Aspartate trna ligase. Medical search

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)

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 ...

https://en.wikipedia.org/wiki/DARS_(gene)

... that are uniquely present in this genus in the proteins aspartate-tRNA ligase, A/G-specific adenine glycosylase, thymidylate ...

https://en.wikipedia.org/wiki/Sporosarcina

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 ...

https://en.wikipedia.org/wiki/Aspartate—tRNA_ligase

... 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 ...

https://en.wikipedia.org/wiki/Alanine—tRNA_ligase

This enzyme participates in alanine and aspartate metabolism and aminoacyl-trna biosynthesis. As of late 2007, 3 structures ... In enzymology, an asparagine-tRNA ligase (EC 6.1.1.22) is an enzyme that catalyzes the chemical reaction ATP + L-asparagine + ... and L-asparaginyl-tRNA(Asn). This enzyme belongs to the family of ligases, to be specific those forming carbon-oxygen bonds in ... aminoacyl-tRNA and related compounds. The systematic name of this enzyme class is L-asparagine:tRNAAsn ligase (AMP-forming). ...

https://en.wikipedia.org/wiki/Asparagine—tRNA_ligase

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 ...

https://en.wikipedia.org/wiki/Aspartate—tRNA(Asn)_ligase

This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds carbon-nitrogen ligases with ... This enzyme participates in glutamate metabolism and alanine and aspartate metabolism. Min B, Pelaschier JT, Graham DE, Tumbula ... aspartyl-tRNA(Asn), and L-glutamine, whereas its 4 products are ADP, phosphate, asparaginyl-tRNA(Asn), and L-glutamate. ... In enzymology, an asparaginyl-tRNA synthase (glutamine-hydrolysing) (EC 6.3.5.6) is an enzyme that catalyzes the chemical ...

https://en.wikipedia.org/wiki/Asparaginyl-tRNA_synthase_(glutamine-hydrolysing)

This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds carbon-nitrogen ligases with ... This enzyme participates in glutamate metabolism and alanine and aspartate metabolism. Horiuchi KY, Harpel MR, Shen L, Luo Y, ... glutamyl-tRNA(Gln), and L-glutamine, whereas its 4 products are ADP, phosphate, glutaminyl-tRNA(Gln), and L-glutamate. ... Ibba M, Soll D (2000). "Aminoacyl-tRNA synthesis". Annu. Rev. Biochem. 69: 617-50. doi:10.1146/annurev.biochem.69.1.617. PMID ...

https://en.wikipedia.org/wiki/Glutaminyl-tRNA_synthase_(glutamine-hydrolysing)

... alanine-tRNA ligase MeSH D08.811.464.263.200.100 - arginine-tRNA ligase MeSH D08.811.464.263.200.150 - aspartate-tRNA ligase ... glutamate-trna ligase MeSH D08.811.464.263.200.350 - glycine-trna ligase MeSH D08.811.464.263.200.400 - histidine-trna ligase ... isoleucine-trna ligase MeSH D08.811.464.263.200.500 - leucine-trna ligase MeSH D08.811.464.263.200.550 - lysine-trna ligase ... serine-trna ligase MeSH D08.811.464.263.200.800 - threonine-tRNA ligase MeSH D08.811.464.263.200.850 - tryptophan-tRNA ligase ...

https://en.wikipedia.org/wiki/List_of_MeSH_codes_(D08)

... 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 ...

https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_6)

... glutamate-tRNA ligase, EC 1.2.1.70, glutamyl-tRNA reductase and EC 5.4.3.8 EC 2.7.2.14: branched-chain-fatty-acid kinase EC 2.7 ... tRNA-5-methyluridine54 2-sulfurtransferase (*) EC 2.8.1.16: L-aspartate semialdehyde sulfurtransferase (*) (*) No Wikipedia ... tRNA (guanine46-N7)-methyltransferase EC 2.1.1.34: tRNA (guanosine18-2′-O)-methyltransferase EC 2.1.1.35: tRNA (uracil54-C5)- ... tRNA (guanine110-N2)-dimethyltransferase EC 2.1.1.214: tRNA (guanine10-N2)-methyltransferase EC 2.1.1.215: tRNA (guanine26-N2/ ...

https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)

... 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 ...

https://en.wikipedia.org/wiki/Chromosome_6

DNA polymerase and DNA ligase then completes the process by incorporating the correct base pair and closing the nick. The UDG ... Hydrogen bonding between water and aspartate prepares the water molecule for nucleophilic attack of the N-glycosidic bond, ... is a naturally-occurring base in human tRNA or in wobble base pairing, it is mistakenly incorporated into DNA either through ...

https://en.wikipedia.org/wiki/DNA-deoxyinosine_glycosylase

... aspartate 4-decarboxylase EC 4.1.1.11: aspartate 1-decarboxylase EC 4.1.1.12: aspartate 4-decarboxylase EC 4.1.1.13: deleted EC ... tRNA-intron lyase EC 4.6.1.17: cyclic pyranopterin monophosphate synthase * EC 4.6.1.18: pancreatic ribonuclease * EC 4.6.1.19 ... heme ligase EC 4.99.1.9:: coproporphyrin ferrochelatase * EC 4.99.1.10: magnesium dechelatase * EC 4.99.1.11: sirohydrochlorin ... 3-hydroxy-D-aspartate aldolase EC 4.1.3.42: (4S)-4-hydroxy-2-oxoglutarate aldolase * EC 4.1.3.43: 4-hydroxy-2-oxohexanoate ...

https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_4)

ARNt ligase EC 6.1.1.22 asparagine ARNt ligase EC 6.1.1.23 aspartate ARNt Asn ligase EC 6.1.1.24 glutamate ARNtGln ligase EC ... EC 6.3.4.17 formate-dihydrofolate ligase EC 6.3.4.18 5-(carboxyamino)imidazole ribonucleotide synthase EC 6.3.4.19 tRNAIle- ... 6.1.1.9 valine ARNt ligase EC 6.1.1.10 methionine ARNt ligase EC 6.1.1.11 serine ARNt ligase EC 6.1.1.12 aspartate ARNt ligase ... 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 acide-CoA ligase ( ...

https://fr.m.wikipedia.org/wiki/Ligase

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, all of which are bound by the polyhistidine-tag with micromolar ...

https://en.wikipedia.org/wiki/Polyhistidine-tag

... 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 ...

https://en.wikipedia.org/wiki/Biosynthesis

This entry comprises bacterial enzymes that import Histidine, Arginine, Lysine, Glutamine, Glutamate, Aspartate, ornithine, ... and ligases (EC 6). However, it became apparent that none of these could describe the important group of enzymes that catalyse ... tRNA) and messenger RNA (mRNA) through the ribosome. The enzyme classification and nomenclature list was first approved by the ...

https://en.wikipedia.org/wiki/Translocase

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 fed ... kynurenine hydroxylase and fatty acid Co-A ligase. Disruption of the outer membrane permits proteins in the intermembrane space ... It encodes 37 genes: 13 for subunits of respiratory complexes I, III, IV and V, 22 for mitochondrial tRNA (for the 20 standard ...

https://en.wikipedia.org/wiki/Mitochondrion

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- ...

https://en.wikipedia.org/wiki/List_of_enzymes

... tRNA(adenine34) deaminase * EC 3.5.4.34: tRNAAla(adenine37) deaminase * EC 3.5.4.35: tRNA(cytosine8) deaminase * EC 3.5.4.36: ... 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. ... glutamateammonia ligase] phosphorylase EC 3.1.4.16: 2′,3′-cyclic-nucleotide 2′-phosphodiesterase EC 3.1.4.17: 3′,5′-cyclic- ... tRNA(adenine34) deaminase * EC 3.5.4.34: tRNAAla(adenine37) deaminase * EC 3.5.4.35: tRNA(cytosine8) deaminase * EC 3.5.4.36: ...

https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_3)

1 Amino Acyl-tRNA Synthetases --che.... *1 Aspartate-tRNA Ligase. *1 Bombyx --genetics ... Calcium regulates the expression of a Dictyostelium discoideum asparaginyl tRNA synthetase gene.. Jaiswal, Jyoti K; Nanjundiah ...

https://imsear.searo.who.int/handle/123456789/110572/simple-search?query=&sort_by=score&order=desc&rpp=10&filter_field_1=subject&filter_type_1=equals&filter_value_1=Molecular Sequence Data&filter_field_2=subject&filter_type_2=equals&filter_value_2=Base Sequence&etal=0&filtername=dateIssued&filterquery=2003&filtertype=equals

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 ...

https://medlineplus.gov/genetics/gene/dars2/

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 } ...

https://phinvads.cdc.gov/vads/ViewCodeSystemConcept.action?oid=2.16.840.1.113883.6.96&code=58787004

The DARS1 gene provides instructions for making an enzyme called aspartyl-tRNA synthetase. Learn about this gene and related ... Asp tRNA Ligase. *Aspartate tRNA Ligase. *aspartate tRNA ligase 1, cytoplasmic. *Aspartyl tRNA Synthetase ... Aspartyl-tRNA synthetase attaches the amino acid aspartate to the correct tRNA, which helps ensure that aspartate is added at ... These alterations occur in a region of the enzyme called the active site, where aspartate and the tRNA come together so the ...

https://medlineplus.gov/genetics/gene/dars1/

Mouse AIMP1(Aminoacyl tRNA Synthetase Complex Interacting Multifunctional Protein 1) ELISA Kit ... Human Anti-GRIN2A(Anti-Glutamate Receptor, Ionotropic, N-Methyl-D-Aspartate 2A Antibody) ELISA Kit ... Rat SMURF2(Smad Specific E3 Ubiquitin Protein Ligase 2) ELISA Kit. *Rat SOD(Superoxide Dismutases) ELISA Kit ... Mouse GRIN2B(Glutamate Receptor, Ionotropic, N-Methyl-D-Aspartate 2B) ELISA Kit ...

https://www.gkts.net/rat-cyp3a4cytochrome-p450-3a4-elisa-kit/

alanine-tRNA ligase activity. 1.49% (1/67). 8.14. 0.00355. 0.00776. GO:0006419. alanyl-tRNA aminoacylation. 1.49% (1/67). 8.14 ... aspartate 1-decarboxylase activity. 2.99% (2/67). 9.14. 3e-06. 1.2e-05. ... aminoacyl-tRNA ligase activity. 13.43% (9/67). 6.61. 0.0. 0.0. GO:0016875. ligase activity, forming carbon-oxygen bonds. 13.43 ... phenylalanine-tRNA ligase activity. 1.49% (1/67). 7.55. 0.00532. 0.010754. GO:0016307. phosphatidylinositol phosphate kinase ...

https://protists.sbs.ntu.edu.sg/cluster/view/4918

Článek Loss of a Conserved tRNA Anticodon Modification Perturbs Plant Immunity Článek Genome-Wide Association Analysis of ... a Walker B aspartate mutation, D244A, and a Walker A/Walker B double mutation K167A/D244A (S1 Fig), and tested their ability to ... Since transpeptidases and/or ligases can incorporate D-alanine into the stem peptide that is conjugated to the glycan strand of ... Loss of a Conserved tRNA Anticodon Modification Perturbs Plant Immunity * Genome-Wide Association Analysis of Adaptation Using ...

https://www.prolekare.cz/casopisy/plos-genetics/2015-10/regulation-of-spore-formation-by-the-spoiiq-and-spoiiia-proteins-56274

tRNA carrying dipeptide is now in P site, A site is empty. 4. New appropriately amino acid charged tRNA enters A site 5. ... GAC=aspartate CCU=proline UUG=leucine Genetic code: Redundant (more than one codon for each amino acid) yet specific (each ... 6. Ligase: skakel kort rye DNA (genaamd Okazaki -fragmente) saam op en ldquolagging strand & rdquo huiswerk sien remming van ... B. Translation requires tRNA, amino acids, ATP/GTP, ribosomes and mRNA. C. tRNA =transfer RNA. Adaptor/translator molecule. ...

https://af.dualjuridik.org/6194-the-proofreading-function-of-coronavirus-polymerases.html

https://en.wikipedia.org/wiki/Aspartate%E2%80%94tRNA_ligase

ATP + L-aspartate + tRNA(Asp) <=> AMP + diphosphate + L-aspartyl-tRNA(Asp ...

https://enzyme.expasy.org/EC/6.1.1.12

IPR002312 Aspartyl/Asparaginyl-tRNA synthetase, class IIb. IPR045864 Class II Aminoacyl-tRNA synthetase/Biotinyl protein ligase ... IPR004523 Aspartate-tRNA synthetase, type 2. ... IPR004364 Aminoacyl-tRNA synthetase, class II (D/K/N). ... J:242754 Frohlich D, et al., In vivocharacterization of the aspartyl-tRNA synthetase DARS: Homing in on the leukodystrophy HBSL ...

http://www.informatics.jax.org/marker/MGI:2442544

https://medlineplus.gov/genetics/gene/dars2/

Asp-tRNA Ligase Aspartyl T RNA Synthetase Aspartyl-tRNA Synthetase Registry Number. EC 6.1.1.12. CAS Type 1 Name. L-Aspartate: ... Carbon-Oxygen Ligases [D08.811.464.263] * Amino Acyl-tRNA Synthetases [D08.811.464.263.200] * Alanine-tRNA Ligase [D08.811. ... Aspartate-tRNA Ligase Preferred Term Term UI T003677. Date01/01/1999. LexicalTag ACX. ThesaurusID NLM (1975). ... Aspartate-tRNA Ligase Preferred Concept UI. M0001848. Registry Number. EC 6.1.1.12. Scope Note. An enzyme that activates ...

https://meshb.nlm.nih.gov/record/ui?ui=D001226

Aspartate--tRNA ligase. 189. SEQF1671,JH376827.1. SEQF1671_00195 jb [NA] [AA] 1011/336. 235448-236458. Lipoate-protein ligase ... Isoleucine--tRNA ligase. 58. SEQF1671,JH376827.1. SEQF1671_00061 jb [NA] [AA] 390/129. 71907-72296. General stress protein 16O ... Threonine--tRNA ligase 1. 9. SEQF1671,JH376827.1. SEQF1671_00009 jb [NA] [AA] 639/212. 19407-20045. Translation initiation ... Asparagine--tRNA ligase. 184. SEQF1671,JH376827.1. SEQF1671_00190 jb [NA] [AA] 1356/451. 230839-229484. Ribosomal large subunit ...

https://www.homd.org/genome/explorer?gid=SEQF1671&anno=prokka

Aspartate--tRNA ligase. 2483. SEQF1653,KE150261.1. SEQF1653_02537 jb [NA] [AA] 798/265. 7804-8601. 4%2C5-DOPA dioxygenase ... Long-chain-fatty-acid--CoA ligase FadD15. 2495. SEQF1653,KE150261.1. SEQF1653_02549 jb [NA] [AA] 1620/539. 19416-17797. ...

https://homd.org/genome/explorer?gid=SEQF1653&anno=prokka&page=0

https://phinvads.cdc.gov/vads/ViewCodeSystemConcept.action?oid=2.16.840.1.113883.6.96&code=58787004

https://imsear.searo.who.int/handle/123456789/110572/simple-search?query=&sort_by=score&order=desc&rpp=10&filter_field_1=subject&filter_type_1=equals&filter_value_1=Molecular+Sequence+Data&filter_field_2=subject&filter_type_2=equals&filter_value_2=Base+Sequence&etal=0&filtername=dateIssued&filterquery=2003&filtertype=equals

Arginine-tRNA ligase. aspS. J. COG0173. TIGR00459. Aspartate-tRNA ligase. cgtA. DL. COG0536. TIGR02729/PF01018. GTPase ObgE/ ... Alanine-tRNA ligase. argS. J. COG0018. TIGR00456. ... Serine-tRNA ligase. smpB. O. COG0691. TIGR00086. SsrA-binding ... Histidine-tRNA ligase. ileS. J. COG0060. TIGR00392. Isoleucine-tRNA ligase 1. infB. J. COG0532. TIGR00487. Translation ... Phenylalanine-tRNA ligase alpha subunit. pheT. J. COG0073. TIGR00472. Phenylalanine-tRNA ligase beta subunit. ...

https://help.ezbiocloud.net/ubcg-gene-set/

aspartate--tRNA ligase. Location. Chromosome 1: 128,960-130,840 reverse strand.. ASM276v2:AL844501.2 ...

http://protists.ensembl.org/Plasmodium_falciparum/Gene/Summary?g=PF3D7_0102900

pyrrolysyl-tRNA synthetase activity. GO:0043816. phosphoserine-tRNA(Cys) ligase activity. GO:0050560. aspartate-tRNA(Asn) ... aminoacyl-tRNA ligase activity. id: GO:0004812. name: aminoacyl-tRNA ligase activity. namespace: molecular_function. type: go. ... Description: Catalysis of the formation of aminoacyl-tRNA from ATP, amino acid, and tRNA with the release of diphosphate and ... lysine-tRNA(Pyl) ligase activity. Parent Functions. id. name. GO:0016876. ligase activity, forming aminoacyl-tRNA and related ...

http://networks.systemsbiology.net/function/GO:0004812/

Serine-tRNA Ligase 12% * Aspartate-tRNA Ligase 12% * Nucleotides 11% * pyrimidine 8% ...

https://pure.skoltech.ru/en/publications/mcce-provides-resistance-to-protein-synthesis-inhibitor-microcin--3/fingerprints/

Aspartate-semialdehyde dehydrogenase (4) * 6-phosphogluconate dehydrogenase, decarboxylating 1 (4) * Tyrosine--tRNA ligase, ... Glutamate--tRNA ligase, mitochondrial (4) * High-affinity glucose transporter HXT2 (4) * Tyrosine--tRNA ligase, mitochondrial ( ... Phenylalanine--tRNA ligase beta subunit (4) * Phenylalanine--tRNA ligase alpha subunit (4) ...

https://www.ebi.ac.uk/biomodels/search?query=CHEBI:CHEBI:16566

https://www.ebi.ac.uk/biomodels/search?query=CHEBI:CHEBI:18319

Résumé , Liens , BibTeX , Étiquettes: Amino Acid, Amino Acid Sequence Amino Acids/chemistry Animals Aspartate-tRNA Ligase/* ... keywords = {Amino Acid, Amino Acid Sequence Amino Acids/chemistry Animals Aspartate-tRNA Ligase/*metabolism Aspartic Acid/ ... Comparison of the tRNA aminoacylation activity of wild-type and mutant parasite AspRSs with those of yeast and human AspRSs ... Comparison of the tRNA aminoacylation activity of wild-type and mutant parasite AspRSs with those of yeast and human AspRSs ...

https://ibmc.cnrs.fr/laboratoire/arn/publications/?tgid=4226

"Aspartyl-tRNA synthetase, mitochondrial, protein biosynthesis, aspartate--tRNA ligase, mitochondrion" YFL019C -5.080596 ... "alpha subunit of yeast mitochondrial phenylalanyl-tRNA synthetase, protein biosynthesis, phenylalanine--tRNA ligase, ... "aspartate aminotransferase, mitochondrial, aspartate catabolism, aspartate aminotransferase, mitochondrion" YJR128W 9.031074 ... tRNA isopentenyltransferase, " YMR022W -0.280013 INESSENTIAL QRI8 "ubiquitin conjugating enzyme,ubiquitin--protein ligase," ...

https://genomics.lbl.gov/YeastFitnessData/websitefiles/ratioresults/thrRatio_07.txt

tRNA ligase,. cytoplasmic. Adenylosuccinate. synthetase. isozyme 1. L-amino-acid. oxidase. Aspartate--tRNA. ligase,. ... tRNA(Asn). L-. Asparaginyl-. tRNA(Asn). tRNA(Asp). L- Aspartyl-. tRNA(Asp). Pyrimidine. Metabolism. Histidine. Metabolism. Urea ... D-aspartate. oxidase. Isoaspartyl. peptidase/L-. asparaginase. Argininosuccinate. lyase. Aspartoacylase. Asparagine--. ...

https://smpdb.ca/view/SMP0000067?highlight%5Bcompounds%5D%5B%5D=DB03107&highlight%5Bproteins%5D%5B%5D=DB03107

6.1.1.12 aspartate---tRNA ligase 6.1.1.22 asparagine---tRNA ligase - - BK ... 6.3.5.6 asparaginyl-tRNA synthase (glutamine-hydrolysing) 6.3.5.7 glutaminyl-tRNA synthase (glutamine-hydrolysing) - - K ...

https://metano.tu-bs.de/search/L-asparaginyl-tRNAAsn%20=

EC 6.1.1.26 pyrrolysine tRNAPyl ligase (10 August 2007). EC 6.3.2.29 cyanophycin synthase (L-aspartate-adding) (10 August 2007) ... Accepted name: pyrrolysine tRNAPyl ligase. Reaction: ATP + L-pyrrolysine + tRNAPyl = AMP + diphosphate + L-pyrrolysyl-tRNAPyl. ... Accepted name: tRNA-guanine transglycosylase. Reaction: (1) [tRNA]-guanine + queuine = [tRNA]-queuine + guanine. (2) [tRNA]- ... Other name(s): PylS; pyrrolysyl-tRNA synthetase. Systematic name: L-pyrrolysine:tRNAPyl ligase (AMP-forming). Comments: In ...

https://iubmb.qmul.ac.uk/enzyme/supplements/sup2007/newenz2.html

ASPARTATE--TRNA-LIGASE-RXN. *ASPARTATEKIN-RXN. *ASPCARBTRANS-RXN. *L-ASPARTATE-OXID-RXN ... Retrieved from "https://gem-aureme.genouest.org/sjapgem/index.php?title=L-ASPARTATE&oldid=137327" ...

https://gem-aureme.genouest.org/sjapgem/index.php/L-ASPARTATE

Aspartate--tRNA ligase. 602. aspS. Treponema pallidum subsp. pallidum (strain SS14). B2S4P6. Glycerol-3-phosphate dehydrogenase ... Histidine--tRNA ligase. 442. hisS. Treponema pallidum subsp. pallidum (strain SS14). B2S3N6. Serine--tRNA ligase. 426. serS. ... Glycine--tRNA ligase. 462. glyQS. Treponema pallidum subsp. pallidum (strain SS14). B2S3R2. Glutamate--tRNA ligase. 537. gltX. ... Arginine--tRNA ligase. 589. argS. Treponema pallidum subsp. pallidum (strain SS14). B2S475. Threonine--tRNA ligase. 592. thrS. ...

http://repeat.biol.ucy.ac.cy/fgb2/gbrowse/swissprot/?q=Treponema%20pallidum%20subsp.%20pallidum%20%28strain%20SS14%29

The aminoacyl-tRNA synthetases (also known as aminoacyl-tRNA ligases) catalyse the attachment of an amino acid to its cognate ... a putative citrulline-aspartate ligase domain or a nitrilase/amidase domain. The HUP domain class (after HIGH-signature ... Thus, the two TilS enzymes discriminate tRNA(Ile)(2)from tRNA(Met) by strategies similar to that used by IleRS, but indistinct ... In reactions catalysed by the class I aminoacyl-tRNA synthetases, the aminoacyl group is coupled to the 2-hydroxyl of the tRNA ...

http://smart.embl.de/smart/do_annotation.pl?DOMAIN=TilS_C&BLAST=DUMMY

Arginine-tRNA Ligase. *Aspartate-tRNA Ligase. *Glutamate-tRNA Ligase. *Glycine-tRNA Ligase ... "Glycine-tRNA Ligase" by people in this website by year, and whether "Glycine-tRNA Ligase" was a major or minor topic of these ... "Glycine-tRNA Ligase" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH (Medical ... Below are the most recent publications written about "Glycine-tRNA Ligase" by people in Profiles. ...

https://profiles.ouhsc.edu/display/9061

Aspartate--ammonia ligase (EC 6.3.1.1)::Flavoprotein MioC::16S rRNA (guanine(527)-N(7))-methyltransferase (EC 2.1.1.170)::tRNA- ... CoA ligase [ADP-forming] beta chain (EC 6.2.1.5)::Succinyl-CoA ligase [ADP-forming] alpha chain (EC 6.2.1.5)::5- ... alanine ligase (EC 6.3.2.10)::UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase (EC 6.3.2.13)::Cell division ... Aspartate aminotransferase (EC 2.6.1.1)::Outer membrane porin OmpF::Asparaginyl-tRNA synthetase (EC 6.1.1.22)::Nicotinate ...

https://www.bv-brc.org/docs/cli_tutorial/cli_clustering.html

Aspartate. aminotransferase,. cytoplasmic. Nitric oxide. synthase, brain. Bifunctional. glutamate/proline-. -tRNA ligase. ... tRNA(Arg). L-Arginyl-. tRNA(Arg). tRNA(Pro). L-Prolyl-. tRNA(Pro). Citric Acid. Cycle. Alanine. Metabolism. D-Arginine and. D- ... arginine--tRNA. ligase,. mitochondrial. Glycine. amidinotransferase,. mitochondrial. Guanidinoacetate. N-. methyltransferase. ...

https://smpdb.ca/view/SMP0000507?highlight%5Bcompounds%5D%5B%5D=DB00148&highlight%5Bproteins%5D%5B%5D=DB00148

Aspartate. aminotransferase,. cytoplasmic. Glutamate--. cysteine ligase. Cysteine--tRNA. ligase,. cytoplasmic. L-Glutamic acid ... tRNA(Cys). L-. Cysteinyl-. tRNA(Cys). Glutamate. Metabolism. Glutamate. Metabolism. Taurine and. Hypotaurine. Metabolism. ... tRNA(Cys). L-. Cysteinyl-. tRNA(Cys). Glutamate. Metabolism. Glutamate. Metabolism. Taurine and. Hypotaurine. Metabolism. ... Aspartate. aminotransferase,. cytoplasmic. 3-. mercaptopyruvate. sulfurtransferase. L-lactate. dehydrogenase. A-like 6A. ...

https://pathman.smpdb.ca/view/SMP0000722

Aspartate--ammonia ligase. 19. SEQF2033,AEJQ02000001.1. SEQF2033_00019 jb [NA] [AA] 984/327. 15166-14183. tRNA-dihydrouridine( ... Glycine--tRNA ligase alpha subunit. 80. SEQF2033,AEJQ02000003.1. SEQF2033_00080 jb [NA] [AA] 261/86. 37342-37602. hypothetical ... Glycine--tRNA ligase beta subunit. 85. SEQF2033,AEJQ02000003.1. SEQF2033_00085 jb [NA] [AA] 1023/340. 42252-41230. Delta- ... Methionyl-tRNA formyltransferase. 3. SEQF2033,AEJQ02000001.1. SEQF2033_00003 jb [NA] [AA] 1356/451. 1666-3021. Ribosomal RNA ...

https://homd.org/genome/explorer?gid=SEQF2033&anno=prokka

aspartate-ammonia ligase activity. IEP. Enrichment. MF. GO:0004812. aminoacyl-tRNA ligase activity. IEP. Enrichment. ... tRNA aminoacylation for protein translation. IEP. Enrichment. BP. GO:0006432. phenylalanyl-tRNA aminoacylation. IEP. Enrichment ...

https://bacteria.sbs.ntu.edu.sg/sequence/view/2087

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)
Studies on aspartyl-tRNA synthetase from Baker's yeast. (wikipedia.org)
aspartyl-tRNA synthetase. (expasy.org)
The DARS2 gene provides instructions for making an enzyme called mitochondrial aspartyl-tRNA synthetase. (medlineplus.gov)
Enzymes called aminoacyl-tRNA synthetases, including mitochondrial aspartyl-tRNA synthetase, attach a particular amino acid to a specific tRNA. (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 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)
Researchers do not understand why reduced activity of mitochondrial aspartyl-tRNA synthetase specifically affects certain parts of the brain and spinal cord. (medlineplus.gov)
This domain is found in the tRNA(Ile) lysidine synthetase (TilS) protein. (embl.de)
This entry represents the C-terminal domain of lysidine-tRNA(Ile) synthetase, which ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. (embl.de)
some, including characterised proteins of Escherichia coli and Bacillus subtilis known to be tRNA(Ile)-lysidine synthetase, include a conserved 50-residue domain that many other members lack. (embl.de)
Nichols RC, Pai SI, Ge Q, Targoff IN, Plotz PH, Liu P. 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. (ouhsc.edu)
Primary structure and functional expression of human Glycyl-tRNA synthetase, an autoantigen in myositis. (ouhsc.edu)
Childhood onset epilepsy is also reported in various aminoacyl-tRNA synthetase disorders. (cnrs.fr)
We describe a case with a milder neurological phenotype than previously reported with QARS1 variants and review the seizure associations with aminoacyl-tRNA synthetase disorders. (cnrs.fr)
We also summarise literature regarding epilepsy in aminoacyl-tRNA synthetase disorders, which is also often early onset, severe and drug-refractory. (cnrs.fr)
INTRODUCTION: Mutations in QARS1, which encodes human glutaminyl-tRNA synthetase, have been associated with epilepsy, developmental regression, progressive microcephaly and cerebral atrophy. (cnrs.fr)
These enzymes are involved in joining together 2 substrates e.g., alanyl-t-RNA synthetase, glutamine synthetase, DNA ligases. (amano-enzyme.com)

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)
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)
This enzyme participates in alanine and aspartate metabolism and aminoacyl-trna biosynthesis. (wikipedia.org)
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)
En biochimie , une ligase est une enzyme qui catalyse la jonction de deux molécules (en anglais ligation ) par de nouvelles liaisons covalentes avec hydrolyse concomitante de l' ATP ou d'autres molécules similaires. (wikipedia.org)
In fact, the origins of the word "Enzyme" derive from Greek: "en" (in) and "zyme" (ferment). (amano-enzyme.com)
Enzyme classification.EC_6 ligases.EC_6.3 ligase forming. (ntu.edu.sg)

Each tRNA carries a specific amino acid to the growing chain. (medlineplus.gov)
Catalysis of the formation of aminoacyl-tRNA from ATP, amino acid, and tRNA with the release of diphosphate and AMP. (systemsbiology.net)
Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine. (embl.de)
This helps bind amino-acid to tRNA. (studyread.com)

Glycine-tRNA Ligase" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (ouhsc.edu)
This graph shows the total number of publications written about "Glycine-tRNA Ligase" by people in this website by year, and whether "Glycine-tRNA Ligase" was a major or minor topic of these publications. (ouhsc.edu)
Below are the most recent publications written about "Glycine-tRNA Ligase" by people in Profiles. (ouhsc.edu)

Le nom courant des enzymes de type ligase inclut souvent le terme « ligase » comme l' ADN ligase du phage T4 utilisée pour structurer des fragments d' ADN . (wikipedia.org)
Attention cependant à ne pas confondre les enzymes synthétases avec les enzymes synthases (qui sont toutes deux des enzymes du groupe des ligases). (wikipedia.org)
Les ligases sont classées EC 6 dans la nomenclature EC des enzymes. (wikipedia.org)
These enzymes catalyze the transfer of a particular group from one substrate to another e.g., aspartate amino transferase (AST), alanine aminotransferase (ALT), hexokinase, phosphoglucomutase, hexose- 1-phosphate uridyltransferase, ornithine carbamoyl transferase etc. (amano-enzyme.com)

2030) plays inhibiting become by primary cancers perfused on post-translational Aspects' structure, performing the draft of corneal tRNA, ubiquitin residue, assembly kinases and catalytic subunit system. (evakoch.com)

In other proteins, the pyrophosphatase domain is associated with amidotransferase domains (type I or type II), a putative citrulline-aspartate ligase domain or a nitrilase/amidase domain. (embl.de)

En fait la synthase forme et défait les doubles liaisons d'une protéine. (wikipedia.org)

The 20 aminoacyl-tRNA synthetases are divided into two classes, I and II. (embl.de)
In reactions catalysed by the class I aminoacyl-tRNA synthetases, the aminoacyl group is coupled to the 2'-hydroxyl of the tRNA, while, in class II reactions, the 3'-hydroxyl site is preferred. (embl.de)
The HUP domain class (after HIGH-signature proteins, UspA, and PP-ATPase) groups together PP-loop ATPases, the nucleotide-binding domains of class I aminoacyl-tRNA synthetases, UspA protein (USPA domains), photolyases, and electron transport flavoproteins (ETFP). (embl.de)

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)
CONCLUSION: We describe two QARS1 variants associated with overall conserved tRNA aminoacylation activity but characterized by significantly reduced QARS protein solubility, resulting in a milder clinical phenotype. (cnrs.fr)

deltex E3 ubiquitin ligase 3L [Source:H. (gsea-msigdb.org)

EC 6.3.5 Carbone-Azote Ligases avec Glutamine comme Amido-N-Donneur. (wikipedia.org)

However, tRNA binding involves an alpha-helical structure that is conserved between class I and class II synthetases. (embl.de)

OBJECTIVE: Quinolinic acid (QA), a kynurenine (KYN)/tryptophan (TRP) pathway metabolite, is an N-methyl-D-aspartate receptor agonist that can produce excitotoxic neuron damage. (bvsalud.org)

The acidic midwifery of trimer increase is exposed by O-phosphoseryl-tRNA: process particle( SEPSECS) that is galactose) to selenocysteinyl-tRNA(Sec). inactivated eco-friendly JavaScript to member might convert process endophilins through the low spectrum and pathway of PAK, LIMK1 and cofilin. (evakoch.com)

aspartate beta-hydroxylase [Sour. (gsea-msigdb.org)

These enzymes catalyze the transfer of a particular group from one substrate to another e.g., aspartate amino transferase (AST), alanine aminotransferase (ALT), hexokinase, phosphoglucomutase, hexose- 1-phosphate uridyltransferase, ornithine carbamoyl transferase etc. (amano-enzyme.com)

This raises questions about identity elements in mt-tRNAs and adaptation of their cognate mt-aaRSs. (cnrs.fr)
It is established that the aminoacylation identity of a single tRNA or of a family of tRNA isoacceptors is linked to the presence of positive signals (determinants) allowing recognition by cognate synthetases and negative signals (antideterminants) leading to rejection by the noncognate ones. (cnrs.fr)

Huperzine A also is non-competitive antagonist of N-methyl-D-aspartate glutamate (NMDA) receptor . (medchemexpress.com)

As the nature of tRNA pools and modifications can vary across biological conditions, codon elongation rates may also vary, leading to fluctuations in the protein production from individual mRNAs. (biomedcentral.com)
Here, we reveal that mRNAs whose expression increases during cell proliferation are enriched in rare codons, poorly adapted to tRNA pools. (biomedcentral.com)
Cleaves mRNAs and tRNAs containing inosine. (nih.gov)

5 plasma) is these HSPs to be up tyrosine stepwise of proteins in form phospholipase ligases. (evakoch.com)

This study explores expression of the defined yeast aspartate identity set into different tRNA scaffolds of a same specificity, namely the four yeast tRNA(Arg) isoacceptors. (cnrs.fr)

The groups called tRNA humans, which become rapidly distributed in eukaryotic processes, as gene for the DNA. (evakoch.com)

We have explored here the human mt-aspartate system in which a prokaryotic-type AspRS, highly similar to the Escherichia coli enzyme, recognizes a bizarre tRNA(Asp). (cnrs.fr)

Mt-tRNAs are atypical with biased sequences, size variations in loops and stems, and absence of residues forming classical tertiary interactions, whereas synthetases appear typical. (cnrs.fr)
The goal was to investigate whether expression of the new identity is similar due to the unique specificity of the host tRNAs or whether it is differently expressed due to their peculiar sequences and structural features. (cnrs.fr)

complexes mostly are fibroblast induction tRNA and tissue of regulatory to immediate transition. (evakoch.com)

Such transplantation experiments were also useful to detect peculiar structural refinements required for optimal expression of a given aminoacylation identity set within a host tRNA. (cnrs.fr)

In vitro transcribed native tRNA(Arg) isoacceptors and variants bearing the aspartate identity elements were prepared and their aminoacylation properties established. (cnrs.fr)

Compositional properties of Aspartate--tRNA ligase (bottom) versus UniprotKB/SwissProt (top). (ucy.ac.cy)

The speed of translation elongation is primarily determined by the abundance of tRNAs. (biomedcentral.com)
Although the translation capacity of proliferating cells was higher compared to resting cells, we did not find evidence for the regulation of individual tRNAs. (biomedcentral.com)
This suggested that tRNA pools fluctuate between cellular states such as proliferation and differentiation to match the "codon demand" of the corresponding transcriptomes and presumably enhance translation efficiency. (biomedcentral.com)

Conversion of the single base-pair C6-G67 into G6-C67, the pair present in tRNA(Asp), allows full expression of the aspartate identity in the transplanted tRNA(2)(Arg), but not in tRNA(3)(Arg). (cnrs.fr)

Among the models that were proposed so far to account for codon-mediated translational regulation upon changing conditions, the one that seems most consistent with our data involves a global upregulation of ready-to-translate tRNAs, which we show can lead to a higher increase in the elongation velocity at rare codons compared to common codons. (biomedcentral.com)

Search for antideterminants in these two tRNAs reveals idiosyncratic features. (cnrs.fr)

Anatomy3

Organisms2

Chemicals and Drugs64

Analytical, Diagnostic and Therapeutic Techniques and Equipment6

Phenomena and Processes24

Information Science3

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

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

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

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

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

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

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

RNA Ligase (ATP)

Polynucleotide Ligases

Polynucleotide 5'-Hydroxyl-Kinase

RNA, Transfer

Amino Acyl-tRNA Synthetases

RNA Splicing

Aspartate Aminotransferases

Aspartate Carbamoyltransferase

Basic-Leucine Zipper Transcription Factors

Saccharomyces cerevisiae

tRNA Methyltransferases

Aspartic Acid

Molecular Sequence Data

Escherichia coli

Ubiquitin-Protein Ligases

Amino Acid Sequence

Anticodon

DNA Ligases

RNA, Transfer, Amino Acid-Specific

RNA, Transfer, Amino Acyl

Base Sequence

RNA, Transfer, Ser

Nucleic Acid Conformation

Aspartate Kinase

Ubiquitination

RNA, Transfer, Phe

Ubiquitin-Protein Ligase Complexes

RNA, Transfer, Trp

RNA, Transfer, Asp

RNA, Transfer, Arg

Ligases

Mutation

Cullin Proteins

RNA, Transfer, Met

RNA, Transfer, Gly

RNA, Transfer, Ile

Ubiquitin

Kinetics

RNA, Transfer, Ala

Glutamate-Cysteine Ligase

RNA, Transfer, Glu

RNA, Transfer, Val

Alanine Transaminase

Aspartate Ammonia-Lyase

Binding Sites

RNA, Transfer, Gln

Substrate Specificity

RNA, Transfer, Pro

RNA, Transfer, His

Protein Binding

Receptors, Amino Acid

RNA, Bacterial

Models, Molecular

Glutamates

Ligase Chain Reaction

SKP Cullin F-Box Protein Ligases

Protein Structure, Tertiary

Codon

Aspartate Aminotransferase, Mitochondrial

Amino Acids

F-Box Proteins

RNA, Transfer, Thr

Phosphonoacetic Acid

Ubiquitin-Conjugating Enzymes

Mutagenesis, Site-Directed

Aminoacylation

Serine-tRNA Ligase

Carbamyl Phosphate

RING Finger Domains

RNA, Fungal

Cytidine Triphosphate

Thiouridine

RNA, Transfer, Cys

Catalysis

Cloning, Molecular

Sequence Homology, Amino Acid

Glutamic Acid

Dihydroorotase

Aspartate-tRNA Ligase

Protein Biosynthesis