyl-tRNA synthetase to perform protein biosynthesis. Alanine can also be used to provide energy under fasting conditions. There are two pathways that can facilitate this: (1) alanine is converted to pyruvate to synthesize glucose via the gluconeogenesis pathway in liver tissue or (2) alanine converted into pyruvate moves into the TCA cycle to be oxidized in other tissues ...
https://pathbank.org/view/SMP0087164
Mitochondrial aminoacyl-tRNA synthetase disorders: an emerging group of developmental disorders of myelination | Journal of...Mitochondrial aminoacyl-tRNA synthetase disorders: an emerging group of developmental disorders of myelination | Journal of...
The mitochondrial aminoacyl-tRNA synthetase proteins (mt-aaRSs) are a group of nuclear-encoded enzymes that facilitate conjugation of each of the 20 amino acids to its cognate tRNA molecule. Mitochondrial diseases are a large, clinically heterogeneous group of disorders with diverse etiologies, ages of onset, and involved organ systems. Diseases related to mt-aaRS mutations are associated with specific syndromes that affect the central nervous system and produce highly characteristic MRI patterns, prototypically the DARS2, EARS, and AARS2 leukodystrophies, which are caused by mutations in mitochondrial aspartyl-tRNA synthetase, mitochondria glutamate tRNA synthetase, and mitochondrial alanyl-tRNA synthetase, respectively. The disease patterns emerging for these leukodystrophies are distinct in terms of the age of onset, nature of disease progression, and predominance of involved white matter tracts. In DARS2 and EARS2 disorders, earlier disease onset is typically correlated with more significant brain
https://jneurodevdisorders.biomedcentral.com/articles/10.1186/s11689-019-9292-y
British Library EThOS: Glycyl-tRNA synthetase mutations in neurological disease : mechanisms and modelsBritish Library EThOS: Glycyl-tRNA synthetase mutations in neurological disease : mechanisms and models
Charcot-Marie- Tooth disease type 2D (CMT2D) is a dominantly inherited axonal neuropathy caused by missense mutations in the glycyl-tRN A synthetase gene (CARS). Dominant mutations in tyrosyl-tRNA synthetase and alanyl-tRNA synthetase also cause CMT, suggesting a shared mechanism for all three diseases. The goal of this thesis was to investigate possible mechanisms and narrow the potential ways that mutations in CARS could lead to axon loss. GARS mutations are distributed throughout the protein in multiple functional domains. The localization, dimerization, and degradation of GARS were examined as in vitro measures of protein function. Dimer function was preserved in most mutants. Similarly, no differences in wild-type and mutant localization or degradation were seen. In vitro experiments did not show evidence of a loss of function in most GARS mutants. Progress has also been made towards the development of a Drosophila model of CMT2D. Overexpression of mutant Aats-gly, the Drosophila ortholog ...
https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.558205
dtd - D-aminoacyl-tRNA deacylase - Escherichia coli (strain K12) - dtd gene & proteindtd - D-aminoacyl-tRNA deacylase - Escherichia coli (strain K12) - dtd gene & protein
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
http://www.uniprot.org/uniprot/P0A6M4
Human AARS1 P49588 Information | Boster BioHuman AARS1 P49588 Information | Boster Bio
Human AARS1 Information And Facts | common name: AARS1. Catalyzes the attachment of alanine into tRNA(Ala) in a two-step response: alanine is first activated by ATP to form Ala- AMP and then transferred to the acceptor end of tRNA(Ala) (PubMed:27622773, PubMed:27911835, PubMed:28493438). Additionally edits incorrectly charged tRNA(Ala) via its editing domain (PubMed:27622773, PubMed:27911835, PubMed:28493438).
https://www.bosterbio.com/bosterbio-gene-info-cards/AARS1
alaS - Alanine--tRNA ligase - Aquifex aeolicus (strain VF5) - alaS gene & proteinalaS - Alanine--tRNA ligase - Aquifex aeolicus (strain VF5) - alaS gene & protein
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.
https://www.uniprot.org/uniprot/O67323
ENZYME entry 2.3.2.10ENZYME entry 2.3.2.10
L-alanyl-tRNA(Ala) + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine tRNA(Ala) + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-N(6)-(L-alanyl)-L-lysyl-D-alanyl-D- ...
https://enzyme.expasy.org/EC/2.3.2.10
PL-900 Power Platform Fundamentals Practice Tests ...
Come and prepare for the exam: PL-900 with practice Tests. Social Duty You can reach 100% discounted coupon codes of paid courses. All free courses for popular platforms such as Udemy, Coursera.
https://sosyalgorev.com/course/pl-900-power-platform-fundamentals-practice-tests-11255
Addgene: PL-452 N-CyPetAddgene: PL-452 N-CyPet
Plasmid PL-452 N-CyPet from Dr. Patrik Verstrekens lab contains the insert CyPet and is published in Nucleic Acids Res. 2008 Aug 1. ():. This plasmid is available through Addgene.
https://www.addgene.org/19171/
Accounting for horizontal gene transfers explains conflicting hypotheses regarding the position of aquificales in the phylogeny...Accounting for horizontal gene transfers explains conflicting hypotheses regarding the position of aquificales in the phylogeny...
Despite a large agreement between ribosomal RNA and concatenated protein phylogenies, the phylogenetic tree of the bacterial domain remains uncertain in its deepest nodes. For instance, the position of the hyperthermophilic Aquificales is debated, as their commonly observed position close to Thermotogales may proceed from horizontal gene transfers, long branch attraction or compositional biases, and may not represent vertical descent. Indeed, another view, based on the analysis of rare genomic changes, places Aquificales close to epsilon-Proteobacteria. To get a whole genome view of Aquifex relationships, all trees containing sequences from Aquifex in the HOGENOM database were surveyed. This study revealed that Aquifex is most often found as a neighbour to Thermotogales. Moreover, informational genes, which appeared to be less often transferred to the Aquifex lineage than non-informational genes, most often placed Aquificales close to Thermotogales. To ensure these results did not come from long branch
https://bmcevolbiol.biomedcentral.com/articles/10.1186/1471-2148-8-272
FRI0468 Long-Term Outcome of Pulmonary Function in the Anti-Synthetase Syndrome | Annals of the Rheumatic DiseasesFRI0468 Long-Term Outcome of Pulmonary Function in the Anti-Synthetase Syndrome | Annals of the Rheumatic Diseases
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). ...
http://ard.bmj.com/content/74/Suppl_2/597.1
Q18BE7 | alaS | Alanine--tRNA ligase | Druggability | CancerQ18BE7 | alaS | Alanine--tRNA ligase | Druggability | Cancer
casSAR Dugability of Q18BE7 | alaS | Alanine--tRNA ligase - Also known as SYA_CLOD6, alaS. 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.
https://cansarblack.icr.ac.uk/target/Q18BE7/synopsis
The distal hereditary motor neuropathies | Journal of Neurology, Neurosurgery & PsychiatryThe distal hereditary motor neuropathies | Journal of Neurology, Neurosurgery & Psychiatry
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, ...
https://jnnp.bmj.com/content/83/1/6?ijkey=3c991dcc9ece0403233c12f38a2622ad79252b61&keytype2=tf_ipsecsha
KEGG BRITE: KEGG Orthology (KO) - Brevibacillus brevis
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 ...
https://www.genome.jp/kegg-bin/get_htext?bbe00001+BBR47_00860
AARS Hot Topics - July 15, 2017 Issue | American Acne and Rosacea SocietyAARS Hot Topics - July 15, 2017 Issue | American Acne and Rosacea Society
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Anti-valyl tRNA synthetase antibody [VARSA7E6] (ab50898)Anti-valyl tRNA synthetase antibody [VARSA7E6] (ab50898)
Mouse monoclonal valyl tRNA synthetase antibody [VARSA7E6] validated for WB, Dot and tested in Human. Immunogen corresponding to recombinant fragment
http://www.abcam.com/valyl-trna-synthetase-antibody-varsa7e6-ab50898.html
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KEGG BRITE: KEGG Orthology (KO) - Halomonas chromatireducensKEGG BRITE: KEGG Orthology (KO) - Halomonas chromatireducens
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 ...
https://www.kegg.jp/kegg-bin/get_htext?hco00001+LOKO_02557
Emerging Technologies to Study Long Non-coding RNAs | SpringerLinkEmerging Technologies to Study Long Non-coding RNAs | SpringerLink
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
https://link.springer.com/chapter/10.1007/978-1-4614-8621-3_7
Anti-Glutamyl Prolyl tRNA synthetase antibody - N-terminal (ab71253)Anti-Glutamyl Prolyl tRNA synthetase antibody - N-terminal (ab71253)
Rabbit polyclonal Glutamyl Prolyl tRNA synthetase antibody validated for WB, IHC and tested in Human. With 4 independent reviews. Immunogen corresponding to…
http://www.abcam.com/glutamyl-prolyl-trna-synthetase-antibody-n-terminal-ab71253.html
Tryptophanyl tRNA synthetase Antibody (3A12) [PE] (H00007453-M02PE): Novus BiologicalsTryptophanyl tRNA synthetase Antibody (3A12) [PE] (H00007453-M02PE): Novus Biologicals
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Seryl tRNA synthetase Antibody (1H4) [DyLight 488] (H00006301-M01G): Novus BiologicalsSeryl tRNA synthetase Antibody (1H4) [DyLight 488] (H00006301-M01G): Novus Biologicals
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AARSD1 Polyclonal Antibody, FITC Conjugated | EpiGentekAARSD1 Polyclonal Antibody, FITC Conjugated | EpiGentek
Background Functions in trans to edit the amino acid moiety from incorrectly charged tRNA(Ala). Description AARSD1 Polyclonal Antibody, FITC Conjugated. FITC. Raised in Rabbit. Formulation Liquid. 0.03% Proclin 300. 50%...
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Aars | definition of Aars by Medical dictionaryAars | definition of Aars by Medical dictionary
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?
http://medical-dictionary.thefreedictionary.com/Aars
AARS Hot Topics - January 18, 2018 Issue | American Acne and Rosacea SocietyAARS Hot Topics - January 18, 2018 Issue | American Acne and Rosacea Society
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!
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Trans Globe Two Light Antique White White Marbleized Glass Bowl Flush Mount Antique White PL-13617 AW From Standard CollectionTrans Globe Two Light Antique White White Marbleized Glass Bowl Flush Mount Antique White PL-13617 AW From Standard Collection
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Tyrosyl tRNA synthetase抗体|Abcam中国|Anti-Tyrosyl tRNA synthetase抗体(ab31535)Tyrosyl tRNA synthetase抗体|Abcam中国|Anti-Tyrosyl tRNA synthetase抗体(ab31535)
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。
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Aminoacyl tRNA Synthetase - Proteopedia, life in 3DAminoacyl tRNA Synthetase - Proteopedia, life in 3D
Aminoacyl tRNA synthetase (aaRS) or tRNA ligase catalyzes the esterification of a specific amino acid to its cognate tRNA to form an aminoacyl-tRNA. The amino acid is transferred by the ribosome from the aminoacylated-tRNA onto a growing polypeptide chain. Class I of aaRS is a monomer or dimer, it has 2 highly conserved sequence motifs and it aminoacylates at the 2-OH of an adenosine nucleotide. Class II of aaRS is a dimer or tetramer, it has 3 highly conserved sequence motifs and it aminoacylates at the 3-OH of an adenosine nucleotide. CP1 domain of RS edits a mischarged aa-tRNA. Some of the crystal structures are complexes of the RS with their reactant analog: amino acid-sulfamoyl adenine (aa-SA).[1]. ...
https://proteopedia.org/wiki/index.php/Aminoacyl_tRNA_Synthetase
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Search Results
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 ...
http://stdgen.northwestern.edu/cgi-bin/gene_id_search.cgi?dbname=ngon&gene_id=NG1489
One ancestor for two codes viewed from the perspective of two complementary modes of tRNA aminoacylation | Biology Direct |...
The genetic code is brought into action by 20 aminoacyl-tRNA synthetases. These enzymes are evenly divided into two classes (I and II) that recognize tRNAs from the minor and major groove sides of the acceptor stem, respectively. We have reported recently that: (1) ribozymic precursors of the synthetases seem to have used the same two sterically mirror modes of tRNA recognition, (2) having these two modes might have helped in preventing erroneous aminoacylation of ancestral tRNAs with complementary anticodons, yet (3) the risk of confusion for the presumably earliest pairs of complementarily encoded amino acids had little to do with anticodons. Accordingly, in this communication we focus on the acceptor stem. Our main result is the emergence of a palindrome structure for the acceptor stems common ancestor, reconstructed from the phylogenetic trees of Bacteria, Archaea and Eukarya. In parallel, for pairs of ancestral tRNAs with complementary anticodons, we present updated evidence of concerted
https://0-biologydirect-biomedcentral-com.brum.beds.ac.uk/articles/10.1186/1745-6150-4-4
Histidyl TRNA Synthetase (HARS) ELISA KitsHistidyl TRNA Synthetase (HARS) ELISA Kits
Reaktivität: Rind (Kuh), Human, Maus. 6 verschiedene HARS ELISA Kits vergleichen. Alle direkt auf antikoerper-online.de bestellbar!
https://www.antikoerper-online.de/abstract/Histidyl+TRNA+Synthetase+
Buy Accessories, Covers & Popsockets Online in South Africa | FoschiniBuy Accessories, Covers & Popsockets Online in South Africa | Foschini
err: null, _dynSessConf: 8596754755371537637, data: { products: [ { id: 000003AARS6, name: Volkano Fashion Series Micro USB Cable , productId: 000003AARS6, categoryId:cat3360550, setCompare: true, productType:true, latestPriceRange: R 99.00, originalPriceRange: , isStrikeDownPrice:false, brand: Volkano, defaultImages: [ https://image.tfgmedia.co.za/image/1/process/259x259?source=https://cdn.tfgmedia.co.za/00/ProductImages/57588615.jpg ], swapImage: [ ], widgets: { 57588615 : { widget1URL: , widget2URL: , widget3URL: } }, colors: [ { id: 57588615, name: Multicolour, path: https://image.tfgmedia.co.za/image/1/process/30x30?source=https://cdn.tfgmedia.co.za/00/ProductImages/57588615_SW.jpg, hex: , swapImage: } ], isInCompareList: false, isChanelBrand: false, selectedColorIndex : 0, pdpLinkUrl: /pdp/volkano-fashion-series-micro-usb-cable/_/A-000003AARS6, collections: [] } , { id: ...
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Pulsed sonarPulsed sonar
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
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QARS mutations, tRNA, and neurodegeneration with migrating seizures | Beyond the Ion ChannelQARS mutations, tRNA, and neurodegeneration with migrating seizures | Beyond the Ion Channel
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 ...
http://epilepsygenetics.net/2014/04/14/qars-mutations-trna-and-neurodegeneration-with-migrating-seizures/
Item # PL-3209, PL-3209, Ethoxylated Bis Phenol A Dimethacrylate (EO = 6) On PL IndustriesItem # PL-3209, PL-3209, Ethoxylated Bis Phenol A Dimethacrylate (EO = 6) On PL Industries
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GOV :: Ostróda, Osterode i. Ostpr.GOV :: Ostróda, Osterode i. Ostpr.
OSTODEJO93XQ has 2004 postal code PL-14-100, has external reference SIMC:0964927, has name (in deu) Osterode i. Ostpr. says source_190237 (Ort 27.4), has name (in pol) Ostróda says source_190269, is (in deu) Stadt (Siedlung), is part of object_1074047, is part of object_190244 says source_190237 (Ort 27.4), located at 53.7°N 19.9667°O ...
http://gov.genealogy.net/item/show/OSTODEJO93XQ
Poland / Polska | IAMLPoland / Polska | IAML
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)
http://www.iaml.info/fr/national-branches/poland-polska?page=0%2C0
Alanine-tRNA ligaseAlanine-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- ...
https://en.wikipedia.org/wiki/Alanine—tRNA_ligase
AARS2AARS2
Alanyl-tRNA synthetase, mitochondrial, also known as alanine-tRNA ligase (AlaRS) or alanyl-tRNA synthetase 2 (AARS2), is an ... "Entrez Gene: alanyl-tRNA synthetase 2". Bonnefond L, Fender A, Rudinger-Thirion J, Giegé R, Florentz C, Sissler M (March 2005 ... "Toward the full set of human mitochondrial aminoacyl-tRNA synthetases: characterization of AspRS and TyrRS". Biochemistry. 44 ( ... "Toward the full set of human mitochondrial aminoacyl-tRNA synthetases: characterization of AspRS and TyrRS". Biochemistry. 44 ( ...
https://en.wikipedia.org/wiki/AARS2
Aspartate-tRNA(Asn) ligaseAspartate-tRNA(Asn) ligase
This enzyme participates in alanine and asparagine metabolism. Ibba M, Soll D (2000). "Aminoacyl-tRNA synthesis". Annual Review ... 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 ...
https://en.wikipedia.org/wiki/Aspartate—tRNA(Asn)_ligase
Aspartate-tRNA ligaseAspartate-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). ...
https://en.wikipedia.org/wiki/Aspartate—tRNA_ligase
Asparagine-tRNA ligaseAsparagine-tRNA ligase
This enzyme participates in alanine and aspartate metabolism and aminoacyl-trna biosynthesis. As of late 2007, 3 structures ... In enzymology, an asparagine-tRNA ligase (EC 6.1.1.22) is an enzyme that catalyzes the chemical reaction ATP + L-asparagine + ... and L-asparaginyl-tRNA(Asn). 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-asparagine:tRNAAsn ligase (AMP-forming). ...
https://en.wikipedia.org/wiki/Asparagine—tRNA_ligase
MorganellaceaeMorganellaceae
... histidine-tRNA ligase, and N-acetylmuramoyl-L-alanine amidase. These molecular signatures provide a novel and reliable means of ...
https://en.wikipedia.org/wiki/Morganellaceae
D-alanine-poly(phosphoribitol) ligaseD-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 ...
https://en.wikipedia.org/wiki/D-alanine—poly(phosphoribitol)_ligase
CaldibacillusCaldibacillus
O-succinylbenzoate-CoA ligase, tetratricopeptide repeat protein, d-alanyl-d-alanine carboxypeptidase, ribonuclease Z, late ... tRNA uridine-5- carboxymethylaminomethyl(34) synthesis enzyme MnmG, ...
https://en.wikipedia.org/wiki/Caldibacillus
List of EC numbers (EC 6)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 ...
https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_6)
List of MeSH codes (D08)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 ligase ... glutamate-trna ligase MeSH D08.811.464.263.200.350 - glycine-trna ligase MeSH D08.811.464.263.200.400 - histidine-trna ligase ... isoleucine-trna ligase MeSH D08.811.464.263.200.500 - leucine-trna ligase MeSH D08.811.464.263.200.550 - lysine-trna ligase ... serine-trna ligase MeSH D08.811.464.263.200.800 - threonine-tRNA ligase MeSH D08.811.464.263.200.850 - tryptophan-tRNA ligase ...
https://en.wikipedia.org/wiki/List_of_MeSH_codes_(D08)
Transfer-messenger RNATransfer-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 ...
https://en.wikipedia.org/wiki/Transfer-messenger_RNA
Asparaginyl-tRNA synthase (glutamine-hydrolysing)Asparaginyl-tRNA synthase (glutamine-hydrolysing)
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds carbon-nitrogen ligases with ... This enzyme participates in glutamate metabolism and alanine and aspartate metabolism. Min B, Pelaschier JT, Graham DE, Tumbula ... aspartyl-tRNA(Asn), and L-glutamine, whereas its 4 products are ADP, phosphate, asparaginyl-tRNA(Asn), and L-glutamate. ... In enzymology, an asparaginyl-tRNA synthase (glutamine-hydrolysing) (EC 6.3.5.6) is an enzyme that catalyzes the chemical ...
https://en.wikipedia.org/wiki/Asparaginyl-tRNA_synthase_(glutamine-hydrolysing)
Glutaminyl-tRNA synthase (glutamine-hydrolysing)Glutaminyl-tRNA synthase (glutamine-hydrolysing)
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds carbon-nitrogen ligases with ... This enzyme participates in glutamate metabolism and alanine and aspartate metabolism. Horiuchi KY, Harpel MR, Shen L, Luo Y, ... glutamyl-tRNA(Gln), and L-glutamine, whereas its 4 products are ADP, phosphate, glutaminyl-tRNA(Gln), and L-glutamate. ... Ibba M, Soll D (2000). "Aminoacyl-tRNA synthesis". Annu. Rev. Biochem. 69: 617-50. doi:10.1146/annurev.biochem.69.1.617. PMID ...
https://en.wikipedia.org/wiki/Glutaminyl-tRNA_synthase_(glutamine-hydrolysing)
SelenocysteineSelenocysteine
The selenocysteine tRNAs are initially charged with serine by seryl-tRNA ligase, but the resulting Ser-tRNASec is not used for ... Selenocysteine is decomposed by the enzyme selenocysteine lyase into L-alanine and selenide. As of 2021[update], 136 human ... two enzymes are required to convert tRNA-bound seryl residue into tRNA selenocysteinyl residue: PSTK (O-phosphoseryl-tRNA[Ser] ... The primary and secondary structure of selenocysteine-specific tRNA, tRNASec, differ from those of standard tRNAs in several ...
https://en.wikipedia.org/wiki/Selenocysteine
List of biomoleculesList of biomolecules
... in this case alanine). Lactase Lactic acid Lactose Lanolin Lauric acid Lectin Leptin Leptomycin B Leucine Leukotriene Ligase ... tRNA) Triacsin C Thyroid-stimulating hormone (TSH) Thyrotropin-releasing hormone (TRH) Thyroxine (T4) Tocopherol (Vitamin E) ... prefix such as L-alanine or DL-alanine, please see the parent page ( ... Aequorin Aflatoxin Agar Alamethicin Alanine Albumins Aldosterone Aleurone Alpha-amanitin Alpha-MSH (Melaninocyte stimulating ...
https://en.wikipedia.org/wiki/List_of_biomolecules
List of EC numbers (EC 4)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 lyase EC 4.6.1.17: cyclic pyranopterin monophosphate synthase * EC 4.6.1.18: pancreatic ribonuclease * EC 4.6.1.19 ... heme ligase EC 4.99.1.9:: coproporphyrin ferrochelatase * EC 4.99.1.10: magnesium dechelatase * EC 4.99.1.11: sirohydrochlorin ... tRNA 4-demethylwyosine synthase (AdoMet-dependent) * EC 4.1.3.45: 3-hydroxybenzoate synthase * EC 4.1.3.46: (R)-citramalyl-CoA ...
https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_4)
N-end ruleN-end rule
The removal of the methionine is more efficient when the second residue is small and uncharged (for example alanine), but ... In eukaryotic cells, these N-terminal residues are recognized and targeted by ubiquitin ligases, mediating ubiquitination ... destabilising residues are modified by the attachment of a Primary destabilising residue by the enzyme leucyl/phenylalanyl-tRNA ... This study revealed that Alanine, Serine, Threonine, and Valine were the most abundant N-terminal residues, while Leucine, ...
https://en.wikipedia.org/wiki/N-end_rule
TRNA-intron endonucleaseTRNA-intron endonuclease
Popow J, Schleiffer A, Martinez J (August 2012). "Diversity and roles of (t)RNA ligases". Cellular and Molecular Life Sciences ... leading to a substitution at position 307 of alanine by serine. This mutation causes destabilization of the β-β-interaction, ... The use of tRNA-intron endonuclease in pre-tRNA intron excision is just one of the steps for tRNA maturation. pre-tRNAs undergo ... tRNA-intron lyase (EC 4.6.1.16, tRNA intron endonuclease, transfer ribonucleate intron endoribonuclease, tRNA splicing ...
https://en.wikipedia.org/wiki/TRNA-intron_endonuclease
List of EC numbers (EC 3)List of EC numbers (EC 3)
... alanine carboxypeptidase EC 3.4.17.7: Now EC 3.5.1.28, N-acetylmuramoyl-L-alanine amidase EC 3.4.17.8: muramoylpentapeptide ... tRNA(adenine34) deaminase * EC 3.5.4.34: tRNAAla(adenine37) deaminase * EC 3.5.4.35: tRNA(cytosine8) deaminase * EC 3.5.4.36: ... glutamateammonia ligase] phosphorylase EC 3.1.4.16: 2′,3′-cyclic-nucleotide 2′-phosphodiesterase EC 3.1.4.17: 3′,5′-cyclic- ... alanine carboxypeptidase EC 3.4.17.7: Now EC 3.5.1.28, N-acetylmuramoyl-L-alanine amidase EC 3.4.17.8: muramoylpentapeptide ...
https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_3)
MitochondrionMitochondrion
Mitochondrial tRNA genes have different sequences from the nuclear tRNAs, but lookalikes of mitochondrial tRNAs have been found ... which converts lactate and de-aminated alanine into glucose, under the influence of high levels of glucagon and/or epinephrine ... kynurenine hydroxylase and fatty acid Co-A ligase. Disruption of the outer membrane permits proteins in the intermembrane space ... It encodes 37 genes: 13 for subunits of respiratory complexes I, III, IV and V, 22 for mitochondrial tRNA (for the 20 standard ...
https://en.wikipedia.org/wiki/Mitochondrion
List of enzymesList of enzymes
L-firefly luciferin-CoA ligase EC 6.2.1.53: L-proline-L-prolyl-carrier protein ligase EC 6.2.1.54: D-alanine-D-alanyl-carrier ... L-seryl-tRNA(Sec) selenium transferase EC 2.9.1.2: O-phospho-L-seryl-tRNA(Sec):L-selenocysteinyl-tRNA synthase Hydrolytic ... Glutarate-CoA ligase EC 6.2.1.7: Cholate-CoA ligase EC 6.2.1.8: Oxalate-CoA ligase EC 6.2.1.9: Malate-CoA ligase EC 6.2.1.10: ... ligase EC 6.2.1.23: Dicarboxylate-CoA ligase EC 6.2.1.24: Phytanate-CoA ligase EC 6.2.1.25: Benzoate-CoA ligase EC 6.2.1.26: o- ...
https://en.wikipedia.org/wiki/List_of_enzymes
Chromosome 2Chromosome 2
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 ...
https://en.wikipedia.org/wiki/Chromosome_2
Artificial gene synthesisArtificial gene synthesis
Taq DNA ligase repairs the nicks on both DNA strands. Because the T5 exonuclease is heat labile, it is inactivated at 50 °C ... 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". Journal of Molecular Biology. 72 ( ... Next, each linker part is attached to its respective DNA part by incubating with T4 DNA ligase. Each DNA part will have a ...
https://en.wikipedia.org/wiki/Artificial_gene_synthesis
List of EC numbers (EC 2)List of EC numbers (EC 2)
... glutamate-tRNA ligase, EC 1.2.1.70, glutamyl-tRNA reductase and EC 5.4.3.8 EC 2.7.2.14: branched-chain-fatty-acid kinase EC 2.7 ... D-alanine 2-hydroxymethyltransferase EC 2.1.2.8: deoxycytidylate 5-hydroxymethyltransferase EC 2.1.2.9: methionyl-tRNA ... tRNA (guanine46-N7)-methyltransferase EC 2.1.1.34: tRNA (guanosine18-2′-O)-methyltransferase EC 2.1.1.35: tRNA (uracil54-C5)- ... tRNA (guanine110-N2)-dimethyltransferase EC 2.1.1.214: tRNA (guanine10-N2)-methyltransferase EC 2.1.1.215: tRNA (guanine26-N2/ ...
https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)
HOMD :: SEQF2940HOMD :: SEQF2940
Alanine--tRNA ligase. 183. SEQF2940,KI515728.1. SEQF2940_00186 jb [NA] [AA] 1386/461. 187677-186292. putative AAA domain- ... Aspartate--tRNA(Asp/Asn) ligase. 186. SEQF2940,KI515728.1. SEQF2940_00189 jb [NA] [AA] 933/310. 191067-191999. hypothetical ... Histidine--tRNA ligase. 191. SEQF2940,KI515728.1. SEQF2940_00194 jb [NA] [AA] 636/211. 197458-196823. Hydroxyacylglutathione ... Pup--protein ligase. 70. SEQF2940,KI515728.1. SEQF2940_00072 jb [NA] [AA] 192/63. 69135-68944. Prokaryotic ubiquitin-like ...
https://www.homd.org/genome/explorer?gid=SEQF2940&anno=prokka
HOMD :: SEQF2448HOMD :: SEQF2448
Alanine--tRNA ligase. 7. SEQF2448,KI273076.1. SEQF2448_00007 jb [NA] [AA] 1155/384. 4062-2908. Glycerate 2-kinase. ... tRNA ligase alpha subunit. 96. SEQF2448,KI273077.1. SEQF2448_00098 jb [NA] [AA] 2427/808. 85828-88254. Phenylalanine--tRNA ... D-alanyl-D-alanine carboxypeptidase DacB. 20. SEQF2448,KI273076.1. SEQF2448_00020 jb [NA] [AA] 1416/471. 19857-21272. ... Putative TrmH family tRNA/rRNA methyltransferase. 118. SEQF2448,KI273077.1. SEQF2448_00121 jb [NA] [AA] 1014/337. 112542-113555 ...
https://homd.org/genome/explorer?gid=SEQF2448&anno=prokka
Code System Concept
Alanyl-tRNA synthetase Active Synonym false false 2971540018 Alanine-transfer ribonucleic acid ligase Active Synonym false ... Alanine-transfer ribonucleic acid ligase (substance). Code System Preferred Concept Name. Alanine-transfer ribonucleic acid ... Alanine-tRNA ligase Active Synonym false false 113649019 ...
https://phinvads.cdc.gov/vads/ViewCodeSystemConcept.action?oid=2.16.840.1.113883.6.96&code=68429002
DeCSDeCS
Alanine-tRNA ligase - Concept préféré Concept UI. M0000623. Terme préféré. Alanine-tRNA ligase ... Alanine-tRNA ligase Descripteur en anglais: Alanine-tRNA Ligase Descripteur en espagnol: Alanina-ARNt Ligasa Espagnol dEspagne ... An enzyme that activates alanine with its specific transfer RNA. EC 6.1.1.7.. ... Alanina-tRNA Ligase Synonymes:. Alanine-ARNt ligase. Alanine-ARNt synthétase. Alanyl-ARNt synthétase. ...
https://decs.bvsalud.org/fr/ths/resource/?id=415
UBCG] Gene set - EzBioCloud Help centerUBCG] Gene set - EzBioCloud Help center
Alanine-tRNA ligase. argS. J. COG0018. TIGR00456. Arginine-tRNA ligase. aspS. J. COG0173. TIGR00459. Aspartate-tRNA ligase. ... Histidine-tRNA ligase. ileS. J. COG0060. TIGR00392. Isoleucine-tRNA ligase 1. infB. J. COG0532. TIGR00487. Translation ... Phenylalanine-tRNA ligase alpha subunit. pheT. J. COG0073. TIGR00472. Phenylalanine-tRNA ligase beta subunit. ...
https://help.ezbiocloud.net/ubcg-gene-set/
HOMD :: SEQF1909HOMD :: SEQF1909
Alanine--tRNA ligase. 199. SEQF1909,AJZR01000006.1. SEQF1909_00205 jb [NA] [AA] 564/187. 96983-97546. Acyl carrier protein ... Phenylalanine--tRNA ligase alpha subunit. 39. SEQF1909,AJZR01000002.1. SEQF1909_00039 jb [NA] [AA] 2442/813. 37456-39897. ... Alanine racemase 1. 123. SEQF1909,AJZR01000006.1. SEQF1909_00128 jb [NA] [AA] 768/255. 15711-14944. 2%2C3-dehydroadipyl-CoA ... D-alanyl-D-alanine carboxypeptidase. 138. SEQF1909,AJZR01000006.1. SEQF1909_00144 jb [NA] [AA] 876/291. 31939-31064. Succinate ...
https://ehomd.org/genome/explorer?gid=SEQF1909&anno=prokka
Network Portal - Function aminoacyl-tRNA ligase activity
alanine-tRNA ligase activity. GO:0004814. arginine-tRNA ligase activity. GO:0004815. aspartate-tRNA ligase activity. ... aminoacyl-tRNA ligase activity. id: GO:0004812. name: aminoacyl-tRNA ligase activity. namespace: molecular_function. type: go. ... Description: Catalysis of the formation of aminoacyl-tRNA from ATP, amino acid, and tRNA with the release of diphosphate and ... valine-tRNA ligase activity. GO:0043767. pyrrolysyl-tRNA synthetase activity. GO:0043816. phosphoserine-tRNA(Cys) ligase ...
http://networks.systemsbiology.net/function/GO:0004812/
SustainPineDB
alanine-tRNA ligase activity GO:0004813 Molecular Function 0.0. - Sma3. ionotropic glutamate receptor activity GO:0004970 ... alanyl-tRNA aminoacylation GO:0006419 Biological Process 0.0. - Sma3. protein phosphorylation GO:0006468 Biological Process 0.0 ...
https://www.scbi.uma.es/sustainpinedb/unigens/28?tab=ung&ung_id=1352436
Protein OntologyProtein Ontology
alanine--tRNA ligase, cytoplasmic isoform 1 (mouse). organism-sequence. PR:000050486 alanine--tRNA ligase, cytoplasmic isoform ...
https://proconsortium.org/cgi-bin/browser_pro?quick_browse=Methylated_forms
lcl|LHPG02000004.1 cds PRW59070.1 7315 details
aminoacyl-tRNA ligase activity. IEP. Enrichment. MF. GO:0004813. alanine-tRNA ligase activity. IEP. Enrichment. ... ligase activity, forming carbon-oxygen bonds. IEP. Enrichment. MF. GO:0017111. nucleoside-triphosphatase activity. IEP. ...
https://protists.sbs.ntu.edu.sg/sequence/view/62713
CCL20590 details
aminoacyl-tRNA ligase activity. IEP. Enrichment. MF. GO:0004813. alanine-tRNA ligase activity. IEP. Enrichment. ... catalytic activity, acting on a tRNA. IEP. Enrichment. BP. GO:1901360. organic cyclic compound metabolic process. IEP. ...
https://bacteria.sbs.ntu.edu.sg/sequence/view/5245
Systematic identification of miRNA-regulatory networks unveils their potential roles in sugarcane response to Sorghum mosaic...Systematic identification of miRNA-regulatory networks unveils their potential roles in sugarcane response to Sorghum mosaic...
... alanine-tRNA ligase, chloroplastic; ELP6, elongator complex protein 6; NAC078, NAC domain-containing protein 78; rbcLBP, ...
https://bmcplantbiol.biomedcentral.com/articles/10.1186/s12870-022-03641-6/figures/3
ANKRD16 prevents neuron loss caused by an editing-defective tRNA synthetase<...
Alanine-tRNA Ligase Medicine & Life Sciences 100% * Amino Acyl-tRNA Synthetases Medicine & Life Sciences 99% ... Editing domains of aminoacyl tRNA synthetases correct tRNA charging errors to maintain translational fidelity. A mutation in ... N2 - Editing domains of aminoacyl tRNA synthetases correct tRNA charging errors to maintain translational fidelity. A mutation ... AB - Editing domains of aminoacyl tRNA synthetases correct tRNA charging errors to maintain translational fidelity. A mutation ...
https://utsouthwestern.pure.elsevier.com/en/publications/ankrd16-prevents-neuron-loss-caused-by-an-editing-defective-trna-
PathBankPathBank
Matched Proteins: Leucine-, isoleucine-, valine-, threonine-, and alanine-binding protein … Leucine--tRNA ligase … Valine--tRNA ...
https://pathbank.org/search?q=valine+AND+leucine
ISMARA results: CEBPBISMARA results: CEBPB
threonine-tRNA ligase activity(GO:0004829). 0.0. 0.1. GO:0004813. alanine-tRNA ligase activity(GO:0004813). ... glutamate-tRNA ligase activity(GO:0004818) proline-tRNA ligase activity(GO:0004827). ... glutamine-tRNA ligase activity(GO:0004819) leucine-tRNA ligase activity(GO:0004823). ... isoleucine-tRNA ligase activity(GO:0004822). 0.0. 0.0. GO:1990259. protein-glutamine N-methyltransferase activity(GO:0036009) ...
https://www.ismara.unibas.ch/ISMARA/scratch/NHBE_SC2/ismara_report/pages/CEBPB.html
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... kiaa1048aarshuman alanine‑‑trna ligase, cytoplasmiccmt2n, syacпоказать ещё 19 строк. Generally, animal-based proteins (meat, ...
https://www.cleancoatspaintingllc.com/forum/welcome-to-the-forum/en-donde-puedo-comprar-esteroides-en-guatemala-steroider-online-kob-sm-bodybuilding-2022-resultat
MMTBMMTB
6.1.1.15 proline---tRNA ligase 6.1.1.20 phenylalanine---tRNA ligase 6.1.1.6 lysine---tRNA ligase 6.1.1.7 alanine---tRNA ligase ... tRNAMet + L-alanine + ATP <=> L-alanyl-[tRNAAla] + diphosphate + AMP 6.1.1.7 alanine---tRNA ligase - M ... ATP + L-alanine + anticapsin <=> ADP + phosphate + L-alanyl-L-anticapsin + H+ 6.3.2.49 L-alanine---L-anticapsin ligase - BMK ... L-glutamate + L-alanine + ATP <=> gamma-L-glutamyl-D-alanine + ADP + phosphate + H+ 6.3.2.2 glutamate---cysteine ligase - ...
https://metano.tu-bs.de/search/L-alanine%20=
Model Search | BioModelsModel Search | BioModels
Alanine--tRNA ligase, mitochondrial (4) * 1,3-beta-glucan synthase component FKS1 (4) ... Glutamate--tRNA ligase, mitochondrial (4) * High-affinity glucose transporter HXT2 (4) * Tyrosine--tRNA ligase, mitochondrial ( ... Phenylalanine--tRNA ligase beta subunit (4) * Phenylalanine--tRNA ligase alpha subunit (4) ...
https://www.ebi.ac.uk/biomodels/search?query=CHEBI:CHEBI:16566
AARS Gene - genomics-online.com | cDNA | ORF | Primers | KitsAARS Gene - genomics-online.com | cDNA | ORF | Primers | Kits
alanine--tRNA ligase. *transfer RNA-Ala synthetase. Proteomics products related to AARS Gene. Other products related to AARS ... AARS (Alanyl tRNA Synthetase, AARS). Short Description: The human alanyl-tRNA synthetase (AARS) belongs to a family of tRNA ... tRNA synthases are the enzymes that interpret the RNA code and attach specific aminoacids to the tRNAs that contain the cognate ... Class II tRNA synthases evolved early in evolution and are highly conserved. This is reflected by the fact that 498 of the 968- ...
https://www.genomics-online.com/gene-index-a/aars/
Búsqueda | BVS BoliviaBúsqueda | BVS Bolivia
The study identified alanine, serine and glycine tRNA ligases for the first time and also showed their up-regulation on day 7 ... The amino acid repeat of fibroin protein is enriched with the three amino acids, glycine, serine and alanine. The identified ...
https://pesquisa.bvsalud.org/bolivia/?lang=es&q=au:Mamillapalli,+Anitha
Domain IPR003439:ABC transporter-likeDomain IPR003439:ABC transporter-like
Alanine-tRNA ligase, class IIc 32 Domain IPR015879:Aromatic-ring-hydroxylating dioxygenase, alpha subunit, C-terminal domain 32 ... D-alanine--D-alanine ligase/VANA/B/C, conserved site 37 Family IPR006127:Periplasmic solute binding protein, ZnuA-like 37 ... D-alanine--D-alanine ligase, N-terminal domain 34 Domain IPR001086:Prephenate dehydratase 34 Domain IPR004150:NAD-dependent DNA ... D-alanine--D-alanine ligase 28 Domain IPR012792:3-oxoacid CoA-transferase, subunit A 28 Family IPR003170:UDP-N- ...
https://www.cbrc.kaust.edu.sa/aamg/1502720332816_CamiLowProdigalV2_40.0_intikhab/WWWAAMG/visuals/CamiLowProdigalV2_AAMG_DOMAINS_data_summary.txt
ALA1 - LEU4 | S. cerevisiae SSL interaction - SlorthALA1 - LEU4 | S. cerevisiae SSL interaction - Slorth
aminoacyl-tRNA ligase activity. alanine-tRNA ligase activity. ATP binding. nucleotide binding. nucleic acid binding. ligase ... tRNA binding. amino acid binding. metal ion binding. ligase activity. RNA binding. AARS2 (H. sapiens). AARS (H. sapiens). ... activity, forming aminoacyl-tRNA and related compounds. ...
http://rails.biochem.susx.ac.uk/interactions/633447
Genes | Free Full-Text | Impacts of the Type I Toxin-Antitoxin System, SprG1/SprF1, on Staphylococcus aureus Gene ExpressionGenes | Free Full-Text | Impacts of the Type I Toxin-Antitoxin System, SprG1/SprF1, on Staphylococcus aureus Gene Expression
Alanine dehydrogenase 2 (Ald2). Q99TF4. 1.86 ↓. 7. Phenylalanine--tRNA ligase α subunit (PheS). P68848. 1.55 ↓. ... Glutamate----tRNA ligase (GltX). P99170. 1.74 ↓. 1.72 ↓. 2. 1-pyrroline-5-carboxylate dehydrogenase (RocA). P99076. 1.96 ↓. ... Succinate--CoA ligase (ADP-forming) subunit α (SucD). P99070. 1.55 ↓. 3. Putative peptidyl-prolyl cis-trans isomerase (PpiB). ... Formate--tetrahydrofolate ligase (FHS). Q7A535. 3.41 ↓. 2.75 ↓. 18. Phosphoenolpyruvate-protein phosphotransferase (PtsI). ...
https://www.mdpi.com/2073-4425/12/5/770/htm
SCOP 1.57: Superfamily c.26.1: Nucleotidylyl transferaseSCOP 1.57: Superfamily c.26.1: Nucleotidylyl transferase
c.26.1.4: Pantothenate synthetase (Pantoate-beta-alanine ligase, PanC) [63976] (1 protein). ... c.26.1.1: Class I aminoacyl-tRNA synthetases (RS), catalytic domain [52375] (8 proteins). ...
https://scop.berkeley.edu/sunid=52374&ver=1.57
SMART: Pfam domain Anticodon 1SMART: Pfam domain Anticodon 1
The aminoacyl-tRNA synthetases (also known as aminoacyl-tRNA ligases) catalyse the attachment of an amino acid to its cognate ... The synthetases specific for alanine, asparagine, aspartic acid, glycine, histidine, phenylalanine, proline, serine, threonine ... In reactions catalysed by the class I aminoacyl-tRNA synthetases, the aminoacyl group is coupled to the 2-hydroxyl of the tRNA ... Based on their mode of binding to the tRNA acceptor stem, both classes of tRNA synthetases have been subdivided into three ...
https://smart.embl.de/smart/do_annotation.pl?DOMAIN=Pfam:Anticodon_1&START=983&END=1138&E_VALUE=2.6e-34&TYPE=PFAM&BLAST=DRWIRSRLTEAVRLSNEGFQAYDFPAITTAQYSFWLYELCDVYLECLKPVLNGVDQVAAECARQTLYTCLDVGLRLLSPFMPFVTEELFQRLPRRTPKAPASLCVTPYPEPSECSWKDPEAEAALELALSITRAVRSLRADYNLTRTRPDCFLEVA
SMPDBSMPDB
tRNA(Met). Selenomethionyl-. tRNA(Met). Aspartate. Metabolism. Glutamate. Metabolism. Alanine. Metabolism. D-Arginine and. D- ... tRNA ligase,. cytoplasmic. Bifunctional. 3-. phosphoadenosine. 5-. phosphosulfate. synthase 1. Bifunctional. 3-. ... Alanine. Metabolism. D-Arginine and. D-Ornithine. Metabolism. Internal. digestion and. absorption. ... L-Alanine. Selenite. Selenite. Se-Methylselenocysteine. Se-Methylselenocysteine. Selenocysteine. Selenocysteine. Hydrogen ...
https://smpdb.ca/view/SMP0000029?highlight%5Bcompounds%5D%5B%5D=DB00131&highlight%5Bproteins%5D%5B%5D=DB00131
A systems biology approach to investigate the response of Synechocystis sp. PCC6803 to a high salt environment | Aquatic...A systems biology approach to investigate the response of Synechocystis sp. PCC6803 to a high salt environment | Aquatic...
Cell envelope enzyme UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diamino-pimelate-D-alanyl-D-alanine ligase (p+ = NA, 0.9918) is ... the 1.83 and 2.32-fold induction of glutamyl-tRNA synthetase (p+ = 1, 0.99394) has been observed previously in the long-term [ ... Smith CA: Structure, function and dynamics in the mur family of bacterial cell wall ligases. J Mol Biol. 2006, 362: 640-655. ... ammonia ligase (p+ = NA, 0.9965), which functions in the same pathway. Both proteins have not previously been identified in the ...
https://aquaticbiosystems.biomedcentral.com/articles/10.1186/1746-1448-5-8
Ligase - WikipédiaLigase - Wikipédia
... alanine ligase EC 6.3.2.2 glutamate-cysteine ligase EC 6.3.2.3 glutathione synthase EC 6.3.2.4 D-alanine-D-alanine ligase EC ... EC 6.3.4.17 formate-dihydrofolate ligase EC 6.3.4.18 5-(carboxyamino)imidazole ribonucleotide synthase EC 6.3.4.19 tRNAIle- ... γ-L-glutamate ligase EC 6.3.2.35 D-alanine-D-serine ligase EC 6.3.2.36 4-phosphopantoate-β-alanine ligase EC 6.3.2.37 UDP-N- ... ARNt ligase EC 6.1.1.6 lysine ARNt ligase EC 6.1.1.7 alanine ARNt ligase EC 6.1.1.8 supprimé EC 6.1.1.9 valine ARNt ligase EC ...
https://fr.m.wikipedia.org/wiki/Ligase
SynthetaseAminoacyl tRNA syntheThreonineEnzymesAmino acidCysteineMRNAGeneRRNAIsoleucineCatalyseBiosynthesisAcceptorSynthaseLeucylHydrolysisActivityEnzymeSerineGlutamineInvolvesReactionsClass IIProcessSynthetaseMitochondrialSubunitCysteine-tRNA lAminoacyl-tRNA syntheAaRSDiphthine-ammoniAminoacylationHistidineCognateUbiquitin ligaseSynthetasesGenesRibosomeAttachmentProteinsCatalyzes
Synthetase5
  • A mutation in the editing domain of alanyl tRNA synthetase (AlaRS) in Aars sti mutant mice results in an increase in the production of serine-mischarged tRNA Ala and the degeneration of cerebellar Purkinje cells. (elsevier.com)
  • These results identify an amino-acid-accepting co-regulator of tRNA synthetase editing as a new layer of the machinery that is essential to the prevention of severe pathologies that arise from defects in editing. (elsevier.com)
  • A mutation in the editing domain of alanyl tRNA synthetase (AlaRS) in Aarssti mutant mice results in an increase in the production of serine-mischarged tRNAAla and the degeneration of cerebellar Purkinje cells. (elsevier.com)
  • The human alanyl-tRNA synthetase (AARS) belongs to a family of tRNA synthases, of the class II enzymes. (genomics-online.com)
  • These enzymes are involved in joining together 2 substrates e.g., alanyl-t-RNA synthetase, glutamine synthetase, DNA ligases. (amano-enzyme.com)
Aminoacyl tRNA synthe3
  • Editing domains of aminoacyl tRNA synthetases correct tRNA charging errors to maintain translational fidelity. (elsevier.com)
  • The 20 aminoacyl-tRNA synthetases are divided into two classes, I and II. (embl.de)
  • In reactions catalysed by the class I aminoacyl-tRNA synthetases, the aminoacyl group is coupled to the 2'-hydroxyl of the tRNA, while, in class II reactions, the 3'-hydroxyl site is preferred. (embl.de)
Threonine1
  • Compositional properties of Threonine--tRNA ligase (bottom) versus UniprotKB/SwissProt (top). (ucy.ac.cy)
Enzymes5
  • tRNA synthases are the enzymes that interpret the RNA code and attach specific aminoacids to the tRNAs that contain the cognate trinucleotide anticodons. (genomics-online.com)
  • Le nom courant des enzymes de type ligase inclut souvent le terme « ligase » comme l' ADN ligase du phage T4 utilisée pour structurer des fragments d' ADN . (wikipedia.org)
  • Attention cependant à ne pas confondre les enzymes synthétases avec les enzymes synthases (qui sont toutes deux des enzymes du groupe des ligases). (wikipedia.org)
  • Les ligases sont classées EC 6 dans la nomenclature EC des enzymes. (wikipedia.org)
  • These enzymes catalyze the transfer of a particular group from one substrate to another e.g., aspartate amino transferase (AST), alanine aminotransferase (ALT), hexokinase, phosphoglucomutase, hexose- 1-phosphate uridyltransferase, ornithine carbamoyl transferase etc. (amano-enzyme.com)
Amino acid5
  • Catalysis of the formation of aminoacyl-tRNA from ATP, amino acid, and tRNA with the release of diphosphate and AMP. (systemsbiology.net)
  • They consist of a catalytic domain which interacts with the amino acid acceptor-T psi C helix of the tRNA, and a second domain which interacts with the rest of the tRNA structure. (genomics-online.com)
  • This helps bind amino-acid to tRNA. (studyread.com)
  • We then establish a genetic firewall by discovering viral tRNAs that provide exceptionally efficient codon reassignment allowing us to develop cells bearing an amino acid-swapped genetic code that reassigns two of the six serine codons to leucine during translation. (bvsalud.org)
  • E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. (cusabio.com)
Cysteine2
  • As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. (string-db.org)
  • Catalyzes the removal of elemental sulfur atoms from cysteine to produce alanine. (cusabio.com)
MRNA1
  • Another undetectable mRNA existing addition was that transition receptor ligase NCAPD2 and NCAPH are complete upon contraction transcription, frequently by forest or formalism replication( Matsuoka et al. (evakoch.com)
Gene1
  • Here we show that such mobile transfer RNAs (tRNAs) enable gene transfer and allow viral replication in Escherichia coli despite the genome-wide removal of 3 of the 64 codons and the previously essential cognate tRNA and release factor genes. (bvsalud.org)
RRNA1
Isoleucine1
  • Catalyzes the attachment of isoleucine to tRNA(Ile). (string-db.org)
Catalyse1
  • En biochimie , une ligase est une enzyme qui catalyse la jonction de deux molécules (en anglais ligation ) par de nouvelles liaisons covalentes avec hydrolyse concomitante de l' ATP ou d'autres molécules similaires. (wikipedia.org)
Biosynthesis1
  • Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. (cusabio.com)
Acceptor1
  • Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). (string-db.org)
Synthase1
  • En fait la synthase forme et défait les doubles liaisons d'une protéine. (wikipedia.org)
Leucyl1
  • This domain is found methionyl, valyl, leucyl and isoleucyl tRNA synthetases. (embl.de)
Hydrolysis1
  • One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. (string-db.org)
Activity1
  • Replacement of individual amino acids of the 3His/1Glu metal binding motif by alanine drastically reduced or abolished quercetinase activity and affected its structural integrity. (biomedcentral.com)
Enzyme2
  • An enzyme that activates alanine with its specific transfer RNA. (bvsalud.org)
  • In fact, the origins of the word "Enzyme" derive from Greek: "en" (in) and "zyme" (ferment). (amano-enzyme.com)
Serine1
  • Serine that is misactivated by AlaRS is captured by the lysine side chains of ANKRD16, which prevents the charging of serine adenylates to tRNA Ala and precludes serine misincorporation in nascent peptides. (elsevier.com)
Glutamine1
  • EC 6.3.5 Carbone-Azote Ligases avec Glutamine comme Amido-N-Donneur. (wikipedia.org)
Involves1
  • However, tRNA binding involves an alpha-helical structure that is conserved between class I and class II synthetases. (embl.de)
Reactions1
  • L-alanine = 499 reactions were found. (tu-bs.de)
Class II1
  • Class II tRNA synthases evolved early in evolution and are highly conserved. (genomics-online.com)
Process1
  • As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. (string-db.org)
Synthetase13
  • CDC64 encodes cytoplasmic alanyl-tRNA synthetase, Ala1p, of Saccharomyces cerevisiae. (tamu.edu)
  • We report that CDC64 encodes Ala1p, an alanyl-tRNA synthetase. (tamu.edu)
  • The protein encoded by this gene belongs to the class-II aminoacyl-tRNA synthetase family. (nih.gov)
  • Protein biosynthesis.aminoacyl-tRNA synthetase. (ntu.edu.sg)
  • threonyl-tRNA synthetase, putative / threonine--tRNA. (ntu.edu.sg)
  • Sequence and structural studies show that two highly conserved amino acid residues, Asp and Asn, in the tRNA-binding domain of alanyl-tRNA synthetase (AlaRS) are responsible for recognition of the canonical identity elements G3:U70. (ncu.edu.tw)
  • This domain is found at the amino terminus of Arginyl tRNA synthetase, also called additional domain 1 (Add-1). (embl.de)
  • Crystal structure of arginyl-tRNA synthetase from Klebsiella pneumoniae subsp. (embl.de)
  • Mutations in the nuclear encoded mitochondrial arginyl- tRNA synthetase gene underlie PCH6. (biomedcentral.com)
  • The tRNA splicing endonuclease, the mitochondrial arginyl- tRNA synthetase and the vaccinia related kinase1 are mutated in the minority of PCH1 cases. (biomedcentral.com)
  • In this review we describe the neuroradiological, neuropathological, clinical and genetic features of the different PCH subtypes and we report on in vitro and in vivo studies on the tRNA splicing endonuclease and mitochondrial arginyl-tRNA synthetase and discuss their relation to pontocerebellar hypoplasia. (biomedcentral.com)
  • Ito, K., Kawakami, K., and Nakamura, Y. (1993) Multiple control of Escherichia coli lysyl-tRNA synthetase expression involves a transcriptional repressor and a translational enhancer element. (zfin.org)
  • Nakamura, Y., and Kawakami, K. (1992) Overproduction and purification of lysyl-tRNA synthetase encoded by the herC gene of Escherichia coli. (zfin.org)
Mitochondrial1
  • The encoded protein is a mitochondrial enzyme that specifically aminoacylates alanyl-tRNA. (nih.gov)
Subunit2
  • In ltn1∆ mutant cells, Rqc2 engages the stalled nascent chain, and recruits tRNAs charged with alanine and threonine, so that the 60S catalyzes the C-terminal addition of alanine and threonine to the nascent chain (a "CAT-tail") in an unusual reaction that is not dependent on either the 40S subunit or mRNA 12 . (nature.com)
  • Mutations in three tRNA splicing endonuclease subunit genes were found to be responsible for PCH2, PCH4 and PCH5. (biomedcentral.com)
Cysteine-tRNA l1
Aminoacyl-tRNA synthe4
  • Aminoacyl-tRNA synthetases play critical roles in mRNA translation by charging tRNAs with their cognate amino acids. (nih.gov)
  • Aminoacyl-tRNA synthetases (aaRSs) are a family of translation enzymes, each of which catalyzes the attachment of a specific amino acid to its cognate tRNAs. (ncu.edu.tw)
  • The 20 aminoacyl-tRNA synthetases are divided into two classes, I and II. (embl.de)
  • In reactions catalysed by the class I aminoacyl-tRNA synthetases, the aminoacyl group is coupled to the 2'-hydroxyl of the tRNA, while, in class II reactions, the 3'-hydroxyl site is preferred. (embl.de)
AaRS2
  • Each tRNA is recognized by its cognate aaRS through a specific set of "identity elements", which often reside in the acceptor stem and anticodon. (ncu.edu.tw)
  • In contrast to DTD1, deacylates L-Ala mischarged on tRNA(Thr)(G4.U69) by alanine-tRNA ligase AARS (PubMed:29410408). (nih.gov)
Diphthine-ammoni1
  • EC 6.3.2.22: Now EC 6.3.1.14 , diphthine-ammonia ligase. (wikibedia.ru)
Aminoacylation1
  • For example, almost all known alanine tRNA (tRNAAla) isoacceptors contain a G3:U70 wobble base pair in the acceptor stem that identifies tRNAAla for aminoacylation with alanine. (ncu.edu.tw)
Histidine3
  • Histidine-tRNA Ligase" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (ouhsc.edu)
  • This graph shows the total number of publications written about "Histidine-tRNA Ligase" by people in this website by year, and whether "Histidine-tRNA Ligase" was a major or minor topic of these publications. (ouhsc.edu)
  • Below are the most recent publications written about "Histidine-tRNA Ligase" by people in Profiles. (ouhsc.edu)
Cognate1
  • This raised the question of how AARS2 recognizes its cognate tRNA. (ncu.edu.tw)
Ubiquitin ligase1
  • Here we report that ubiquitination of the 40S ribosomal protein uS10 by the E3 ubiquitin ligase Hel2 (or RQT1) is required for RQC. (nature.com)
Synthetases2
  • However, tRNA binding involves an alpha-helical structure that is conserved between class I and class II synthetases. (embl.de)
  • Kawakami, K., Ito, K., and Nakamura, Y. (1992) Differential regulation of two genes encoding lysyl-tRNA synthetases in Escherichia coli: lysU-constitutive mutations compensate for a lysS null mutation. (zfin.org)
Genes4
  • Five rRNA operons and 74 tRNA genes constitute a total of 89 RNA genes leaving 4,953 protein-encoding genes (CDS). (atm-signaling.com)
  • D. hafniense DZNeP in vivo Y51 contains six rRNA operons and 59 tRNA genes, and has a slightly larger genome by 448 kb (8.5% of the DCB-2 genome) with 166 more genes [9]. (atm-signaling.com)
  • A download Französisches und Deutsches of required genes combine been trained to approach to the target in a tRNA and UNC119B: ARL3: ubiquitin turn. (evakoch.com)
  • These genes are involved in essential processes in protein synthesis in general and tRNA processing in particular. (biomedcentral.com)
Ribosome1
  • Cryo-electron microscopy analysis reveals that Hel2-bound ribosome are dominantly the rotated form with hybrid tRNAs. (nature.com)
Attachment1
  • 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 tRNA(Ala) via its editing domain. (nih.gov)
Proteins4
  • There are 26085 Arg_tRNA_synt_N domains in 26083 proteins in SMART's nrdb database. (embl.de)
  • Taxonomic distribution of proteins containing Arg_tRNA_synt_N domain. (embl.de)
  • The complete taxonomic breakdown of all proteins with Arg_tRNA_synt_N domain is also avaliable . (embl.de)
  • Click on the protein counts, or double click on taxonomic names to display all proteins containing Arg_tRNA_synt_N domain in the selected taxonomic class. (embl.de)
Catalyzes1
  • Catalyzes the hydrolysis of D-tyrosyl-tRNA(Tyr), has no activity on correctly charged L-tyrosyl-tRNA(Tyr) (By similarity). (nih.gov)