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 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.
Enzymes of the transferase class that catalyze the conversion of L-aspartate and 2-ketoglutarate to oxaloacetate and L-glutamate. EC 2.6.1.1.
An enzyme that catalyzes the conversion of carbamoyl phosphate and L-aspartate to yield orthophosphate and N-carbamoyl-L-aspartate. (From Enzyme Nomenclature, 1992) EC 2.1.3.2.
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.
One of the non-essential amino acids commonly occurring in the L-form. It is found in animals and plants, especially in sugar cane and sugar beets. It may be a neurotransmitter.
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.
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 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.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
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.
An enzyme that catalyzes the formation of beta-aspartyl phosphate from aspartic acid and ATP. Threonine serves as an allosteric regulator of this enzyme to control the biosynthetic pathway from aspartic acid to threonine. EC 2.7.2.4.
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.
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 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.
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.
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 transfer RNA which is specific for carrying isoleucine 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.
The rate dynamics in chemical or physical systems.
A transfer RNA which is specific for carrying alanine 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 valine to sites on the ribosomes in preparation for protein synthesis.
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.
An enzyme that catalyzes the conversion of aspartic acid to ammonia and fumaric acid in plants and some microorganisms. EC 4.3.1.1.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
A transfer RNA which is specific for carrying glutamine to sites on the ribosomes in preparation for protein synthesis.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
A transfer RNA which is specific for carrying proline to sites on the ribosomes in preparation for protein synthesis.
A transfer RNA which is specific for carrying histidine 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.
Cell surface proteins that bind amino acids and trigger changes which influence the behavior of cells. Glutamate receptors are the most common receptors for fast excitatory synaptic transmission in the vertebrate central nervous system, and GAMMA-AMINOBUTYRIC ACID and glycine receptors are the most common receptors for fast inhibition.
Ribonucleic acid in bacteria having regulatory and catalytic roles as well as involvement in protein synthesis.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
Derivatives of GLUTAMIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the 2-aminopentanedioic acid structure.
A DNA amplification technique based upon the ligation of OLIGONUCLEOTIDE PROBES. The probes are designed to exactly match two adjacent sequences of a specific target DNA. The chain reaction is repeated in three steps in the presence of excess probe: (1) heat denaturation of double-stranded DNA, (2) annealing of probes to target DNA, and (3) joining of the probes by thermostable DNA ligase. After the reaction is repeated for 20-30 cycles the production of ligated probe is measured.
A subset of ubiquitin protein ligases that are formed by the association of a SKP DOMAIN PROTEIN, a CULLIN DOMAIN PROTEIN and a F-BOX DOMAIN PROTEIN.
The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.
A set of three nucleotides in a protein coding sequence that specifies individual amino acids or a termination signal (CODON, TERMINATOR). Most codons are universal, but some organisms do not produce the transfer RNAs (RNA, TRANSFER) complementary to all codons. These codons are referred to as unassigned codons (CODONS, NONSENSE).
An aspartate aminotransferase found in MITOCHONDRIA.
Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.
A family of proteins that share the F-BOX MOTIF and are involved in protein-protein interactions. They play an important role in process of protein ubiquition by associating with a variety of substrates and then associating into SCF UBIQUITIN LIGASE complexes. They are held in the ubiquitin-ligase complex via binding to SKP DOMAIN PROTEINS.
A transfer RNA which is specific for carrying threonine to sites on the ribosomes in preparation for protein synthesis.
A simple organophosphorus compound that inhibits DNA polymerase, especially in viruses and is used as an antiviral agent.
A class of enzymes that form a thioester bond to UBIQUITIN with the assistance of UBIQUITIN-ACTIVATING ENZYMES. They transfer ubiquitin to the LYSINE of a substrate protein with the assistance of UBIQUITIN-PROTEIN LIGASES.
Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.
A reaction that introduces an aminoacyl group to a molecule. TRANSFER RNA AMINOACYLATION is the first step in GENETIC TRANSLATION.
An enzyme that activates serine with its specific transfer RNA. EC 6.1.1.11.
The monoanhydride of carbamic acid with PHOSPHORIC ACID. It is an important intermediate metabolite and is synthesized enzymatically by CARBAMYL-PHOSPHATE SYNTHASE (AMMONIA) and CARBAMOYL-PHOSPHATE SYNTHASE (GLUTAMINE-HYDROLYZING).
A zinc-binding domain defined by the sequence Cysteine-X2-Cysteine-X(9-39)-Cysteine-X(l-3)-His-X(2-3)-Cysteine-X2-Cysteine -X(4-48)-Cysteine-X2-Cysteine, where X is any amino acid. The RING finger motif binds two atoms of zinc, with each zinc atom ligated tetrahedrally by either four cysteines or three cysteines and a histidine. The motif also forms into a unitary structure with a central cross-brace region and is found in many proteins that are involved in protein-protein interactions. The acronym RING stands for Really Interesting New Gene.
Ribonucleic acid in fungi having regulatory and catalytic roles as well as involvement in protein synthesis.
Cytidine 5'-(tetrahydrogen triphosphate). A cytosine nucleotide containing three phosphate groups esterified to the sugar moiety.
A photoactivable URIDINE analog that is used as an affinity label.
A transfer RNA which is specific for carrying cysteine to sites on the ribosomes in preparation for protein synthesis.
The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.
The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
A non-essential amino acid naturally occurring in the L-form. Glutamic acid is the most common excitatory neurotransmitter in the CENTRAL NERVOUS SYSTEM.
An enzyme that, in the course of pyrimidine biosynthesis, catalyzes ring closure by removal of water from N-carbamoylaspartate to yield dihydro-orotic acid. EC 3.5.2.3.
An enzyme that activates aspartic acid with its specific transfer RNA. EC 6.1.1.12.
The biosynthesis of PEPTIDES and PROTEINS on RIBOSOMES, directed by MESSENGER RNA, via TRANSFER RNA that is charged with standard proteinogenic AMINO ACIDS.
A non-essential amino acid present abundantly throughout the body and is involved in many metabolic processes. It is synthesized from GLUTAMIC ACID and AMMONIA. It is the principal carrier of NITROGEN in the body and is an important energy source for many cells.
Mutation process that restores the wild-type PHENOTYPE in an organism possessing a mutationally altered GENOTYPE. The second "suppressor" mutation may be on a different gene, on the same gene but located at a distance from the site of the primary mutation, or in extrachromosomal genes (EXTRACHROMOSOMAL INHERITANCE).
A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.
A large multisubunit complex that plays an important role in the degradation of most of the cytosolic and nuclear proteins in eukaryotic cells. It contains a 700-kDa catalytic sub-complex and two 700-kDa regulatory sub-complexes. The complex digests ubiquitinated proteins and protein activated via ornithine decarboxylase antizyme.
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
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 arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.
Multicomponent ribonucleoprotein structures found in the CYTOPLASM of all cells, and in MITOCHONDRIA, and PLASTIDS. They function in PROTEIN BIOSYNTHESIS via GENETIC TRANSLATION.
A transfer RNA which is specific for carrying asparagine to sites on the ribosomes in preparation for protein synthesis.
The biosynthesis of RNA carried out on a template of DNA. The biosynthesis of DNA from an RNA template is called REVERSE TRANSCRIPTION.
An essential amino acid. It is often added to animal feed.
Established cell cultures that have the potential to propagate indefinitely.
This is the active form of VITAMIN B 6 serving as a coenzyme for synthesis of amino acids, neurotransmitters (serotonin, norepinephrine), sphingolipids, aminolevulinic acid. During transamination of amino acids, pyridoxal phosphate is transiently converted into pyridoxamine phosphate (PYRIDOXAMINE).
Extrachromosomal, usually CIRCULAR DNA molecules that are self-replicating and transferable from one organism to another. They are found in a variety of bacterial, archaeal, fungal, algal, and plant species. They are used in GENETIC ENGINEERING as CLONING VECTORS.
The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Post-transcriptional biological modification of messenger, transfer, or ribosomal RNAs or their precursors. It includes cleavage, methylation, thiolation, isopentenylation, pseudouridine formation, conformational changes, and association with ribosomal protein.
The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups.
Proteins found in any species of bacterium.

Synthesis of aspartyl-tRNA(Asp) in Escherichia coli--a snapshot of the second step. (1/130)

The 2.4 A crystal structure of the Escherichia coli aspartyl-tRNA synthetase (AspRS)-tRNA(Asp)-aspartyl-adenylate complex shows the two substrates poised for the transfer of the aspartic acid moiety from the adenylate to the 3'-hydroxyl of the terminal adenosine of the tRNA. A general molecular mechanism is proposed for the second step of the aspartylation reaction that accounts for the observed conformational changes, notably in the active site pocket. The stabilization of the transition state is mediated essentially by two amino acids: the class II invariant arginine of motif 2 and the eubacterial-specific Gln231, which in eukaryotes and archaea is replaced by a structurally non-homologous serine. Two archetypal RNA-protein modes of interactions are observed: the anticodon stem-loop, including the wobble base Q, binds to the N-terminal beta-barrel domain through direct protein-RNA interactions, while the binding of the acceptor stem involves both direct and water-mediated hydrogen bonds in an original recognition scheme.  (+info)

A missense mutation in the nuclear gene coding for the mitochondrial aspartyl-tRNA synthetase suppresses a mitochondrial tRNA(Asp) mutation. (2/130)

The nuclear suppressor allele NSM3 in strain FF1210-6C/170-E22 (E22), which suppresses a mutation of the yeast mitochondrial tRNA(Asp)gene in Saccharomyces cerevisiae, was cloned and identified. To isolate the NSM3 allele, a genomic DNA library using the vector YEp13 was constructed from strain E22. Nine YEp13 recombinant plasmids were isolated and shown to suppress the mutation in the mitochondrial tRNA(Asp)gene. These nine plasmids carry a common 4. 5-kb chromosomal DNA fragment which contains an open reading frame coding for yeast mitochondrial aspartyl-tRNA synthetase (AspRS) on the basis of its sequence identity to the MSD1 gene. The comparison of NSM3 DNA sequences between the suppressor and the wild-type version, cloned from the parental strain FF1210-6C/170, revealed a G to A transition that causes the replacement of amino acid serine (AGU) by an asparagine (AAU) at position 388. In experiments switching restriction fragments between the wild type and suppressor versions of the NSM3 gene, the rescue of respiratory deficiency was demonstrated only when the substitution was present in the construct. We conclude that the base substitution causes the respiratory rescue and discuss the possible mechanism as one which enhances interaction between the mutated tRNA(Asp)and the suppressor version of AspRS.  (+info)

A domain in the N-terminal extension of class IIb eukaryotic aminoacyl-tRNA synthetases is important for tRNA binding. (3/130)

Cytoplasmic aspartyl-tRNA synthetase (AspRS) from Saccharomyces cerevisiae is a homodimer of 64 kDa subunits. Previous studies have emphasized the high sensitivity of the N-terminal region to proteolytic cleavage, leading to truncated species that have lost the first 20-70 residues but that retain enzymatic activity and dimeric structure. In this work, we demonstrate that the N-terminal extension in yeast AspRS participates in tRNA binding and we generalize this finding to eukaryotic class IIb aminoacyl-tRNA synthetases. By gel retardation studies and footprinting experiments on yeast tRNA(Asp), we show that the extension, connected to the anticodon-binding module of the synthetase, contacts tRNA on the minor groove side of its anticodon stem. Sequence comparison of eukaryotic class IIb synthetases identifies a lysine-rich 11 residue sequence ((29)LSKKALKKLQK(39) in yeast AspRS with the consensus xSKxxLKKxxK in class IIb synthetases) that is important for this binding. Direct proof of the role of this sequence comes from a mutagenesis analysis and from binding studies using the isolated peptide.  (+info)

Metabolism of D-aminoacyl-tRNAs in Escherichia coli and Saccharomyces cerevisiae cells. (4/130)

In Escherichia coli, tyrosyl-tRNA synthetase is known to esterify tRNA(Tyr) with tyrosine. Resulting d-Tyr-tRNA(Tyr) can be hydrolyzed by a d-Tyr-tRNA(Tyr) deacylase. By monitoring E. coli growth in liquid medium, we systematically searched for other d-amino acids, the toxicity of which might be exacerbated by the inactivation of the gene encoding d-Tyr-tRNA(Tyr) deacylase. In addition to the already documented case of d-tyrosine, positive responses were obtained with d-tryptophan, d-aspartate, d-serine, and d-glutamine. In agreement with this observation, production of d-Asp-tRNA(Asp) and d-Trp-tRNA(Trp) by aspartyl-tRNA synthetase and tryptophanyl-tRNA synthetase, respectively, was established in vitro. Furthermore, the two d-aminoacylated tRNAs behaved as substrates of purified E. coli d-Tyr-tRNA(Tyr) deacylase. These results indicate that an unexpected high number of d-amino acids can impair the bacterium growth through the accumulation of d-aminoacyl-tRNA molecules and that d-Tyr-tRNA(Tyr) deacylase has a specificity broad enough to recycle any of these molecules. The same strategy of screening was applied using Saccharomyces cerevisiae, the tyrosyl-tRNA synthetase of which also produces d-Tyr-tRNA(Tyr), and which, like E. coli, possesses a d-Tyr-tRNA(Tyr) deacylase activity. In this case, inhibition of growth by the various 19 d-amino acids was followed on solid medium. Two isogenic strains containing or not the deacylase were compared. Toxic effects of d-tyrosine and d-leucine were reinforced upon deprivation of the deacylase. This observation suggests that, in yeast, at least two d-amino acids succeed in being transferred onto tRNAs and that, like in E. coli, the resulting two d-aminoacyl-tRNAs are substrates of a same d-aminoacyl-tRNA deacylase.  (+info)

Magnesium ion-mediated binding to tRNA by an amino-terminal peptide of a class II tRNA synthetase. (5/130)

Aspartyl-tRNA synthetase is a class II tRNA synthetase and occurs in a multisynthetase complex in mammalian cells. Human Asp-tRNA synthetase contains a short 32-residue amino-terminal extension that can control the release of charged tRNA and its direct transfer to elongation factor 1 alpha; however, whether the extension binds to tRNA directly or interacts with the synthetase active site is not known. Full-length human AspRS, but not amino-terminal 32 residue-deleted, fully active AspRS, was found to bind to noncognate tRNA(fMet) in the presence of Mg(2+). Synthetic amino-terminal peptides bound similarly to tRNA(fMet), whereas little or no binding of polynucleotides, poly(dA-dT), or polyphosphate to the peptides was found. The apparent binding constants to tRNA by the peptide increased with increasing concentrations of Mg(2+), suggesting Mg(2+) mediates the binding as a new mode of RNA.peptide interactions. The binding of tRNA(fMet) to amino-terminal peptides was also observed using fluorescence-labeled tRNAs and circular dichroism. These results suggest that a small peptide can bind to tRNA selectively and that evolution of class II tRNA synthetases may involve structural changes of amino-terminal extensions for enhanced selective binding of tRNA.  (+info)

Human anti-asparaginyl-tRNA synthetase autoantibodies (anti-KS) increase the affinity of the enzyme for its tRNA substrate. (6/130)

Autoantibodies directed against specific human aminoacyl-tRNA synthetases have been associated with a clinical picture including myositis, arthritis, interstitial lung disease and other features that has been referred to as the "anti-synthetase syndrome". Anti-asparaginyl-tRNA synthetase autoantibodies (anti-KS), the most recently described anti-synthetase autoantibodies, are directed against human cytosolic asparaginyl-tRNA synthetase and neutralize specifically its activity. Here we show that these antibodies recognize two epitopes on the human enzyme, an N-terminal epitope reactive in immunoblot experiments and a heat-labile epitope in the catalytic domain. In contrast to the well studied anti-Jo-1 autoantibodies anti-KS when bound to the synthetase increase the affinity of the synthetase for its tRNA substrate and prevent aminoacylation without interfering with the amino acid activation step.  (+info)

A dual-specific Glu-tRNA(Gln) and Asp-tRNA(Asn) amidotransferase is involved in decoding glutamine and asparagine codons in Acidithiobacillus ferrooxidans. (7/130)

The gatC, gatA and gatB genes encoding the three subunits of glutamyl-tRNA(Gln) amidotransferase from Acidithiobacillus ferrooxidans, an acidophilic bacterium used in bioleaching of minerals, have been cloned and expressed in Escherichia coli. As in Bacillus subtilis the three gat genes are organized in an operon-like structure in A. ferrooxidans. The heterologously overexpressed enzyme converts Glu-tRNA(Gln) to Gln-tRNA(Gln) and Asp-tRNA(Asn) to Asn-tRNA(Asn). Biochemical analysis revealed that neither glutaminyl-tRNA synthetase nor asparaginyl-tRNA synthetase is present in A. ferrooxidans, but that glutamyl-tRNA synthetase and aspartyl-tRNA synthetase enzymes are present in the organism. These data suggest that the transamidation pathway is responsible for the formation of Gln-tRNA and Asn-tRNA in A. ferrooxidans.  (+info)

The structure of an AspRS-tRNA(Asp) complex reveals a tRNA-dependent control mechanism. (8/130)

The 2.6 A resolution crystal structure of an inactive complex between yeast tRNA(Asp) and Escherichia coli aspartyl-tRNA synthetase reveals the molecular details of a tRNA-induced mechanism that controls the specificity of the reaction. The dimer is asymmetric, with only one of the two bound tRNAs entering the active site cleft of its subunit. However, the flipping loop, which controls the proper positioning of the amino acid substrate, acts as a lid and prevents the correct positioning of the terminal adenosine. The structure suggests that the acceptor stem regulates the loop movement through sugar phosphate backbone- protein interactions. Solution and cellular studies on mutant tRNAs confirm the crucial role of the tRNA three-dimensional structure versus a specific recognition of bases in the control mechanism.  (+info)

The Escherichia coli tls-1 strain carrying a mutated aspS gene (coding for aspartyl-tRNA synthetase), which causes a temperature-sensitive growth phenotype, was cloned by PCR, sequenced, and shown to contain a single mutation resulting in substitution by serine of the highly conserved proline 555, which is located in motif 3. When an aspS fragment spanning the codon for proline 555 was transformed into the tls-1 strain, it was shown to restore the wild-type phenotype via homologous recombination with the chromosomal tls-1 allele. The mutated AspRS purified from an overproducing strain displayed marked temperature sensitivity, with half-life values of 22 and 68 min (at 42 degrees C), respectively, for tRNA aminoacylation and ATP/PPi exchange activities. Km values for aspartic acid, ATP, and tRNA(Asp) did not significantly differ from those of the native enzyme; thus, mutation Pro555Ser lowers the stability of the functional configuration of both the acylation and the amino acid activation sites but has
FIG. 4. The aminopropyl group increases the efficiency of AspRS inhibition by processed McC. (A) E. coli S30 extracts were incubated in the presence of different concentrations of McC or the McC derivative lacking the aminopropyl group for a time period sufficient for complete processing. Next, the tRNAAsp aminoacylation reaction was carried out. The amounts of aminoacylated tRNAAsp (measured by determining the incorporation of [C14]Asp in trichloroacetic acid-precipitable material) are shown. See reference 10 for experimental details. The curves are representative of curves obtained in three independent experiments. (B) Structural modeling of the interaction of processed McC with E. coli AspRS: surface representation of E. coli AspRS (PDB code 1c0a) (4) residues within 10 Å of bound aspartyl-AMP and modeled processed McC (both shown using ball-and-stick representation). Distances between the modeled position of the propylamine nitrogen atom and side chain oxygen atoms of Glu482 and Asp475 are ...
Metabolic & Genetic Information Center Inborn erros of metabolism LEUKOENCEPHALOPATHY WITH BRAINSTEM AND SPINAL CORD INVOLVEMENT AND LACTATE ELEVATION (LBSL) MITOCHONDRIAL ASPARTYL-tRNA SYNTHETASE DEFICIENCY
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
mitochondrial matrix, mitochondrion, nucleus, aspartate-tRNA ligase activity, aspartate-tRNA(Asn) ligase activity, ATP binding, protein homodimerization activity, tRNA binding, mitochondrial asparaginyl-tRNA aminoacylation, tRNA aminoacylation
TY - JOUR. T1 - Tax incidence on competing two-sided platforms. AU - Belleflamme, Paul. AU - Toulemonde, Eric. PY - 2018/2/1. Y1 - 2018/2/1. N2 - We analyze the effects of various taxes on competing two-sided platforms. First, we consider nondiscriminating taxes. We show that specific taxes are entirely passed to the agents on the side on which they are levied; other agents and platforms are left unaffected. Transaction taxes hurt agents on both sides and benefit platforms. Ad valorem taxes are the only tax instrument that allows the tax authority to capture part of the platforms profits. Second, regarding asymmetric taxes, we show that agents on the untaxed side benefit from the tax. At least one platform, possibly the taxed one, benefits from the tax.. AB - We analyze the effects of various taxes on competing two-sided platforms. First, we consider nondiscriminating taxes. We show that specific taxes are entirely passed to the agents on the side on which they are levied; other agents and ...
Complete information for DARS2 gene (Protein Coding), Aspartyl-TRNA Synthetase 2, Mitochondrial, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
casSAR Dugability of B0SWQ6 | aspS | Aspartate--tRNA(Asp/Asn) ligase - Also known as SYDND_CAUSK, aspS. Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn). Homodimer.
The first mapping calibration test course for Unmanned Aircraft Systems (UAS) will be established by ASPRS at the Reno Stead airport, an FAA-designate...
Uyga berilgan vazifa 4-mashq yuzasidan suhbat.. Sher ifodali oqitladi.. ‒ Sherga nima uchun Tinchlik deb sarlavha qoyilgan?. ‒ Sher necha qtorda iborat?. ‒ Har bir qator oxiriga qanday tinish belgisi qoyilgan?. Doskaga Vatanning sevimli farzandi bolish uchun nima qilish kerak? soroq gapi yoziladi. Bu gap yuzasidan suhbat uyushtiriladi.. Ornini top talimiy oyini otkaziladi. Buning uchun oquvchilar soz birikmalarni oz va kochma manosiga kora chiziqchalar yordamida ajratishlari kerak III. Mustahkamlash.. Darslikda berilgan 5-mashqdagi Kimning xati chiroyli? sheridan olingan parchani ifodali oqitiladi. U qaysi shoirning sheri ekani soraladi.. ‒ Sher necha gapdan tuzilgan?. ‒ Uni qanday aniqladingiz?. ‒ Sher nacha qatordan uborat?. ‒ Har bir qator qanday harf bilan boshlangan? Nima uchun?. Sherni husnixat bilan kochirib bolingach, yozuvdagi kamchiliklarni ozlari aniqlash kerakligi aytiladi.. 6- mashq. Alpomish dostonidan olingan matn ifodali ...
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1B8A: Crystal structure of aspartyl-tRNA synthetase from Pyrococcus kodakaraensis KOD: archaeon specificity and catalytic mechanism of adenylate formation.
We diagnosed three siblings from consanguineous east Asian parents with leukoencephalopathy with brainstem and spinal cord involvement and high lactate (LBSL) from characteristic MRI, MRS findings and a homozygous mutation in the DARS2 gene. The neurological symptoms of the three patients consisted …
Here we demonstrate association of variants in the mitochondrial asparaginyl-tRNA synthetase NARS2 with human hearing loss and Leigh syndrome. A homozygous missense mutation ([c.637G,T; p.Val213Phe]) is the underlying cause of nonsyndromic hearing loss (DFNB94) and compound heterozygous mutations ([c.969T,A; p.Tyr323*] + [c.1142A,G; p.Asn381Ser]) result in mitochondrial respiratory chain deficiency and Leigh syndrome, which is a neurodegenerative disease characterized by symmetric, bilateral lesions in the basal ganglia, thalamus, and brain stem. The severity of the genetic lesions and their effects on NARS2 protein structure cosegregate with the phenotype. A hypothetical truncated NARS2 protein, secondary to the Leigh syndrome mutation p.Tyr323* is not detectable and p.Asn381Ser further decreases NARS2 protein levels in patient fibroblasts. p.Asn381Ser also disrupts dimerization of NARS2, while the hearing loss p.Val213Phe variant has no effect on NARS2 oligomerization. Additionally we ...
Read Properties of the Functioning of the Promoter of the Microcin C51 Operon under Different Conditions of Escherichia coliCell Growth, Russian Journal of Genetics on DeepDyve, the largest online rental service for scholarly research with thousands of academic publications available at your fingertips.
Catalyzes the attachment of the cognate amino acid to the corresponding tRNA in a two-step reaction: the amino acid is first activated by ATP to form a covalent intermediate with AMP and is then transferred to the acceptor end of the cognate tRNA. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma activation and subsequent phosphorylation dissociates from the multisynthetase complex and assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation ...
This gene encodes a member of a multienzyme complex that functions in mediating the attachment of amino acids to their cognate tRNAs. The encoded protein ligates L-aspartate to tRNA(Asp). Mutations in this gene have been found in patients showing hypomyelination with brainstem and spinal cord involvement and leg spasticity. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jun 2014] ...
DKV will offer customers full support during and following the introduction of the new Slovenian toll system DarsGo. DKV also takes care of the toll payment settlemens for its customers. As per today, customers can register for the new toll system through the DKV website. Following this DKV will register the vehicles with toll operator DARS and ensures DARS will sent the post-pay on-board units free of charge to any EU delivery address. Customers can also opt to collect the on-board units from a local DARS customer service point. DKV recommends customers to register and obtain their OBUs quickly in order to avoid delivery bottlenecks and long queues when the toll starts.. Slovenia is switching to a new toll system on 1 April 2018. From that date, access to toll routes will no longer be regulated by toll gates but by the gateless toll system DarsGo. Every vehicle above 3.5 tonnes permitted total weight will require a vehicle-specific toll box (OBU) and must be registered for the new toll system. ...
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Putative Protein Of Unknown Function; Green Fluorescent Protein (GFP)-fusion Protein Localizes To The Cytoplasm And Nucleus; Contains Ankyrin (Ank) Repeats; YCR051W Is Not An Essential Gene
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 ...
Read Activation of the expression of the microcin C51 operon upon glucose starvation of cells at the exponential growth phase, Russian Journal of Genetics on DeepDyve, the largest online rental service for scholarly research with thousands of academic publications available at your fingertips.
We at vom Aztlan Rottweilers We at vom Aztlan Rottweilers we import exceptional Rottweilers for those interested in a quality ADRK German bred dog. We are a COE Rottweiler Importer. In Germany, there are also problematic issues concerning the breeding of Rottweiler these days. With a limited number of approved stud dogs available and the growing demand for German Rottweilers overseas our gene pool continues to get smaller and smaller. For us the use of a stud dog after it has been sold overseas is not an option. As the quality of a producer can only be viewed through his products were left with a lot of guessing work with most of the males being sold before we ever get to see the actual product. Modern techniques such as DNA or shipping of semen are currently prohibited in Germany as is using bloodlines worldwide.
We at vom Aztlan Rottweilers We at vom Aztlan Rottweilers we import exceptional Rottweilers for those interested in a quality ADRK German bred dog. We are a COE Rottweiler Importer. In Germany, there are also problematic issues concerning the breeding of Rottweiler these days. With a limited number of approved stud dogs available and the growing demand for German Rottweilers overseas our gene pool continues to get smaller and smaller. For us the use of a stud dog after it has been sold overseas is not an option. As the quality of a producer can only be viewed through his products were left with a lot of guessing work with most of the males being sold before we ever get to see the actual product. Modern techniques such as DNA or shipping of semen are currently prohibited in Germany as is using bloodlines worldwide.
Non-discriminating cancer therapies, including chemotherapy and radiation, marginally differentiate between tumour and healthy cells...
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TY - JOUR. T1 - Biosynthesis of the RiPP trojan horse nucleotide antibiotic microcin C is directed by the N-formyl of the peptide precursor. AU - Dong, Shi Hui. AU - Kulikovsky, Alexey. AU - Zukher, Inna. AU - Estrada, Paola. AU - Dubiley, Svetlana. AU - Severinov, Konstantin. AU - Nair, Satish K.. PY - 2019/1/1. Y1 - 2019/1/1. N2 - Microcin C7 (McC) is a peptide antibiotic modified by a linkage of the terminal isoAsn amide to AMP via a phosphoramidate bond. Post-translational modification on this ribosomally produced heptapeptide precursor is carried out by MccB, which consumes two equivalents of ATP to generate the N-P linkage. We demonstrate that MccB only efficiently processes the precursor heptapeptide that retains the N-formylated initiator Met (fMet). Binding studies and kinetic measurements evidence the role of the N-formyl moiety. Structural data show that the N-formyl peptide binding results in an ordering of residues in the MccB crossover loop, which dictates specificity in ...
As a result of considerable discussion at the recent American Society for Photogrammetry and Remote Sensing (ASPRS) 2011 Annual Conference in Milwaukee, Wisconsin, the U.S. Geological Survey (USGS) has reversed its original decision to discontinue film camera calibration.
In Escherichia coli, chromosome replication is initiated from oriC by the DnaA initiator protein associated with ATP. Three non-coding regions contribute to the activity of DnaA. The datA locus is instrumental in conversion of DnaAATP to DnaAADP (DDAH; datA dependent DnaAATP hydrolysis) whereas DnaA rejuvenation sequences 1 and 2 (DARS1 and DARS2) reactivate DnaAADP to DnaAATP. The structural organization of oriC, datA, DARS1 and DARS2 were found conserved between 59 fully sequenced E. coli genomes, with differences primarily in the non-functional spacer regions between key protein binding sites. The relative distances from oriC to datA, DARS1 and DARS2, respectively, was also conserved despite of large variations in genome size, suggesting that the gene dosage of either region is important for bacterial growth. Yet all three regions could be deleted alone or in combination without loss of viability. Competition experiments during balanced growth in rich medium and during mouse colonization indicated
Hypothetical protein; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp- tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln) (By similarity) (104 aa ...
Roman Rottweiler information, Photos, Q & A and Reviews. Also learn about training and care. Ask Roman Rottweiler questions and view photos. We provide a complete guide for the breed. Learn about Roman Rottweiler characteristics and owernship requirements.
The Rottweiler Coonhound mix dog can be a great choice for an active person or family who wants to make their dog the center of daily life
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The Rottweiler has a dubious reputation for being an excellent guard dog. Anyone who has lived with this gentle giant knows their protective nature is c...
Tripawds is a user-supported community. Thank you for your support!First the good news, Nikki had appointments with both Dr. Pyne and Dr. Friedly this week, and in both cases the results were fantastic!! Dr. Pyne declared the seroma as completely healed, and said that Nikki is doing very well for this stage of the game. […]. ...
Download: http://www.dars.state.tx.us/dhhs/trilingualsurvey2012.docx Texas DARS-DHHS is conducting a Trilingual training needs assessment and would like to hear from you! Please provide your recommendations for future training. Fill out the survey and return to [email protected]
Lyrics to Lets Get It (Remix) song by G-DEP: They said that Im a Rottweiler And Im from the Rottweiler house, the Rottweiler New York We...
NEW - A complete alphabetical list of ARC Carting Titles (Rottweilers and other breeds) from 2000 thru 1st Qtr. 2016 in Award Information & Top 10 Standings under Top 10 Carting. ...
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Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu). In mitochondria, constitutes the nondiscriminating glutamyl-tRNA synthase that generates the mitochondrial mischarged glutamyl-tRNA(Gln) substrate for the tRNA-dependent amidotransferase (AdT), which generates mitochondrial glutaminyl-tRNA(Gln) by transamidation of glutamyl-tRNA(Gln).
1 - How and why did you come about starting Dars records?. I started work on the Dars Records label in 2003, because I really wanted to publish this kind of music and music I loved by Russian musicians though I had not thought of it as a business. I myself created music at the time, in such styles of electronic music as IDM and ambient so this was a very personal project for me.. 2 - When you started Dars records, were there any labels that you could say were a reference/inspiration for your efforts?. I admired labels like Warp releases, Merck, Morr music, Skam and Sonig but, in Russia, their releases were very difficult to find. Now everything has changed.. In the history of Russia IDM started with the label Art-Tek, whose leaders are Roman Belavkin (Solar X) and Jura Murash. Currently there are other labels issuing IDM and IDM-related music - such as Shaped Harmonics (Moscow), Kama Records (Izhevsk), Zvezda Records, Cheburec Records (St. Petersburg), Exotica Records (Moscow). Among the ...
This version of Dars has all of the same texture high points of the other varieties of Dars. It also has the same tendency to start melting in your fingers if you handle it too much at room temperature. If you buy any type of Dars, its better to keep them refrigerated and then eat them by melting them slowly in your mouth. This particular variety smells like mild chocolate despite the fact that it is coffee flavored. In fact, this tastes a lot like a soft center premium candy (like those from Sees) with a coffee filling. There are milk chocolate notes, but mainly it has a pretty nice, rich coffee flavor. The part of this which is supposed to be like vanilla ice cream is very subdued. It comes across mainly as an aftertaste of vanilla beans ...
A very lovely and beautiful pedigree female rottweiler is available. At just 16 weeks of age and with her distinct black and tan color,large box head,and large body she is a must have to breeders or wants to improve their breeding project or dog lovers who wants to experience what a pedigree rottweiler looks like ...
Meet Dozer the American Pit Bull Terrier / Rottweiler on the Daily Puppy. Read about Dozer, the American Pit Bull Terrier / Rottweiler or any other breed of dog. Connect with other dog owners on DailyPuppy.com.
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4/8/2011 · My boyfriend has always had a rottweiler and has shown interest in getting another one once we get our first house together. I myself am scared so bad of rottweilers and am very hesitant to allow one into our home (especially if there are to be kids in the future) I know it would mean a lot to my boyfriend if I could get over my fear but all the research I do on the breed scares me even more ...
Question: I have a mature Rottweiler and recently got a handsome Pitbull. It seems like my Rott had some kind of skin condition since she had some growths
The team, led by Dr Ryan Taft from The University of Queenslands Institute for Molecular Bioscience (IMB), used genome sequencing to determine that three-year-old Massimo Damiani is suffering from a congenital disease previously unknown to medicine. We analysed the genome sequences of Massimo and his parents using a method called whole genome sequencing and found that a mutation in the DARS gene was likely causing his disorder, Dr Taft said. In collaboration with clinicians from the Netherlands, Australia, and the US we then examined the genomes of nine other children who appeared to be suffering from the same disease and the genomes of their parents and confirmed that they all had mutations in the DARS gene. This gene has never previously been associated with human disease and may not have been identified as the culprit using any other method, he said. The team, comprised of experts from the IMB in Brisbane, VU University Medical Center in Amsterdam, Murdoch Childrens Research Institute ...
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Everything you want to know about Rottweilers including grooming, training, health problems, history, adoption, finding good breeder and more.
Aspartate-tRNA ligase GRCh38: Ensembl release 89: ENSG00000115866 - Ensembl, May 2017 GRCm38: Ensembl release 89: ... Aspartyl-tRNA synthetase charges its cognate tRNA with aspartate during protein biosynthesis. Mutations in DARS have been ... Aspartyl-tRNA synthetase, cytoplasmic is an enzyme that in humans is encoded by the DARS gene. Aspartyl-tRNA synthetase (DARS) ... Reed VS, Wastney ME, Yang DC (1995). "Mechanisms of the transfer of aminoacyl-tRNA from aminoacyl-tRNA synthetase to the ...
In enzymology, an aspartate-tRNA ligase (EC 6.1.1.12) is an enzyme that catalyzes the chemical reaction ATP + L-aspartate + ... L-aspartate, and tRNA(Asp), whereas its 3 products are AMP, diphosphate, and L-aspartyl-tRNA(Asp). This enzyme belongs to the ... The systematic name of this enzyme class is L-aspartate:tRNAAsp ligase (AMP-forming). Other names in common use include ... This enzyme participates in alanine and aspartate metabolism and aminoacyl-trna biosynthesis. As of late 2007, 10 structures ...
... and Ala-tRNA synthetase. This enzyme participates in alanine and aspartate metabolism and aminoacyl-trna biosynthesis. Sticky ... In enzymology, an alanine-tRNA ligase (EC 6.1.1.7) is an enzyme that catalyzes the chemical reaction ATP + L-alanine + tRNAAla ... and L-alanyl-tRNA(Ala). This enzyme belongs to the family of ligases, to be specific those forming carbon-oxygen bonds in ... alanine-transfer RNA ligase, alanine transfer RNA synthetase, alanine tRNA synthetase, alanine translase, alanyl-transfer ...
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). ...
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, ... aspartate:tRNAAsx ligase (AMP-forming). This enzyme catalyses the following chemical reaction ATP + L-aspartate + tRNAAsx ⇌ {\ ... This enzyme belongs to the family of ligases, to be specific those forming carbon-oxygen bonds in aminoacyl-tRNA and related ...
... 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 ...
... 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 ... threonine-tRNA ligase EC 6.1.1.4: leucine-tRNA ligase EC 6.1.1.5: isoleucine-tRNA ligase EC 6.1.1.6: lysine-tRNA ligase EC 6.1. ... 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 ... phenylalanine-tRNA ligase EC 6.1.1.21: histidine-tRNA ligase EC 6.1.1.22: asparagine-tRNA ligase EC 6.1.1.23: aspartate-tRNAAsn ...
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 ...
... ubiquitin protein ligase E3 component n-recognin 2 (6p21.2) UNC5CL: encoding protein Unc-5 homolog C (C. elegans)-like VEGF: ... D-aspartate) O-methyltransferase (6q25.1) PERP: p53 apoptosis effector related to PMP-22 (6q23.3) PKIB: cAMP-dependent protein ... "genetype trna"[Properties] OR "genetype scrna"[Properties] OR "genetype snrna"[Properties] OR "genetype snorna"[Properties]) ... E3 ubiquitin protein ligase 1 (6q21) HEBP2: heme binding protein 2 (6q24.1) IDDM8: insulin dependent diabetes mellitus 8 IDDM15 ...
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 ... Once the tRNA is charged, a ribosome can transfer the amino acid from the tRNA onto a growing peptide, according to the genetic ...
... the enzyme catalyzing the biosynthesis of the cyanobacterial reserve material multi-L-arginyl-poly-L-aspartate (cyanophycin)". ... Enzymes: CO CS and CN ligases (EC 6.1-6.3). 6.1: Carbon-Oxygen. *Aminoacyl tRNA synthetase *Alanine ... Stage two involves four key Mur ubiquitin ligase enzymes: MurC (EC),[1] MurD (EC),[2] MurE (EC) [3] and MurF (EC).[4] These ... 6-diaminopimelate ligase (MurE), and UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase (MurF). This entry also includes ...
Aminoacyl tRNA synthetase *Alanine. *Arginine. *Asparagine. *Aspartate. *Cysteine. *D-alanine-poly(phosphoribitol) ligase ... 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. ...
... aspartate 1-decarboxylase EC 4.1.1.12: aspartate 4-decarboxylase EC 4.1.1.13: deleted EC 4.1.1.14: valine decarboxylase EC 4.1. ... 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 ... 3-hydroxy-D-aspartate aldolase EC 4.1.99.1: tryptophanase EC 4.1.99.2: tyrosine phenol-lyase EC 4.1.99.3: deoxyribodipyrimidine ...
... 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 ( ... aspartate kinase EC 2.7.2.5: now EC 6.3.4.16 EC 2.7.2.6: formate kinase EC 2.7.2.7: butyrate kinase EC 2.7.2.8: acetylglutamate ... 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 guanosine-2'-O-methyltransferase EC 2.1.1.35: tRNA (uracil-5-)-methyltransferase EC 2.1.1.36: tRNA (adenine-N1-)- ...
Aminoacyl tRNA synthetase *Alanine. *Arginine. *Asparagine. *Aspartate. *Cysteine. *D-alanine-poly(phosphoribitol) ligase ... glutamate-ammonia ligase. Active site between two monomers of glutamine synthetase from Salmonella typhimurium. Cation binding ...
Aminoacyl tRNA synthetase *Alanine. *Arginine. *Asparagine. *Aspartate. *Cysteine. *D-alanine-poly(phosphoribitol) ligase ...
Aminoacyl tRNA synthetase *Alanine. *Arginine. *Asparagine. *Aspartate. *Cysteine. *D-alanine-poly(phosphoribitol) ligase ... 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 ...
Aminoacyl tRNA synthetase *Alanine. *Arginine. *Asparagine. *Aspartate. *Cysteine. *D-alanine-poly(phosphoribitol) ligase ... 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 ...
... is an enzyme with systematic name L-aspartate:L-glutamine amido-ligase (AMP-forming).[1][2][3][4][5][6] This enzyme catalyses ... Enzymes: CO CS and CN ligases (EC 6.1-6.3). 6.1: Carbon-Oxygen. *Aminoacyl tRNA synthetase *Alanine ... ATP + L-aspartate + L-glutamine + H2O ⇌. {\displaystyle \rightleftharpoons }. AMP + diphosphate + L-asparagine + L-glutamate ( ... 1b) ATP + L-aspartate + NH3 ⇌. {\displaystyle \rightleftharpoons }. AMP + diphosphate + L-asparagine. The enzyme from ...
The fluorinated analog is incorporated into peptides via the relaxed substrate specificity of histidine-tRNA ligase and lowers ... for nickel and carboxyl-methyl aspartate (Co-CMA) for cobalt, which the polyhistidine-tag binds with micromolar affinity. Ernst ...
... tRNA ↽ − − ⇀ aminoacyl − tRNA + AMP {\displaystyle {\ce {{Aminoacyl-AMP}+ tRNA <=> {aminoacyl-tRNA}+ AMP}}} The combination of ... The biosynthesis of aspartate is a one step reaction that is catalyzed by a single enzyme. The enzyme aspartate ... Okazaki fragments are covalently joined by DNA ligase to form a continuous strand. Then, to complete DNA replication, RNA ... This reaction, called tRNA charging, is catalyzed by aminoacyl tRNA synthetase. A specific tRNA synthetase is responsible for ...
Mitochondrial tRNA genes have different sequences from the nuclear tRNAs but lookalikes of mitochondrial tRNAs have been found ... Reducing equivalents from the cytoplasm can be imported via the malate-aspartate shuttle system of antiporter proteins or feed ... 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 ...
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: ... L-seryl-tRNA(Sec) selenium transferase EC 2.9.1.2: O-phospho-L-seryl-tRNA(Sec):L-selenocysteinyl-tRNA synthase Hydrolytic ... EC 2.1.3 Aspartate transcarbamoylase EC 2.1.3.2 Ornithine transcarbamoylase EC 2.1.3.3 Category:EC 2.2.1 Transketolase EC 2.2. ... 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- ...
The enzyme is not a serine protease, as thought previously, but an aspartate protease EC 3.4.21.88: Repressor LexA EC 3.4.21.89 ... tRNA-intron endonuclease EC 3.1.27.10: rRNA endonuclease EC 3.1.30.1: Aspergillus nuclease S1 EC 3.1.30.2: Serratia marcescens ... glutamate-ammonia ligase) hydrolase EC 3.1.4.16: 2',3'-cyclic-nucleotide 2'-phosphodiesterase EC 3.1.4.17: 3',5'-cyclic- ... N-acyl-D-aspartate deacylase EC 3.5.1.84: biuret amidohydrolase EC 3.5.1.85: (S)-N-acetyl-1-phenylethylamine hydrolase EC 3.5. ...
"tRNA / transfer RNA". Learn Science at Scitable.. *^ "Myoclonic epilepsy with ragged-red fibers". Genetics Home Reference. U.S ... Glutamate aspartate transporter. *Glycerol-3-phosphate dehydrogenase. *ATP synthase. *Carnitine palmitoyltransferase II ... Mitochondrially encoded tRNA isoleucine also known as MT-TI is a transfer RNA which in humans is encoded by the mitochondrial ... "MT-TI mitochondrially encoded tRNA isoleucine [Homo sapiens (human)] - Gene - NCBI". www.ncbi.nlm.nih.gov.. ...
"TRDMT1 tRNA aspartic acid methyltransferase 1 (Homo sapiens)". Entrez Gene. NCBI. 2010-11-01. Retrieved 2010-11-07.. ... Aspartate carbamoyltransferase. *Ornithine carbamoyltransferase. *Oxamate carbamoyltransferase. *Putrescine ... tRNA aspartic acid methyltransferase 1) to better reflect its biological function.[23] TRDMT1 is the first RNA cytosine ... "Methylation of tRNAAsp by the DNA Methyltransferase Homolog Dnmt2". Science. 311 (5759): 395-398. doi:10.1126/science.1120976 ...
Glutamate aspartate transporter. *Glycerol-3-phosphate dehydrogenase. *ATP synthase. *Carnitine palmitoyltransferase II ...
Glutamate aspartate transporter. *Glycerol-3-phosphate dehydrogenase. *ATP synthase. *Carnitine palmitoyltransferase II ...
tRNA biogenesis[edit]. In eukaryotic cells, tRNAs are transcribed by RNA polymerase III as pre-tRNAs in the nucleus.[53] RNA ... Both tRNAs are modeled as phenylalanine-specific tRNA from Escherichia coli, with the A/T tRNA as a homology model of the ... aminoacyl-AMP + tRNA → aminoacyl-tRNA + AMP. Certain organisms can have one or more aminoacyl tRNA synthetases missing. This ... Thus, glutamate tRNA synthetase charges tRNA-glutamine(tRNA-Gln) with glutamate. An amidotransferase then converts the acid ...
... belongs to the class V group of aspartate aminotransferase superfamily of structurally homologous pyridoxal 5'- ...
In enzymology, an aspartate-tRNA ligase (EC 6.1.1.12) is an enzyme that catalyzes the chemical reaction ATP + L-aspartate + ... L-aspartate, and tRNA(Asp), whereas its 3 products are AMP, diphosphate, and L-aspartyl-tRNA(Asp). This enzyme belongs to the ... The systematic name of this enzyme class is L-aspartate:tRNAAsp ligase (AMP-forming). Other names in common use include ... This enzyme participates in alanine and aspartate metabolism and aminoacyl-trna biosynthesis. As of late 2007, 10 structures ...
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, ... aspartate:tRNAAsx ligase (AMP-forming). This enzyme catalyses the following chemical reaction ATP + L-aspartate + tRNAAsx ⇌ {\ ... This enzyme belongs to the family of ligases, to be specific those forming carbon-oxygen bonds in aminoacyl-tRNA and related ...
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- ... ATP + L-aspartate + tRNAAsp = AMP + diphosphate + L-aspartyl-tRNAAsp. UniProt ... Is specific for tRNA(Asp) since it aspartylates tRNA(Asn) 3 orders of magnitude less efficiently than tRNA(Asp). UniProt ... AMP and then transferred to the acceptor end of tRNA(Asp). ...
ATP + L-aspartate + tRNAAsx = AMP + diphosphate + L-aspartyl-tRNAAsx. UniProt ... Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also ... Is 1.5 times more efficient at aminoacylating E.coli tRNA(Asp) over tRNA(Asn). Reaction proceeds in two steps: L-aspartate is ... first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn). UniProt ...
L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp). ... Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: ... IPR004364 Aa-tRNA-synt_II. IPR006195 aa-tRNA-synth_II. IPR004524 Asp-tRNA-ligase_1. IPR002312 Asp/Asn-tRNA-synth_IIb. IPR004115 ... IPR004364 Aa-tRNA-synt_II. IPR006195 aa-tRNA-synth_II. IPR004524 Asp-tRNA-ligase_1. IPR002312 Asp/Asn-tRNA-synth_IIb. IPR004115 ...
... is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA. ... Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid (AA) ... IPR004364, Aa-tRNA-synt_II. IPR006195, aa-tRNA-synth_II. IPR004523, Asp-tRNA_synthase_2. IPR002312, Asp/Asn-tRNA-synth_IIb ... IPR004364, Aa-tRNA-synt_II. IPR006195, aa-tRNA-synth_II. IPR004523, Asp-tRNA_synthase_2. IPR002312, Asp/Asn-tRNA-synth_IIb ...
... tRNA(Asp/Asn) ligase - Also known as SYDND_CAUSK, aspS. Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able ... to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first ... activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn). Homodimer. ... Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also ...
... tRNA ligase (aspS) datasheet and description hight quality product and Backed by our Guarantee ... tRNA ligase (aspS). Alternative names: Aspartate--tRNA ligase, Aspartyl-tRNA synthetase, aspartyl-tRNA synthetase, aspartyl- ... Chlamydia trachomatis serovar L2b Aspartate tRNA ligase (aspS). Short name: Chlamydia trachomatis serovar L2b Aspartate--tRNA ... Aspartate--tRNA ligase (aspS) is a recombinant protein expressed in E. ...
Aspartate-tRNA Ligase. Supplementary concept. *Leukoencephalopathy with Brainstem and Spinal Cord Involvement and Lactate ... Pathogenic mutations causing LBSL affect mitochondrial aspartyl-tRNA synthetase in diverse ways.. van Berge L1, Kevenaar J, ... mitochondrial aspartyl-tRNA synthetase). Generally, patients are compound heterozygous for mutations in DARS2. Many different ... Aspartate-tRNA Ligase/deficiency. *Aspartate-tRNA Ligase/genetics*. *Aspartate-tRNA Ligase/metabolism* ...
... tRNA(Asp/Asn) ligase. Chlorobium phaeobacteroides (strain DSM 266) ... Aspartate--tRNA(Asp/Asn) ligase UniProtKBInterProSTRINGInteractive Modelling. 606 aa; Sequence (Fasta) ... OB-fold nucleic acid binding domain, AA-tRNA synthetase-type. IPR004365PF01336. ...
Aspartate-tRNA Ligase / genetics* * Brain Stem / pathology* * Cerebellum / pathology * Cerebellum / ultrastructure * Child ... We discussed the relationship between deficits in mitochondrial aspartyl-tRNA synthetase activity and the neuropathology ...
Aspartate tRNA ligase 2 mitochondrial antibody. *Aspartate tRNA ligase antibody. *Aspartate tRNA ligase mitochondrial antibody ... Belongs to the class-II aminoacyl-tRNA synthetase family. ... Aspartate--tRNA ligase antibody. *Aspartyl tRNA synthetase 2 ( ...
Trna binding. Specific Function. Not Available. Gene Name. DARS2. Uniprot ID. Q6PI48. Uniprot Name. Aspartate--tRNA ligase, ... UAspartate--tRNA ligase, cytoplasmic. Not Available. Human. UCalcium-binding mitochondrial carrier protein Aralar1. Not ... It is hypothesized that L-aspartate, especially the potassium magnesium aspartate salt, spares stores of muscle glycogen and/or ... L-aspartate is a glycogenic amino acid, and it can also promote energy production via its metabolism in the Krebs cycle. These ...
Aspartyl-TRNA Synthetase 2, Mitochondrial, including: function, proteins, disorders, pathways, orthologs, and expression. ... aminoacyl-tRNA ligase activity. IEA. --. GO:0004815. aspartate-tRNA ligase activity. TAS. --. ... ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp). *SYDM_HUMAN,Q6PI48 ... The protein encoded by this gene belongs to the class-II aminoacyl-tRNA synthetase family. It is a mitochondrial enzyme that ...
... aspartate-tRNA ligase (ARS; unigene18089), prolyl-tRNA synthase (PRS; unigene16762), acetoacetyl-CoA synthase (ACS; ... aspartate aminotransferase (AST; unigene12484), alanine aminotransferase (MAC; unigene9129), ...
aspartate-trna ligase activity. asparagine-trna ligase activity. nucleic acid binding. ligase activity, forming carbon-oxygen ... Showing Protein Asparagine--tRNA ligase, cytoplasmic (HMDBP00611). IdentificationBiological propertiesGene propertiesProtein ... Adenosine triphosphate + L-Asparagine + tRNA(Asn) → Adenosine monophosphate + Pyrophosphate + L-asparaginyl-tRNA(Asn). details ... Adenosine triphosphate + L-Asparagine + tRNA(Asn) → Adenosine monophosphate + Pyrophosphate + L-Asparaginyl-tRNA(Asn). details ...
aspartate--tRNA ligase DPS1. protein-coding. GLE1. nucleoporin GLE1. protein-coding. YHL050C. hypothetical protein. protein- ...
aspartate-tRNA ligase activity. 0.504302440847948. bayes_pls_golite062009. nucleotidyltransferase activity. 0.325774164899685. ... ligase activity, forming carbon-oxygen bonds. 2.04350689362549. bayes_pls_golite062009. aminoacyl-tRNA ligase activity. ... ligase activity, forming aminoacyl-tRNA and related compounds. 2.04350689362549. bayes_pls_golite062009. ... ligase activity. 1.06979791212194. bayes_pls_golite062009. sequence-specific DNA binding. 0.85691075793641. bayes_pls_ ...
Aspartyl-tRNA synthetase, cytoplasmic (Aspartate--tRNA ligase) (AspRS) [nr-271106-contam.fasta] *aspartyl-tRNA synthetase [ ... gi,135100,sp,P04802.3,SYDC_YEAST RecName: Full=Aspartyl-tRNA synthetase, cytoplasmic; AltName: Full=Aspartate--tRNA ligase; ... pir,,SYBYDC aspartate-tRNA ligase (EC 6.1.1.12), cytosolic [validated] - yeast (Saccharomyces cerevisiae) [NCBI NR] *gi,6323011 ... Aspartate--tRNA ligase, cytoplasmic OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=DPS1 PE=1 SV=3 [UniProt_S_ ...
spet:CEP67_02620 aspartate--tRNA ligase K01876 588 105 ( -) 30 0.304 102 -, 1 spoi:IMCC21906_00974 Cytochrome P450 223 105 ... slt:Slit_2716 D-alanine/D-alanine ligase K01921 309 107 ( -) 30 0.410 61 ,-, 1 bpsi:IX83_06960 transcription-repair coupling ... aoi:AORI_6599 AMP-dependent synthetase and ligase 925 139 ( 7) 38 0.354 82 -, 5 fal:FRAAL4012 putative cytochrome P450 405 139 ... sacz:AOT14_14760 tRNA delta(2)-isopentenylpyrophosphate K00791 317 108 ( -) 30 0.323 130 -, 1 shx:MS3_10538 A-kinase anchor ...
parc:CI960_11210 aspartate--tRNA(Asp/Asn) ligase K01876 585 104 ( -) 30 0.345 87 -, 1 pcr:Pcryo_2062 peptidase M48, Ste24p 270 ... sft:NCTC1_03981 DNA ligase B,DNA ligase B,NAD-dependent K01972 560 100 ( -) 29 0.304 102 ,-, 1 sfx:S4082 putative enzyme K01972 ... sfe:SFxv_4015 DNA ligase B K01972 562 100 ( -) 29 0.304 102 ,-, 1 sfl:SF3686 NAD-dependent DNA ligase LigB K01972 560 100 ( -) ... sfn:SFy_5253 NAD-dependent DNA ligase adenylation domai K01972 505 100 ( -) 29 0.304 102 ,-, 1 sfs:SFyv_5328 NAD-dependent DNA ...
The DARS2 gene provides instructions for making an enzyme called mitochondrial aspartyl-tRNA synthetase. Learn about this gene ... aspartate tRNA ligase 2, mitochondrial. *aspartyl-tRNA synthetase, mitochondrial. *aspartyl-tRNA synthetase, mitochondrial ... Mitochondrial aspartyl-tRNA synthetase attaches the amino acid aspartic acid to the correct tRNA, which helps ensure that ... Each tRNA carries a specific amino acid to the growing chain. Enzymes called aminoacyl-tRNA synthetases, including ...
Aspartyl-TRNA Synthetase 1, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The ... Aspartate TRNA Ligase 1, Cytoplasmic 2 3 * Aspartate--TRNA Ligase, Cytoplasmic 3 4 ... Reaction=ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp); Xref=Rhea:RHEA:19649, Rhea:RHEA-COMP:9660, ... Lysyl-tRNA synthetase interacts with EF1alpha, aspartyl-tRNA synthetase and p38 in vitro. (PMID: 18029264) Guzzo CM … Yang DC ( ...
Aspartate--tRNA ligase. Alternative Name(s). Aspartic acid translase.. Aspartyl-tRNA synthetase.. ...
Aspartate--tRNA(Asn) ligase. Alternative Name(s). Nondiscriminating aspartyl-tRNA synthetase.. Reaction catalysed. ... The aspartate-tRNA(Asn) is not used in protein synthesis until it is converted by EC 6.3.5.6 into asparaginyl-tRNA(Asn). ... This relaxation of specificity has been found to result from the absence of a loop in the tRNA that specifically recognizes the ... This accounts for the ability of this enzyme in, for example, Thermus thermophilus, to recognize both tRNA(Asp) (GUC anticodon ...
Crystal structure of the archaeal asparagine synthetase: interrelation with aspartyl-tRNA and asparaginyl-tRNA synthetases ... Information on EC 6.3.1.1 - aspartate-ammonia ligase. for references in articles please use BRENDA:EC6.3.1.1 ... Alanine, aspartate and glutamate metabolism, Biosynthesis of secondary metabolites, Cyanoamino acid metabolism ... Asparagine synthetase is an enzyme that catalyzes the synthesis of asparagine from aspartate using ATP as the energy source in ...
Expression pattern of the aspartyl-tRNA synthetase DARS in the human brain. Fröhlich, D., Suchowerska, A. K., Voss, C., He, R ... In vivo characterization of the aspartyl-tRNA synthetase DARS: homing in on the leukodystrophy HBSL. Fröhlich, D., Suchowerska ...
Aspartate-transfer ribonucleic acid ligase Current Synonym true false 97691011 Aspartate-tRNA ligase Current Synonym true false ... Aspartate-transfer ribonucleic acid ligase (substance). Code System Preferred Concept Name. Aspartate-transfer ribonucleic acid ... Enzyme (substance) {90668006 , SNOMED-CT } Substance with ligase mechanism of action (substance) {1672007 , SNOMED-CT } ...
... aspartate tRNA synthase, DNA ligase, basic-domain leucine zipper DNA binding protein, ATP-binding cassette transporter, and ... aspartate tRNA synthase, DNA ligase, basic-domain leucine zipper DNA binding protein, ATP-binding cassette transporter, and ...
... "aspartate--tRNA(Asp/Asn) ligase" /protein_id="WP_004683546.1" /translation="MHRYRSHTCAALRKTDVGSNVRLSGWVHRVRDHGGILFIDLRDH ... tRNA ligase subunit alpha" /protein_id="WP_004688025.1" /translation="MHPTRSFQGLILTLHNYWAEHGCAILQPYDMEVGAGTFHPATTL ... tRNA ligase subunit beta" /protein_id="WP_004690587.1" /translation="MPDLLLELFSEEIPARMQRKAAGDLKKMITDGLVDAGLTYEAAT ... tRNA ligase" /protein_id="WP_004684672.1" /translation="MSTFKPLVFSGVQPTGNLHLGNYLGAIKRWVEVQKTEECIYCVV ...
  • In enzymology, an aspartate-tRNA ligase (EC 6.1.1.12) is an enzyme that catalyzes the chemical reaction ATP + L-aspartate + tRNAAsp ⇌ {\displaystyle \rightleftharpoons } AMP + diphosphate + L-aspartyl-tRNAAsp The 3 substrates of this enzyme are ATP, L-aspartate, and tRNA(Asp), whereas its 3 products are AMP, diphosphate, and L-aspartyl-tRNA(Asp). (wikipedia.org)
  • When this enzyme acts on tRNAAsp, it catalyses the same reaction as EC 6.1.1.12, aspartate---tRNA ligase. (wikipedia.org)
  • When this enzyme acts on tRNA(Asp), it catalyzes the same reaction as EC 6.1.1.12 . (expasy.org)
  • The aspartyl-tRNAAsn is not used in protein synthesis until it is converted by EC 6.3.5.6, asparaginyl-tRNA synthase (glutamine-hydrolysing), into asparaginyl-tRNAAsn. (wikipedia.org)
  • The protein encoded by this gene belongs to the class-II aminoacyl-tRNA synthetase family. (genecards.org)
  • DARS2 (Aspartyl-TRNA Synthetase 2, Mitochondrial) is a Protein Coding gene. (genecards.org)
  • During protein synthesis, in either the mitochondria or the cytoplasm, a type of RNA called transfer RNA (tRNA) helps assemble protein building blocks (amino acids) into a chain that forms the protein. (medlineplus.gov)
  • Mitochondrial aspartyl-tRNA synthetase attaches the amino acid aspartic acid to the correct tRNA, which helps ensure that aspartic acid is added at the proper place in the mitochondrial protein. (medlineplus.gov)
  • The encoded protein ligates L-aspartate to tRNA(Asp). (genecards.org)
  • DARS1 (Aspartyl-TRNA Synthetase 1) is a Protein Coding gene. (genecards.org)
  • Finally, the N-terminal domain of the predicted ddAsnRS protein shows higher sequence similarity to Glutaminyl tRNA synthetases than to other Asn tRNA synthetases. (bvsalud.org)
  • In addition to its role in protein synthesis, aspartyl-tRNA synthetase may have other functions that are not fully understood. (medlineplus.gov)
  • We also identify a paralogous version of the methionyl-tRNA synthetase, which is widespread in bacteria, and present evidence using contextual information that it might function independently of protein synthesis as a peptide ligase in the formation of a peptide- derived secondary metabolite. (biomedcentral.com)
  • 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)
  • Using sensitive sequence analysis methods we show that PafA, the protein required for pupylation, belongs to the glutamine synthetase fold and predict that it is likely to catalyze an ATP-dependent peptide ligase reaction. (biomedcentral.com)
  • CDC64 encodes cytoplasmic alanyl-tRNA synthetase, Ala1p, of Saccharomyces cerevisiae. (harvard.edu)
  • This enzyme participates in alanine and aspartate metabolism and aminoacyl-trna biosynthesis. (wikipedia.org)
  • Most (107 kb) of plasmid pHSAL1 (91-R6) is very closely related to part of plasmid pHS3 (R1) and codes for essential genes (e.g. arginine-tRNA ligase and the pyrimidine biosynthesis enzyme aspartate carbamoyltransferase). (archives-ouvertes.fr)
  • Both the conventional AAtRS and their closely related paralogs often provide aminoacylated tRNAs for peptide ligations by MprF/Fem/MurM-type acetyltransferase fold ligases in the synthesis of peptidoglycan, N-end rule modifications of proteins, lipid aminoacylation or biosynthesis of antibiotics, such as valinamycin. (biomedcentral.com)
  • This entry also includes folylpolyglutamate synthase that transfers glutamate to folylpolyglutamate and cyanophycin synthetase that catalyses the biosynthesis of the cyanobacterial reserve material multi-L-arginyl-poly-L-aspartate ( cyanophycin ). (wikipedia.org)
  • 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)
  • 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)
  • 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)
  • 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)
  • 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)
  • This enzyme belongs to the family of ligases, to be specific those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. (wikipedia.org)
  • The systematic name of this enzyme class is L-aspartate:tRNAAsp ligase (AMP-forming). (wikipedia.org)
  • Aspartate---tRNAAsn ligase (EC 6.1.1.23, nondiscriminating aspartyl-tRNA synthetase) is an enzyme with systematic name L-aspartate:tRNAAsx ligase (AMP-forming). (wikipedia.org)
  • This enzyme catalyses the following chemical reaction ATP + L-aspartate + tRNAAsx ⇌ {\displaystyle \rightleftharpoons } AMP + diphosphate + aspartyl-tRNAAsx The 3 substrates of this enzyme are ATP, L-asparagine, and tRNAAsx, whereas its 3 products are AMP, diphosphate, and asparaginyl-tRNAAsx. (wikipedia.org)
  • This enzyme is also called nondiscriminating asparaginyl-tRNA synthetase. (wikipedia.org)
  • It is a mitochondrial enzyme that specifically aminoacylates aspartyl-tRNA. (genecards.org)
  • The DARS2 gene provides instructions for making an enzyme called mitochondrial aspartyl-tRNA synthetase. (medlineplus.gov)
  • The most common mutation that causes this condition disrupts the way genetic information is pieced together to make a blueprint for producing the mitochondrial aspartyl-tRNA synthetase enzyme. (medlineplus.gov)
  • This type of mutation results in decreased mitochondrial aspartyl-tRNA synthetase enzyme activity. (medlineplus.gov)
  • With reduced activity, the enzyme has difficulty adding aspartic acid to the tRNA, which hinders the addition of this amino acid to mitochondrial proteins. (medlineplus.gov)
  • This accounts for the ability of this enzyme in, for example, Thermus thermophilus, to recognize both tRNA(Asp) (GUC anticodon) and tRNA(Asn) (GUU anticodon). (expasy.org)
  • Most of the mutations in the DARS1 gene change single amino acids in the aspartyl-tRNA synthetase enzyme. (medlineplus.gov)
  • These alterations occur in a region of the enzyme called the active site, where aspartate and the tRNA come together so the amino acid can be transferred. (medlineplus.gov)
  • The altered enzyme has difficulty adding the amino acid to the tRNA, which in turn hinders the addition of aspartate to proteins. (medlineplus.gov)
  • An aminoacyl-tRNA synthetase ( aaRS or ARS ), also called tRNA-ligase, is an enzyme that attaches the appropriate amino acid onto its tRNA . (wikipedia.org)
  • 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)
  • This enzyme bind amino-acid to tRNA. (studyread.com)
  • In a screen for calcium-regulated gene expression during growth and development of Dictyostelium discoideum we have identified an asparaginyl tRNA synthetase (ddAsnRS) gene, the second tRNA synthetase gene identified in this organism. (bvsalud.org)
  • However, despite encoding asparaginyl-tRNA synthetase and glutaminyl-tRNA synthetase, B. bacteriovorus also contains the amidotransferase GatCAB. (nih.gov)
  • L-aspartate is a glycogenic amino acid, and it can also promote energy production via its metabolism in the Krebs cycle. (drugbank.ca)
  • The accuracy of aminoacyl-tRNA synthetase is so high that it is often paired with the word "superspecificity" when it is compared to other enzymes that are involved in metabolism. (wikipedia.org)
  • Pathogenic mutations causing LBSL affect mitochondrial aspartyl-tRNA synthetase in diverse ways. (nih.gov)
  • The autosomal recessive white matter disorder LBSL (leukoencephalopathy with brain stem and spinal cord involvement and lactate elevation) is caused by mutations in DARS2, coding for mtAspRS (mitochondrial aspartyl-tRNA synthetase). (nih.gov)
  • We discussed the relationship between deficits in mitochondrial aspartyl-tRNA synthetase activity and the neuropathology observed. (nih.gov)
  • Enzymes called aminoacyl-tRNA synthetases, including mitochondrial aspartyl-tRNA synthetase, attach a particular amino acid to a specific tRNA. (medlineplus.gov)
  • Researchers do not understand why reduced activity of mitochondrial aspartyl-tRNA synthetase specifically affects certain parts of the brain and spinal cord. (medlineplus.gov)
  • Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp). (rcsb.org)
  • Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA. (uniprot.org)
  • Catalyzes the attachment of isoleucine to tRNA(Ile). (string-db.org)
  • Catalyzes the attachment of valine to tRNA(Val). (string-db.org)
  • Catalyzes the attachment of serine to tRNA(Ser). (string-db.org)
  • Here we demonstrate the lone B. bacteriovorus aspartyl-tRNA synthetase catalyzes aspartyl-tRNAAsn formation that GatCAB can then amidate to asparaginyl-tRNAAsn.This non-discriminating aspartyl-tRNA synthetase with GatCAB thus provides B. bacteriovorus a second route for Asn-tRNAAsn formation with the asparagine synthesized in a tRNA-dependent manner.Thus, in contrast to a previous prediction, B. bacteriovorus codes for a biosynthetic route for asparagine. (nih.gov)
  • Here we demonstrate the lone B. bacteriovorus aspartyl-tRNA synthetase catalyzes aspartyl-tRNAAsn formation that GatCAB can then amidate to asparaginyl-tRNAAsn. (nih.gov)
  • Hence, we predict that PafA is the Pup ligase, which catalyzes the ATP-dependent ligation of the terminal γ-carboxylate of glutamate to lysines, similar to the above enzymes. (biomedcentral.com)
  • Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp- tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. (string-db.org)
  • Deinococcus radiodurans, and Thermus thermophilus also encode both of these aminoacyl-tRNA synthetases with GatCAB. (nih.gov)
  • Eight core aminoacyl-tRNA synthetases (ARSs) (EPRS, MARS, QARS, RARS, IARS, LARS, KARS, and DARS) combine with three nonenzymatic components to form a complex known as the multisynthetase complex (MSC). (cdc.gov)
  • The least studied of these systems are those utilizing tRNAs or aminoacyl-tRNA synthetases (AAtRS) in non-ribosomal peptide ligation. (biomedcentral.com)
  • Non-discriminating and discriminating aspartyl-tRNA synthetases differ in the anticodon-binding domain. (naver.com)
  • In humans, the 20 different types of aa-tRNA are made by the 20 different aminoacyl-tRNA synthetases, one for each amino acid of the genetic code . (wikipedia.org)
  • Some synthetases also mediate an editing reaction to ensure high fidelity of tRNA charging. (wikipedia.org)
  • Another contribution to the accuracy of these synthetases is the ratio of concentrations of aminoacyl-tRNA synthetase and its cognate tRNA. (wikipedia.org)
  • Alignment of the core domains of aminoacyl-tRNA synthetases class I and class II. (wikipedia.org)
  • Both classes of aminoacyl-tRNA synthetases are multidomain proteins. (wikipedia.org)
  • Disease: Leukoencephalopathy with brainstem and spinal cord involvement and lactate elevation Similarity: Belongs to the class-II aminoacyl-tRNA synthetase family. (abcam.com)
  • Alanine-tRNA Ligase" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (harvard.edu)
  • This graph shows the total number of publications written about "Alanine-tRNA Ligase" by people in Harvard Catalyst Profiles by year, and whether "Alanine-tRNA Ligase" was a major or minor topic of these publication. (harvard.edu)
  • Below are the most recent publications written about "Alanine-tRNA Ligase" by people in Profiles. (harvard.edu)
  • [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)
  • This family includes UDP-N-acetylmuramate-L-alanine ligase (MurC), UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase (MurE), and UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase (MurF). (wikipedia.org)
  • We show that Yersinia pestis and pesticin-sensitive isolates of Y. pseudotuberculosis possess a common 34 kbp DNA region that has all the hallmarks of a pathogenicity island and is inserted into different asparaginyl tRNA genes at different chromosomal locations in each species. (nih.gov)
  • Aminoacyl tRNA therefore plays an important role in RNA translation , the expression of genes to create proteins. (wikipedia.org)
  • Recoding an organism in RED20 requires recoding all of its translated genes into RED20 as well as deleting its tRNA genes associated with RED20 null codons. (freegenes.org)
  • It aminoacylates at the 2'-OH of a terminal adenosine nucleotide on tRNA, and it is usually monomeric or dimeric (one or two subunits, respectively). (wikipedia.org)
  • It aminoacylates at the 3'-OH of a terminal adenosine on tRNA, and is usually dimeric or tetrameric (two or four subunits, respectively). (wikipedia.org)
  • Diseases associated with DARS2 include Leukoencephalopathy With Brain Stem And Spinal Cord Involvement And Lactate Elevation and 3-Methylglutaconic Aciduria, Type V . Among its related pathways are tRNA Aminoacylation and Gene Expression . (genecards.org)
  • This relaxation of specificity has been found to result from the absence of a loop in the tRNA that specifically recognizes the third position of the anticodon [1]. (wikipedia.org)
  • In a typical scenario, an aaRS consists of a catalytic domain (where both the above reactions take place) and an anticodon binding domain (which interacts mostly with the anticodon region of the tRNA and ensures binding of the correct tRNA to the amino acid). (wikipedia.org)
  • Among its related pathways are Viral mRNA Translation and tRNA Aminoacylation . (genecards.org)
  • Alternatively they might supply aminoacylated tRNAs for other biosynthetic pathways like that for tetrapyrrole or directly function as peptide ligases as in the case of mycothiol and those identified here. (biomedcentral.com)
  • Although phenylalanine-tRNA synthetase is class II, it aminoacylates at the 2'-OH. (wikipedia.org)
  • The crystalline aminoacyl-tRNA synthetase. (cbrc.jp)
  • aminoacyl-tRNA synthetase complex. (cbrc.jp)
  • Park SG, Choi EC, Kim S. Aminoacyl-tRNA synthetase-interacting multifunctional proteins (AIMPs): a triad for cellular homeostasis. (medlineplus.gov)
  • 1999) Two Distinct Cytokines Released from a Human Aminoacyl-tRNA Synthetase. (sinobiological.com)
  • It does so by catalyzing the esterification of a specific cognate amino acid or its precursor to one of all its compatible cognate tRNAs to form an aminoacyl-tRNA . (wikipedia.org)
  • the tRNA is found to be improperly charged), the aminoacyl-tRNA bond is hydrolyzed . (wikipedia.org)
  • Regardless of where the aminoacyl is initially attached to the nucleotide, the 2'- O -aminoacyl-tRNA will ultimately migrate to the 3' position via transesterification . (wikipedia.org)
  • A general structure of an aminoacyl-tRNA synthetase is shown here with an editing site as well as an activation site. (wikipedia.org)
  • 1. SGOT is also called as aspartate aminotransferase (AST). (studyread.com)
  • The adenylate-aaRS complex then binds the appropriate tRNA molecule's D arm , and the amino acid is transferred from the aa-AMP to either the 2'- or the 3'-OH of the last tRNA nucleotide (A76) at the 3'-end. (wikipedia.org)
  • NG1489 is paralogously related to NG1454 (lysyl-tRNA synthetase (LysRS)) (1e-11). (northwestern.edu)
  • This metabolite is likely to be heavily modified through multiple reactions catalyzed by a metal-binding cupin domain and a lysine N6 monooxygenase that are strictly associated with this paralogous methionyl-tRNA synthetase (MtRS). (biomedcentral.com)
  • It is hypothesized that L-aspartate, especially the potassium magnesium aspartate salt, spares stores of muscle glycogen and/or promotes a faster rate of glycogen resynthesis during exercise. (drugbank.ca)
  • ATP + L-aspartate + tRNA Asp = AMP + diphosphate + L-aspartyl-tRNA Asp . (rcsb.org)
  • ATP + L-aspartate + tRNA Asx = AMP + diphosphate + L-aspartyl-tRNA Asx . (rcsb.org)
  • Other names in common use include aspartyl-tRNA synthetase, aspartyl ribonucleic synthetase, aspartyl-transfer RNA synthetase, aspartic acid translase, aspartyl-transfer ribonucleic acid synthetase, and aspartyl ribonucleate synthetase. (wikipedia.org)
  • This gene encodes a member of a multienzyme complex that functions in mediating the attachment of amino acids to their cognate tRNAs. (genecards.org)
  • 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)
  • Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). (rcsb.org)
  • Synthesis of aspartyl-tRNA(Asp) in Escherichia coli--a snapshot of the second step. (nagahama-i-bio.ac.jp)
  • Analysis of bacterial genomes suggests a significant number of other bacteria may also code for both routes for Asn-tRNAAsn synthesis with only a limited number encoding a second aspartyl-tRNA synthetase. (nih.gov)
  • Yeast tRNA(Asp)-aspartyl-tRNA synthetase complex: low resolution crystal structure. (cbrc.jp)
  • Crystallographic studies on the aspartyl-tRNA synthetase-tRNAAsp system from yeast. (cbrc.jp)
  • Formation of a catalytically active complex between tRNAAsp and aspartyl-tRNA synthetase from yeast in high concentrations of ammonium sulphate. (cbrc.jp)
  • One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. (string-db.org)