A transfer RNA which is specific for carrying alanine to sites on the ribosomes in preparation for protein synthesis.
An enzyme that activates alanine with its specific transfer RNA. EC 6.1.1.7.
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.
Catalyze the joining of preformed ribonucleotides or deoxyribonucleotides in phosphodiester linkage during genetic processes. EC 6.5.1.
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.
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.
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.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
A subclass of enzymes that aminoacylate AMINO ACID-SPECIFIC TRANSFER RNA with their corresponding AMINO ACIDS.
The ultimate exclusion of nonsense sequences or intervening sequences (introns) before the final RNA transcript is sent to the cytoplasm.
A large superfamily of transcription factors that contain a region rich in BASIC AMINO ACID residues followed by a LEUCINE ZIPPER domain.
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.
Enzymes that catalyze the S-adenosyl-L-methionine-dependent methylation of ribonucleotide bases within a transfer RNA molecule. EC 2.1.1.
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.
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.
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.
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.
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.
The sequential set of three nucleotides in TRANSFER RNA that interacts with its complement in MESSENGER RNA, the CODON, during translation in the ribosome.
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).
A pyridoxal-phosphate protein that reversibly catalyzes the conversion of L-alanine to D-alanine. EC 5.1.1.1.
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.
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.
A transfer RNA which is specific for carrying serine to sites on the ribosomes in preparation for protein synthesis.
The spatial arrangement of the atoms of a nucleic acid or polynucleotide that results in its characteristic 3-dimensional shape.
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.
A transfer RNA which is specific for carrying phenylalanine to sites on the ribosomes in preparation for protein synthesis.
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).
A transfer RNA which is specific for carrying tryptophan to sites on the ribosomes in preparation for protein synthesis.
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.
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.
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.
A transfer RNA which is specific for carrying arginine to sites on the ribosomes in preparation for protein synthesis.
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.
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).
A transfer RNA which is specific for carrying glycine to sites on the ribosomes in preparation for protein synthesis.
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.
A transfer RNA which is specific for carrying isoleucine to sites on the ribosomes in preparation for protein synthesis.
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.
A transfer RNA which is specific for carrying glutamic acid to sites on the ribosomes in preparation for protein synthesis.
A transfer RNA which is specific for carrying aspartic acid to sites on the ribosomes in preparation for protein synthesis.
A transfer RNA which is specific for carrying valine to sites on the ribosomes in preparation for protein synthesis.
A transfer RNA which is specific for carrying glutamine to sites on the ribosomes in preparation for protein synthesis.
A transfer RNA which is specific for carrying proline to sites on the ribosomes in preparation for protein synthesis.
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.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
A transfer RNA which is specific for carrying histidine to sites on the ribosomes in preparation for protein synthesis.
A spiral bacterium active as a human gastric pathogen. It is a gram-negative, urease-positive, curved or slightly spiral organism initially isolated in 1982 from patients with lesions of gastritis or peptic ulcers in Western Australia. Helicobacter pylori was originally classified in the genus CAMPYLOBACTER, but RNA sequencing, cellular fatty acid profiles, growth patterns, and other taxonomic characteristics indicate that the micro-organism should be included in the genus HELICOBACTER. It has been officially transferred to Helicobacter gen. nov. (see Int J Syst Bacteriol 1989 Oct;39(4):297-405).
Infections with organisms of the genus HELICOBACTER, particularly, in humans, HELICOBACTER PYLORI. The clinical manifestations are focused in the stomach, usually the gastric mucosa and antrum, and the upper duodenum. This infection plays a major role in the pathogenesis of type B gastritis and peptic ulcer disease.
Inflammation of the GASTRIC MUCOSA, a lesion observed in a number of unrelated disorders.
An order of anaerobic methanogens in the kingdom EURYARCHAEOTA. They are pseudosarcina, coccoid or sheathed rod-shaped and catabolize methyl groups. The cell wall is composed of protein. The order includes one family, METHANOCOCCACEAE. (From Bergey's Manual of Systemic Bacteriology, 1989)

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)

Sato, K, A mammalian cell mutant with an altered alanyl-trna synthetase. Abstr. (1976). Subject Strain Bibliography 1976. 2737 ...
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...
Complete information for AARS1 gene (Protein Coding), Alanyl-TRNA Synthetase 1, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
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 ...
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
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 ...
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
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).
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.
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- ...
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.
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
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). ...
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.
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 ...
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Mouse monoclonal valyl tRNA synthetase antibody [VARSA7E6] validated for WB, Dot and tested in Human. Immunogen corresponding to recombinant fragment
CellTrics® are disposable filters for isolation of cells and nuclei from cell debris and aggregates. These non-sterile filters are bulk-packed and ha…
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
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.
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%...
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!
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。
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]. ...
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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 ...
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
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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 ...
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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)
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". CS1 maint: discouraged parameter (link) 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: ... "Toward the full set of human mitochondrial aminoacyl-tRNA synthetases: characterization of AspRS and TyrRS". Biochemistry. 44 ( ...
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). ...
... 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- ...
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 ...
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 ...
... 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 ...
... 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 ...
... 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 ...
Enzymes: CO CS and CN ligases (EC 6.1-6.3). 6.1: Carbon-Oxygen. *Aminoacyl tRNA synthetase *Alanine ... 6-diaminopimelate ligase (MurE), and UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase (MurF). This entry also includes ... Deva T, Baker EN, Squire CJ, Smith CA (December 2006). "Structure of Escherichia coli UDP-N-acetylmuramoyl:L-alanine ligase ( ... This family includes UDP-N-acetylmuramate-L-alanine ligase (MurC), UDP-N-acetylmuramoylalanyl-D-glutamate-2, ...
Enzymes: CO CS and CN ligases (EC 6.1-6.3). 6.1: Carbon-Oxygen. *Aminoacyl tRNA synthetase *Alanine ... The common names of ligases often include the word "ligase", such as DNA ligase, an enzyme commonly used in molecular biology ... DNA ligase. References[edit]. *^ "Synthases and ligases". chem.qmul.ac.uk. Archived from the original on October 15, 2012. ... This article is about general ligases. For DNA specific ligases, see DNA ligase. ...
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 ...
Enzymes: CO CS and CN ligases (EC 6.1-6.3). 6.1: Carbon-Oxygen. *Aminoacyl tRNA synthetase *Alanine ... An aminoacyl-tRNA synthetase (aaRS or ARS), also called tRNA-ligase, is an enzyme that attaches the appropriate amino acid onto ... If the incorrect tRNA is added (aka. the tRNA is found to be improperly charged), the aminoacyl-tRNA bond is hydrolyzed. This ... Delarue, M (1995). "Aminoacyl-tRNA synthetases". Structural Biology. 5: 48-55.. *^ "Molecule of the Month: Aminoacyl-tRNA ...
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 2016, fifty-four 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 ...
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 ...
... 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 ...
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, ...
Enzymes: CO CS and CN ligases (EC 6.1-6.3). 6.1: Carbon-Oxygen. *Aminoacyl tRNA synthetase *Alanine ... Alanine, glycine, and serine bind to the glutamate substrate site. GDP, AMP, ADP bind to the ATP site.[6] L-serine, L-alanine, ... glutamate-ammonia ligase. Active site between two monomers of glutamine synthetase from Salmonella typhimurium. Cation binding ... "Feedback inhibition of fully unadenylylated glutamine synthetase from Salmonella typhimurium by glycine, alanine, and serine" ...
Enzymes: CO CS and CN ligases (EC 6.1-6.3). 6.1: Carbon-Oxygen. *Aminoacyl tRNA synthetase *Alanine ...
Enzymes: CO CS and CN ligases (EC 6.1-6.3). 6.1: Carbon-Oxygen. *Aminoacyl tRNA synthetase *Alanine ... L-glutamine amido-ligase, (ADP-forming), 2-N-formyl-1-N-(5-phospho-D-ribosyl)glycinamide:L-glutamine, and amido-ligase (ADP- ... This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds carbon-nitrogen ligases with ... The systematic name of this enzyme class is N2-formyl-N1-(5-phospho-D-ribosyl)glycinamide:L-glutamine amido-ligase (ADP-forming ...
Enzymes: CO CS and CN ligases (EC 6.1-6.3). 6.1: Carbon-Oxygen. *Aminoacyl tRNA synthetase *Alanine ... E3 ligase activity[edit]. The E3 ubiquitin ligase MDM2 is a negative regulator of the p53 tumor suppressor protein. MDM2 binds ... ubiquitin protein ligase activity. • NEDD8 ligase activity. • disordered domain specific binding. • protein domain specific ... The RING domain of Mdm2 confers E3 ubiquitin ligase activity and is sufficient for E3 ligase activity in Mdm2 RING ...
Enzymes: CO CS and CN ligases (EC 6.1-6.3). 6.1: Carbon-Oxygen. *Aminoacyl tRNA synthetase *Alanine ... L-glutamine amido-ligase (AMP-forming).[1][2][3][4][5][6] This enzyme catalyses the following chemical reaction ...
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 ...
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- ...
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 ...
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 ...
... if a tRNA synthases loaded an incorrect amino acid onto a tRNA, the resulting peptide would have unexpectedly altered ... β-cyclohexyl-L-alanine, 4-amino-L-phenylalanine and L-norleucine.[28] ... Perona JJ, Hadd A (November 2012). "Structural diversity and protein engineering of the aminoacyl-tRNA synthetases". ... properties, consequently to enhance fidelity several additional domains are present.[27] Similar in reaction to tRNA synthases ...
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-)- ...
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 ...
... alanines. Humans express one kynureninase enzyme that is encoded by the KYNU gene located on chromosome 2.[6][7] ...
The mitochondrial creatine kinase (CKm) is present in the mitochondrial intermembrane space, where it regenerates phosphocreatine (PCr) from mitochondrially generated ATP and creatine (Cr) imported from the cytosol. Apart from the two mitochondrial CK isoenzyme forms, that is, ubiquitous mtCK (present in non-muscle tissues) and sarcomeric mtCK (present in sarcomeric muscle), there are three cytosolic CK isoforms present in the cytosol, depending on the tissue. Whereas MM-CK is expressed in sarcomeric muscle, that is, skeletal and cardiac muscle, MB-CK is expressed in cardiac muscle, and BB-CK is expressed in smooth muscle and in most non-muscle tissues. Mitochondrial mtCK and cytosolic CK are connected in a so-called PCr/Cr-shuttle or circuit. PCr generated by mtCK in mitochondria is shuttled to cytosolic CK that is coupled to ATP-dependent processes, e.g. ATPases, such as acto-myosin ATPase and calcium ATPase involved in muscle contraction, and sodium/potassium ATPase involved in sodium ...
EC 6.2.1.53: [[L-proline--[L-prolyl-carrier protein] ligase]]. *EC 6.2.1.54: [[D-alanine--[D-alanyl-carrier protein] ligase]] ... EC 2.9.1.2: O-phospho-L-seryl-tRNA(Sec):L-selenocysteinyl-tRNA synthase ... Category:Ligases (EC 6) (Ligase)Edit. Category:EC 6.1 (form carbon-oxygen bonds)Edit. 6-carboxytetrahydropterin synthase ... 6 Category:Ligases (EC 6) (Ligase) *6.1 Category:EC 6.1 (form carbon-oxygen bonds) ...
... 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- ...
... 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 ...
... 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 ... Ala-tRNA-ligase_IIc_anticod-bd. IPR018165, Ala-tRNA-synth_IIc_core. IPR018164, Ala-tRNA-synth_IIc_N. IPR023033, Ala_tRNA_ ... Ala-tRNA-ligase_IIc_anticod-bd. IPR018165, Ala-tRNA-synth_IIc_core. IPR018164, Ala-tRNA-synth_IIc_N. IPR023033, Ala_tRNA_ ...
"Alanine-tRNA Ligase" by people in Harvard Catalyst Profiles by year, and whether "Alanine-tRNA Ligase" was a major or minor ... "Alanine-tRNA Ligase" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH (Medical ... Alanine-tRNA Ligase*Alanine-tRNA Ligase. *Alanine tRNA Ligase. *Ligase, Alanine-tRNA ... Below are the most recent publications written about "Alanine-tRNA Ligase" by people in Profiles. ...
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. ... Catalyzes the attachment of alanine to tRNA(Ala) in a two-step ... Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and ...
... 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 ...
... tRNA ligase 1(alaS1) ,partial. It is produced in Yeast. High purity. Good price. ... Recombinant Clostridium phytofermentans Alanine--tRNA ligase 1(alaS1) ,partial. Recombinant Clostridium phytofermentans Alanine ... alaS1; Cphy_2617; Alanine--tRNA ligase 1; EC 6.1.1.7; Alanyl-tRNA synthetase 1; AlaRS 1. ... Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction. ...
... tRNA ligase. Orientia tsutsugamushi (strain Ikeda) (Rickettsia tsutsugamushi) ... Alanine--tRNA ligase UniProtKBInterProInteractive Modelling. 889 aa; Sequence (Fasta) It is possible new templates exist for ... Alanyl-tRNA synthetase, class IIc, N-terminal. IPR018164PF01411. 663-712. Threonyl/alanyl tRNA synthetase, SAD. IPR012947 ...
... tRNA ligase. Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM15464 / FAM18) ... Alanine--tRNA ligase UniProtKBInterProInteractive Modelling. 874 aa; Sequence (Fasta) Identical sequences: Neisseria ... Alanyl-tRNA synthetase, class IIc, N-terminal. IPR018164PF01411. 651-694. Threonyl/alanyl tRNA synthetase, SAD. IPR012947 ...
Paradox of mistranslation of serine for alanine caused by AlaRS recognition dilemma. ... Alanine--tRNA ligase. > Alanine-tRNA ligase, class IIc * Occurring in:. *Alanine--tRNA ligase. > Alanyl-tRNA synthetase, ... Alanine--tRNA ligase. > Alanine-tRNA ligase, class IIc, anti-codon-binding domain superfamily ... Alanine--tRNA ligase Chain: A Molecule details › Chain: A. Length: 441 amino acids. Theoretical weight: 49.92 KDa. Source ...
The consequent Gly-tRNA,sup,Gly,/sup, misediting paradox is resolved by EF-Tu in the cell. Her … ... Pro motif during chiral proofreading underlies the inability of D-aminoacyl-tRNA deacylase (DTD) to discriminate between D- ... Alanine-tRNA Ligase / antagonists & inhibitors* * Aminoacyltransferases / metabolism* * Escherichia coli / enzymology* * ... The consequent Gly-tRNAGly misediting paradox is resolved by EF-Tu in the cell. Here, we show that DTDs active site ...
Alanyl-TRNA Synthetase 1, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human ... Alanine TRNA Ligase 1, Cytoplasmic 2 3 * Alanine--TRNA Ligase, Cytoplasmic 3 4 ... Reaction=ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala); Xref=Rhea:RHEA:12540, Rhea:RHEA-COMP:9657, Rhea: ... Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and ...
Alanine--tRNA ligase, cytoplasmic. Enzyme. 5 metabolites. HMDBP00871. HEXB. Beta-hexosaminidase subunit beta. Enzyme. 56 ... E3 ubiquitin-protein ligase MIB1. Enzyme. 4 metabolites. HMDBP00626. WARS2. 1p12. Tryptophan--tRNA ligase, mitochondrial. ... Methionine--tRNA ligase, cytoplasmic. Enzyme. 6 metabolites. HMDBP01114. SLC16A4. 1p13.3. Monocarboxylate transporter 5. Enzyme ... E3 ubiquitin-protein ligase NEDD4. Enzyme. 4 metabolites. HMDBP00624. PDE6A. 5q31.2-q34. Rod cGMP-specific 3,5-cyclic ...
Alanine--tRNA ligase, mitochondrial Show on y-axis - References (HTP + LTP). References (LTP). References (HTP). ...
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_ ...
... tRNA-binding; Zinc. FT CHAIN 1..860 FT /note="Alanine--tRNA ligase" FT /id="PRO_0000347860" FT METAL 563 FT /note="Zinc" FT / ... DR HAMAP; MF_00036_B; Ala_tRNA_synth_B; 1. DR InterPro; IPR002318; Ala-tRNA-lgiase_IIc. DR InterPro; IPR018162; Ala-tRNA-ligase ... TRNA_LIGASE_II_ALA; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal- ... DE RecName: Full=Alanine--tRNA ligase {ECO:0000255,HAMAP-Rule:MF_00036}; DE EC=6.1.1.7 {ECO:0000255,HAMAP-Rule:MF_00036}; DE ...
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 ...
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 ( ...
Deficiency of alanine dehydrogenase. *Deficiency of alanine-oxo-acid aminotransferase. *Deficiency of alanine-tRNA ligase ...
... alanine aminotransferase (MAC; unigene9129), aspartate-tRNA ligase (ARS; unigene18089), prolyl-tRNA synthase (PRS; unigene16762 ...
Alanine-tRNA Ligase Mutation update for the SATB2 gene. Zarate, Y. A., Bosanko, K. A., Caffrey, A. R., Bernstein, J. A., Martin ...
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- ...
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 ...
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; ...
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: ...
... from 14 Acanthamoeba species allowed designing PCR systems for one of these core genes that encodes an alanine-tRNA ligase. ...
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 ...
Alanine--tRNA ligase, cytoplasmic. Helix. 319 - 339. Literature citations. A major determinant for binding and aminoacylation ... A recurrent loss-of-function alanyl-tRNA synthetase (AARS) mutation in patients with Charcot-Marie-Tooth disease type 2N (CMT2N ... of tRNA(Ala) in cytoplasmic Alanyl-tRNA synthetase is mutated in dominant axonal Charcot-Marie-Tooth disease. Latour P.; ...
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 ...
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". CS1 maint: discouraged parameter (link) 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: ... "Toward the full set of human mitochondrial aminoacyl-tRNA synthetases: characterization of AspRS and TyrRS". Biochemistry. 44 ( ...
  • Deficient activity of alanyl-tRNA synthetase underlies an autosomal recessive syndrome of progressive microcephaly, hypomyelination, and epileptic encephalopathy. (harvard.edu)
  • A recurrent loss-of-function alanyl-tRNA synthetase (AARS) mutation in patients with Charcot-Marie-Tooth disease type 2N (CMT2N). (harvard.edu)
  • Clinical manifestations of anti-synthetase syndrome positive for anti-alanyl-tRNA synthetase (anti-PL12) antibodies: a retrospective study of 17 cases. (harvard.edu)
  • CDC64 encodes cytoplasmic alanyl-tRNA synthetase, Ala1p, of Saccharomyces cerevisiae. (harvard.edu)
  • Localization of two human autoantigen genes by PCR screening and in situ hybridization--glycyl-tRNA synthetase locates to 7p15 and alanyl-tRNA synthetase locates to 16q22. (harvard.edu)
  • The human alanyl-tRNA synthetase (AARS) belongs to a family of tRNA synthases, of the class II enzymes. (genecards.org)
  • AARS1 (Alanyl-TRNA Synthetase 1) is a Protein Coding gene. (genecards.org)
  • AARSD1 (Alanyl-TRNA Synthetase Domain Containing 1) is a Protein Coding gene. (genecards.org)
  • SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. (genome.jp)
  • AARS(alanyl-tRNA synthetase) is also named as AlaRS(alanine tRNA ligase 1, cytoplasmic), renal carcinoma antigen NY-REN-42 and belongs to the class-II aminoacyl-tRNA synthetase family. (ptglab.com)
  • A major determinant for binding and aminoacylation of tRNA(Ala) in cytoplasmic Alanyl-tRNA synthetase is mutated in dominant axonal Charcot-Marie-Tooth disease. (expasy.org)
  • 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. (prospecbio.com)
  • Alanyl-tRNA synthetase, mitochondrial, also known as alanine-tRNA ligase (AlaRS) or alanyl-tRNA synthetase 2 (AARS2), is an enzyme that in humans is encoded by the AARS2 gene. (wikipedia.org)
  • Isoleucine-tRNA ligase (also known as Isoleucyl-tRNA synthetase)( EC:6.1.1.5 ) is an alpha monomer that belongs to class Ia. (ebi.ac.uk)
  • The aminoacyl-tRNA synthetase (also known as aminoacyl-tRNA ligase) catalyse the attachment of an amino acid to its cognate transfer RNA molecule in a highly specific two-step reaction [ PMID: 10704480 , PMID: 12458790 ]. (ebi.ac.uk)
  • Insights into editing from an ile-tRNA synthetase structure with tRNAile and mupirocin. (ebi.ac.uk)
  • The 2.0 A crystal structure of Thermus thermophilus methionyl-tRNA synthetase reveals two RNA-binding modules. (ebi.ac.uk)
  • Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase. (ebi.ac.uk)
  • The aminoacyl-tRNA synthetase family: modules at work. (ebi.ac.uk)
  • Two mecillinam resistant mutants, lov-1 and lovB, both able to dispense entirely with PBP2, are shown here to be affected in the aminoacyl-tRNA synthetase genes argS and alaS, respectively. (microbialphenotypes.org)
  • The argS and alaS mutants have high pools of the nucleotide ppGpp (effector of the stringent response) and the mecillinam resistance of both mutations is suppressed by a relA mutation, inactivating the ribosome-associated ppGpp synthetase and preventing ppGpp synthesis in response to aminoacyl-tRNA starvation. (microbialphenotypes.org)
  • Provided herein is a Mouse Recombinant Antibody against Alanyl-TRNA Synthetase. (antibody-creativebiolabs.com)
  • Four genes encoding an aminoacyl-tRNA synthetase (ARS) have been implicated in CMT disease. (ox.ac.uk)
  • Chou TF, Tikh IB, Horta BA, Ghosh B, De Alencastro RB, Wagner CR: Engineered monomeric human histidine triad nucleotide-binding protein 1 hydrolyzes fluorogenic acyl-adenylate and lysyl-tRNA synthetase-generated lysyl-adenylate. (drugbank.ca)
  • Data on alanyl-tRNA synthetase from an early eukaryote and other sources are presented and analyzed here. (scripps.edu)
  • Recombinant alanyl-tRNA synthetase Protein, Mouse (His Tag) Recombinant Proteins The mouse AARS (Q8BGQ7) (Met 1-Asn 968) was fused with a polyhistidine tag at the C-terminus The secreted recombinant mouse AARS consists of 978a.a and has a calculated molecular weight of 108.3 kDa. (thebiotek.com)
  • Alanyl-tRNA synthetase (AARS) belongs to the family of ligases, specifically those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. (thebiotek.com)
  • Alanyl-tRNA synthetase (AlaRS) catalyzes synthesis of Ala-tRNA (Ala) and hydrolysis of mis-acylated Ser- and Gly-tRNA (Ala) at 2 different catalytic sites. (thebiotek.com)
  • Secretion of this tRNA synthetase may contribute to apoptosis both by arresting translation and producing needed cytokines. (thebiotek.com)
  • AARS / alanyl-tRNA synthetase specific IgG was purified by Mouse AARS / alanyl-tRNA synthetase affinity chromatography. (sinobiological.com)
  • This antibody can be used at 0.1-0.2 μg/ml with the appropriate secondary reagents to detect Mouse AARS / alanyl-tRNA synthetase. (sinobiological.com)
  • 1999) Two Distinct Cytokines Released from a Human Aminoacyl-tRNA Synthetase. (sinobiological.com)
  • 2009) The structure of alanyl-tRNA synthetase with editing domain. (sinobiological.com)
  • Full length Clone DNA of Human alanyl-tRNA synthetase with C terminal HA tag. (sinobiological.com)
  • Human alanyl-tRNA synthetase: conservation in evolution of catalytic core and microhelix recognition. (bosterbio.com)
  • The conserved sequence motifs found in the four Mur enzymes also map to other members of the Mur ligase family, including folylpolyglutamate synthetase, cyanophycin synthetase and the capB enzyme from Bacillales. (wikipedia.org)
  • Other common names for ligases include the word "synthetase", because they are used to synthesize new molecules. (wikipedia.org)
  • It is also said that a synthase is a lyase (a lyase is an enzyme that catalyzes the breaking of various chemical bonds by means other than hydrolysis and oxidation, often forming a new double bond or a new ring structure) and does not require any energy, whereas a synthetase is a ligase (a ligase is an enzyme that binds two chemicals or compounds) and thus requires energy. (wikipedia.org)
  • This all alpha helical domain is the anticodon binding domain of Arginyl tRNA synthetase. (embl-heidelberg.de)
  • This all alpha helical domain is the anticodon binding domain (ABD) of arginyl tRNA synthetase, and also matches the ABD of some glycine tRNA synthetases. (embl-heidelberg.de)
  • Aminoacyl-tRNA synthetase (aaRS) is a key enzyme during protein biosynthesis. (embl-heidelberg.de)
  • Preliminary data suggest that epitope spreading occurs in the autoimmune PL-12 response such that even antibodies to an isolated alanyl-tRNA molecule can develop. (prospecbio.com)
  • Biological process: alanyl-tRNA aminoacylation. (expasy.org)
  • Among its related pathways are tRNA Aminoacylation and Gene Expression . (genecards.org)
  • The CC editing domain removes incorrectly charged amino acids, while the CC C-Ala domain, along with tRNA(Ala), serves as a bridge to CC cooperatively bring together the editing and aminoacylation CC centers thus stimulating deacylation of misacylated tRNAs. (genome.jp)
  • An important gene associated with Mitochondrial Cardiomyopathy is MT-TL2 (Mitochondrially Encoded TRNA Leucine 2 (CUN)), and among its related pathways/superpathways are Glucose / Energy Metabolism and tRNA Aminoacylation . (malacards.org)
  • The enzyme, isoleucine-tRNA ligase, activates not only the cognate substrate L-isoleucine but also the minimally distinct L-valine in the first, aminoacylation step. (ebi.ac.uk)
  • Kinetic parameters were obtained for aminoacylation with each amino acid of the tRNA with double identity and of related tRNAs. (scripps.edu)
  • Alanine is highly concentrated in meat products and other high-protein foods like wheat germ and cottage cheese. (selfdecode.com)
  • Yeast tRNA ligase (Trl1) is an essential trifunctional enzyme that catalyzes exon-exon ligation during tRNA biogenesis and the non-conventional splicing of HAC1 mRNA during the unfolded protein response (UPR). (elifesciences.org)
  • The fungal tRNA ligase Trl1 (previously named Rlg1) is encoded by an essential gene and is involved in tRNA splicing and the unfolded protein response (UPR). (elifesciences.org)
  • Modulates proteasomal degradation of target proteins by the SCF (SKP2-CUL1-F-box protein) E3 ubiquitin-protein ligase complex. (drugbank.ca)
  • A recent paper in Science provides evidence that when protein synthesis is stalled a protein called Rqc2 ("conserved from yeast to man") catalyzes the addition of random amounts of alanine and threonine the the C-terminus of the proteins that's about to be destroyed (Shen et al. (blogspot.com)
  • Ltn1p, a ubiquitin ligase, binds near the nascent polypeptide exit tunnel on the ribosome, well placed to tag the truncated protein for destruction. (blogspot.com)
  • The Rqc2p protein interacts with the transfer RNA binding sites on the partial ribosome and recruits alanine- and threonine-bearing tRNAs. (blogspot.com)
  • A protein complex that includes a ubiquitin-protein ligase and enables ubiquitin protein ligase activity. (leibniz-fli.de)
  • Here, we show that DTD's active site architecture can efficiently edit mischarged Gly-tRNA Ala species four orders of magnitude more efficiently than even AlaRS, the only ubiquitous cellular checkpoint known for clearing the error. (nih.gov)
  • Also, DTD knockout in AlaRS editing-defective background causes pronounced toxicity in Escherichia coli even at low-glycine levels which is alleviated by alanine supplementation. (nih.gov)
  • Together, our data suggest that impaired tRNA charging plays a role in the molecular pathology of CMT2N, and that patients with CMT should be directly tested for the p.Arg329His AARS mutation. (ox.ac.uk)
  • Each aaRS contains a catalytic central domain (CCD), responsible for activating amino acid, and an anticodon-binding domain (ABD), necessary for binding the anticodon in cognate tRNA. (embl-heidelberg.de)
  • Gene Ontology (GO) annotations related to this gene include nucleic acid binding and aminoacyl-tRNA editing activity . (genecards.org)
  • Evolution of aminoacyl-tRNA synthetases--analysis of unique domain architectures and phylogenetic trees reveals a complex history of horizontal gene transfer events. (ebi.ac.uk)
  • GO annotations related to this gene include alanine-tRNA ligase activity and molecular_function. (science-marketplace.org)
  • tRNA synthases are the enzymes that interpret the RNA code and attach. (genecards.org)
  • tRNA synthases are the enzymes that interpret the RNA code and attach specific aminoacids to the tRNAs that contain the cognate trinucleotide anticodons. (genecards.org)
  • Alanine dehydrogenase and alanine transaminase are the enzymes which catalyse this one step conversion. (llamp.net)
  • Normal alanine metabolism, like that of other amino acids, is highly dependent upon enzymes that contain vitamin B6. (selfdecode.com)
  • ARSs are ubiquitously expressed, essential enzymes that ligate amino acids to cognate tRNA molecules. (ox.ac.uk)
  • In biochemistry , a ligase is an enzyme that can catalyze the joining of two large molecules by forming a new chemical bond , usually with accompanying hydrolysis of a small pendant chemical group on one of the larger molecules or the enzyme catalyzing the linking together of two compounds, e.g., enzymes that catalyze joining of C-O, C-S, C-N, etc. (wikipedia.org)
  • Ligases are classified as EC 6 in the EC number classification of enzymes. (wikipedia.org)
  • Several unexpected evolutionaryconnections were identified, including the apparent origin of thebeta-subunit of bacterial GlyRS from the HD superfamily of hydrolases, adomain shared by bacterial AspRS and the B subunit of archaealglutamyl-tRNA amidotransferases, and another previously undetected domainthat is conserved in a subset of ThrRS, guanosine polyphosphate hydrolasesand synthetases, and a family of GTPases. (embl-heidelberg.de)
  • We've known about ubiquitin ligase for decades but this is a different way of tagging proteins for destruction. (blogspot.com)
  • A ubiquitin ligase complex found in the nucleus. (leibniz-fli.de)
  • A ubiquitin ligase complex found in the ER. (leibniz-fli.de)
  • In S. cerevisiae, this complex contains the ubiquitin ligase Hrd1p. (leibniz-fli.de)
  • In mammals, this complex contains the ubiquitin ligase HRD1 (Synoviolin) or AMFR (gp78). (leibniz-fli.de)
  • In S. cerevisiae, this complex contains the ubiquitin ligase Ssm4p/Doa10p. (leibniz-fli.de)
  • Some ligases associate with biological membranes as peripheral membrane proteins or anchored through a single transmembrane helix , [2] for example certain ubiquitin ligase related proteins. (wikipedia.org)
  • 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. (uniprot.org)
  • 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) (PubMed:27622773, PubMed:27911835, PubMed:28493438). (genecards.org)
  • Hydrolyzes lysyl-AMP (AMP-N-epsilon-(N-alpha-acetyl lysine methyl ester)) generated by lysine tRNA ligase, as well as Met-AMP, His-AMP and Asp-AMP, lysyl-GMP (GMP-N-epsilon-(N-alpha-acetyl lysine methyl ester)) and AMP-N-alanine methyl ester. (drugbank.ca)
  • [4] These four Mur ligases are responsible for the successive additions of L-alanine, D-glutamate, meso- diaminopimelate or L-lysine, and D-alanyl-D-alanine to UDP- N-acetylmuramic acid . (wikipedia.org)
  • Strict L-chiral rejection through Gly- cis Pro motif during chiral proofreading underlies the inability of D-aminoacyl-tRNA deacylase (DTD) to discriminate between D-amino acids and achiral glycine. (nih.gov)
  • Plasma alanine is often decreased when the BCAA (Branched Chain Amino Acids) are deficient. (selfdecode.com)
  • A tRNA with "double identity" was created, and this tRNA was demonstrated in vitro to aminoacylate quantitatively with either of two amino acids. (scripps.edu)
  • Selenocysteine, also known as 3-seleno-alanine, belongs to the class of organic compounds known as l-alpha-amino acids. (hmdb.ca)
  • Previous delineation of a core genome encompassing 826 genes based on draft genome sequences from 14 Acanthamoeba species allowed designing PCR systems for one of these core genes that encodes an alanine-tRNA ligase. (doaj.org)
  • A number of genes exist only within deep-sea adapted species, such as those encoding d-alanine-d-alanine ligase for peptidoglycan formation, alanine dehydrogenase for NADH/NAD + homeostasis, and a SAM methyltransferase for tRNA modification. (biomedcentral.com)
  • Catalysis of the reaction: poly(ribitol phosphate) + D-alanine + ATP = O-D-alanyl-poly(ribitol phosphate) + diphosphate + AMP. (systemsbiology.net)
  • Catalysis of the reaction: ATP + (R)-pantoate + beta-alanine = AMP + diphosphate + (R)-pantothenate. (leibniz-fli.de)
  • Moreover, DTD's activity on non-cognate Gly-tRNA Ala is conserved across all bacteria and eukaryotes, suggesting DTD's key cellular role as a glycine deacylator. (nih.gov)
  • Alanine and derivatives are compounds containing alanine or a derivative thereof resulting from reaction of alanine at the amino group or the carboxy group, or from the replacement of any hydrogen of glycine by a heteroatom. (foodb.ca)
  • This enzyme participates in alanine and aspartate metabolism and aminoacyl-trna biosynthesis. (wikipedia.org)
  • Alanine racemase, a pyridoxal phosphate dependent enzyme which catalyses isomerisation of L-alanine to D-alanine is present in both Plasmodium falciparum and Toxoplasma gondii genomes and annotated to the pyridoxal phosphate metabolism pathway in MPMP as an example of an enzyme that requires pyridoxal phosphate as a cofactor for its function. (llamp.net)
  • Alanine is an important participant as well as regulator in glucose metabolism. (selfdecode.com)
  • In cattle, L-histidine is involved in a couple of metabolic pathways, which include the histidine metabolism pathway and the beta-alanine metabolism pathway. (bovinedb.ca)
  • 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)
  • belongs to the class of organic compounds known as alanine and derivatives. (foodb.ca)
  • PanC belongs to a large superfamily of nucleotidyltransferases that includes , ATP sulfurylase (ATPS), phosphopantetheine adenylyltransferase (PPAT), and the amino-acyl tRNA synthetases. (bu.edu)
  • Vancomycin binds relatively poorly to peptidoglycan ending in d -alanyl- d -lactate and binds with high affinity to peptidoglycan ending in d -alanyl- d -alanine ( d -Ala- d -Ala), which results in vancomycin resistance and sensitivity, respectively. (asm.org)
  • The enzyme responsible for generating these peptidoglycan precursors is dipeptide ligase (Ddl). (asm.org)
  • Here, we show that heterologous expression of the enzyme Ddl (dipeptide ligase)-an essential enzyme involved in peptidoglycan synthesis-increases sensitivity to vancomycin in a dose-dependent manner. (asm.org)
  • Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs. (ebi.ac.uk)
  • Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases. (ebi.ac.uk)
  • Is the sequence-specific binding of aminoacyl-tRNAs by EF-Tu universal among bacteria? (northwestern.edu)
  • The results delineate some of the kinetic boundaries for the design and accommodation of tRNA sequence variations in the elaboration of identity in vivo. (scripps.edu)
  • The alanine and threonine are added at random, in no particular order, therefore there is no sequence information associated with the CAT tail. (blogspot.com)
  • All four Mur ligases are topologically similar to one another, even though they display low sequence identity. (wikipedia.org)
  • Also edits incorrectly charged tRNA(Ala) via its editing domain (PubMed:27622773, PubMed:27911835, PubMed:28493438). (genecards.org)
  • Functions in trans to edit the amino acid moiety from incorrectly charged tRNA(Ala). (genecards.org)
  • 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. (genecards.org)
  • Class I aminoacyl-tRNA synthetases contain a characteristic Rossman fold catalytic domain and are mostly monomeric [ PMID: 10673435 ]. (ebi.ac.uk)
  • EC 6.1.1.17 ) is a class Ic ligase and shows several similarities with glutamate-tRNA ligase concerning structure and catalytic properties. (embl.de)
  • This family is pantoate--beta-alanine ligase, the last enzyme of pantothenate biosynthesis. (bu.edu)
  • Furthermore, L-Histidine and beta-alanine can be converted into carnosine through the action of the enzyme carnosine synthase 1. (bovinedb.ca)
  • Finally, beta-Alanine and L-histidine can be biosynthesized from carnosine through the action of the enzyme Beta-ala-his dipeptidase. (bovinedb.ca)
  • Misacylation of pyrrolysine tRNA in vitro and in vivo. (harvard.edu)
  • The single step synthesis of alanine from pyruvate is unique to Coccidians such as Toxoplasma and Neospora among the phylum of Apicomplexa . (llamp.net)
  • Then, in a second, "editing" step, the ligase itself rapidly hydrolyses only the valylated products [ PMID: 9554847 , PMID: 10446055 ] as shown from the crystal structures. (ebi.ac.uk)
  • Class II aminoacyl-tRNA synthetases share an anti-parallel beta-sheet fold flanked by alpha-helices [ PMID: 8364025 ], and are mostly dimeric or multimeric, containing at least three conserved regions [ PMID: 8274143 , PMID: 2053131 , PMID: 1852601 ]. (ebi.ac.uk)
  • Based on their mode of binding to the tRNA acceptor stem, both classes of tRNA synthetases have been subdivided into three subclasses, designated 1a, 1b, 1c and 2a, 2b, 2c [ PMID: 10447505 ]. (ebi.ac.uk)
  • The selenocysteine tRNAs are initially charged with serine by seryl-tRNA ligase, but the resulting Ser-tRNASec is not used for translation because it is not recognised by the normal translation elongation factor (EF-Tu in bacteria, eEF1A in eukaryotes). (hmdb.ca)
  • Molecular function: alanine-tRNA ligase activity. (expasy.org)
  • Alanine is a nonessential amino acid made in the body from the conversion of the carbohydrate pyruvate or the breakdown of DNA and the dipeptides carnosine and anserine. (selfdecode.com)