RNA Ligase (ATP): An enzyme that catalyzes the conversion of linear RNA to a circular form by the transfer of the 5'-phosphate to the 3'-hydroxyl terminus. It also catalyzes the covalent joining of two polyribonucleotides in phosphodiester linkage. EC 6.5.1.3.Polynucleotide Ligases: Catalyze the joining of preformed ribonucleotides or deoxyribonucleotides in phosphodiester linkage during genetic processes. EC 6.5.1.Polynucleotide 5'-Hydroxyl-Kinase: An enzyme that catalyzes the transfer of a phosphate group to the 5'-terminal hydroxyl groups of DNA and RNA. EC 2.7.1.78.RNA, Transfer: The small RNA molecules, 73-80 nucleotides long, that function during translation (TRANSLATION, GENETIC) to align AMINO ACIDS at the RIBOSOMES in a sequence determined by the mRNA (RNA, MESSENGER). There are about 30 different transfer RNAs. Each recognizes a specific CODON set on the mRNA through its own ANTICODON and as aminoacyl tRNAs (RNA, TRANSFER, AMINO ACYL), each carries a specific amino acid to the ribosome to add to the elongating peptide chains.Amino Acyl-tRNA Synthetases: A subclass of enzymes that aminoacylate AMINO ACID-SPECIFIC TRANSFER RNA with their corresponding AMINO ACIDS.RNA Splicing: The ultimate exclusion of nonsense sequences or intervening sequences (introns) before the final RNA transcript is sent to the cytoplasm.Aspartate Aminotransferases: 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.Aspartate Carbamoyltransferase: 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.Basic-Leucine Zipper Transcription Factors: A large superfamily of transcription factors that contain a region rich in BASIC AMINO ACID residues followed by a LEUCINE ZIPPER domain.Saccharomyces cerevisiae: A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement.tRNA Methyltransferases: Enzymes that catalyze the S-adenosyl-L-methionine-dependent methylation of ribonucleotide bases within a transfer RNA molecule. EC 2.1.1.Aspartic Acid: 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.Molecular Sequence Data: Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.Escherichia coli: A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.Ubiquitin-Protein Ligases: A diverse class of enzymes that interact with UBIQUITIN-CONJUGATING ENZYMES and ubiquitination-specific protein substrates. Each member of this enzyme group has its own distinct specificity for a substrate and ubiquitin-conjugating enzyme. Ubiquitin-protein ligases exist as both monomeric proteins multiprotein complexes.Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.Anticodon: The sequential set of three nucleotides in TRANSFER RNA that interacts with its complement in MESSENGER RNA, the CODON, during translation in the ribosome.DNA Ligases: Poly(deoxyribonucleotide):poly(deoxyribonucleotide)ligases. Enzymes that catalyze the joining of preformed deoxyribonucleotides in phosphodiester linkage during genetic processes during repair of a single-stranded break in duplex DNA. The class includes both EC 6.5.1.1 (ATP) and EC 6.5.1.2 (NAD).RNA, Transfer, Amino Acid-Specific: A group of transfer RNAs which are specific for carrying each one of the 20 amino acids to the ribosome in preparation for protein synthesis.RNA, Transfer, Amino Acyl: Intermediates in protein biosynthesis. The compounds are formed from amino acids, ATP and transfer RNA, a reaction catalyzed by aminoacyl tRNA synthetase. They are key compounds in the genetic translation process.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.RNA, Transfer, Ser: A transfer RNA which is specific for carrying serine to sites on the ribosomes in preparation for protein synthesis.Nucleic Acid Conformation: The spatial arrangement of the atoms of a nucleic acid or polynucleotide that results in its characteristic 3-dimensional shape.Aspartate Kinase: 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.Ubiquitination: The act of ligating UBIQUITINS to PROTEINS to form ubiquitin-protein ligase complexes to label proteins for transport to the PROTEASOME ENDOPEPTIDASE COMPLEX where proteolysis occurs.RNA, Transfer, Phe: A transfer RNA which is specific for carrying phenylalanine to sites on the ribosomes in preparation for protein synthesis.Ubiquitin-Protein Ligase Complexes: Complexes of enzymes that catalyze the covalent attachment of UBIQUITIN to other proteins by forming a peptide bond between the C-terminal GLYCINE of UBIQUITIN and the alpha-amino groups of LYSINE residues in the protein. The complexes play an important role in mediating the selective-degradation of short-lived and abnormal proteins. The complex of enzymes can be broken down into three components that involve activation of ubiquitin (UBIQUITIN-ACTIVATING ENZYMES), conjugation of ubiquitin to the ligase complex (UBIQUITIN-CONJUGATING ENZYMES), and ligation of ubiquitin to the substrate protein (UBIQUITIN-PROTEIN LIGASES).RNA, Transfer, Trp: A transfer RNA which is specific for carrying tryptophan to sites on the ribosomes in preparation for protein synthesis.RNA, Transfer, Asp: A transfer RNA which is specific for carrying aspartic acid to sites on the ribosomes in preparation for protein synthesis.RNA, Transfer, Arg: A transfer RNA which is specific for carrying arginine to sites on the ribosomes in preparation for protein synthesis.Ligases: A class of enzymes that catalyze the formation of a bond between two substrate molecules, coupled with the hydrolysis of a pyrophosphate bond in ATP or a similar energy donor. (Dorland, 28th ed) EC 6.Mutation: Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.Cullin Proteins: A family of structurally related proteins that were originally discovered for their role in cell-cycle regulation in CAENORHABDITIS ELEGANS. They play important roles in regulation of the CELL CYCLE and as components of UBIQUITIN-PROTEIN LIGASES.RNA, Transfer, Met: A transfer RNA which is specific for carrying methionine to sites on the ribosomes. During initiation of protein synthesis, tRNA(f)Met in prokaryotic cells and tRNA(i)Met in eukaryotic cells binds to the start codon (CODON, INITIATOR).RNA, Transfer, Gly: A transfer RNA which is specific for carrying glycine to sites on the ribosomes in preparation for protein synthesis.RNA, Transfer, Ile: A transfer RNA which is specific for carrying isoleucine to sites on the ribosomes in preparation for protein synthesis.Ubiquitin: A highly conserved 76-amino acid peptide universally found in eukaryotic cells that functions as a marker for intracellular PROTEIN TRANSPORT and degradation. Ubiquitin becomes activated through a series of complicated steps and forms an isopeptide bond to lysine residues of specific proteins within the cell. These "ubiquitinated" proteins can be recognized and degraded by proteosomes or be transported to specific compartments within the cell.Kinetics: The rate dynamics in chemical or physical systems.RNA, Transfer, Ala: A transfer RNA which is specific for carrying alanine to sites on the ribosomes in preparation for protein synthesis.Glutamate-Cysteine Ligase: One of the enzymes active in the gamma-glutamyl cycle. It catalyzes the synthesis of gamma-glutamylcysteine from glutamate and cysteine in the presence of ATP with the formation of ADP and orthophosphate. EC 6.3.2.2.RNA, Transfer, Glu: A transfer RNA which is specific for carrying glutamic acid to sites on the ribosomes in preparation for protein synthesis.RNA, Transfer, Val: A transfer RNA which is specific for carrying valine to sites on the ribosomes in preparation for protein synthesis.Alanine Transaminase: An enzyme that catalyzes the conversion of L-alanine and 2-oxoglutarate to pyruvate and L-glutamate. (From Enzyme Nomenclature, 1992) EC 2.6.1.2.Aspartate Ammonia-Lyase: An enzyme that catalyzes the conversion of aspartic acid to ammonia and fumaric acid in plants and some microorganisms. EC 4.3.1.1.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.RNA, Transfer, Gln: A transfer RNA which is specific for carrying glutamine to sites on the ribosomes in preparation for protein synthesis.Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.RNA, Transfer, Pro: A transfer RNA which is specific for carrying proline to sites on the ribosomes in preparation for protein synthesis.RNA, Transfer, His: A transfer RNA which is specific for carrying histidine to sites on the ribosomes in preparation for protein synthesis.Protein Binding: The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.Receptors, Amino Acid: 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.RNA, Bacterial: Ribonucleic acid in bacteria having regulatory and catalytic roles as well as involvement in protein synthesis.Models, Molecular: Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.Glutamates: 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.Ligase Chain Reaction: 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.SKP Cullin F-Box Protein Ligases: 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.Protein Structure, Tertiary: 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.Codon: 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).Aspartate Aminotransferase, Mitochondrial: An aspartate aminotransferase found in MITOCHONDRIA.Amino Acids: 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.F-Box 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.RNA, Transfer, Thr: A transfer RNA which is specific for carrying threonine to sites on the ribosomes in preparation for protein synthesis.Phosphonoacetic Acid: A simple organophosphorus compound that inhibits DNA polymerase, especially in viruses and is used as an antiviral agent.Ubiquitin-Conjugating Enzymes: 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.Mutagenesis, Site-Directed: Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.Aminoacylation: A reaction that introduces an aminoacyl group to a molecule. TRANSFER RNA AMINOACYLATION is the first step in GENETIC TRANSLATION.Serine-tRNA Ligase: An enzyme that activates serine with its specific transfer RNA. EC 6.1.1.11.Carbamyl Phosphate: 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).RING Finger Domains: 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.RNA, Fungal: Ribonucleic acid in fungi having regulatory and catalytic roles as well as involvement in protein synthesis.Cytidine Triphosphate: Cytidine 5'-(tetrahydrogen triphosphate). A cytosine nucleotide containing three phosphate groups esterified to the sugar moiety.Thiouridine: A photoactivable URIDINE analog that is used as an affinity label.RNA, Transfer, Cys: A transfer RNA which is specific for carrying cysteine to sites on the ribosomes in preparation for protein synthesis.Catalysis: The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.Cloning, Molecular: 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.Sequence Homology, Amino Acid: The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.Glutamic Acid: A non-essential amino acid naturally occurring in the L-form. Glutamic acid is the most common excitatory neurotransmitter in the CENTRAL NERVOUS SYSTEM.Dihydroorotase: 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.Aspartate-tRNA Ligase: An enzyme that activates aspartic acid with its specific transfer RNA. EC 6.1.1.12.Protein Biosynthesis: The biosynthesis of PEPTIDES and PROTEINS on RIBOSOMES, directed by MESSENGER RNA, via TRANSFER RNA that is charged with standard proteinogenic AMINO ACIDS.Glutamine: 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.Suppression, Genetic: 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).Liver: A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.Proteasome Endopeptidase Complex: 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.Protein Conformation: 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).Alanine: A non-essential amino acid that occurs in high levels in its free state in plasma. It is produced from pyruvate by transamination. It is involved in sugar and acid metabolism, increases IMMUNITY, and provides energy for muscle tissue, BRAIN, and the CENTRAL NERVOUS SYSTEM.Sequence Alignment: 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.Ribosomes: Multicomponent ribonucleoprotein structures found in the CYTOPLASM of all cells, and in MITOCHONDRIA, and PLASTIDS. They function in PROTEIN BIOSYNTHESIS via GENETIC TRANSLATION.RNA, Transfer, Asn: A transfer RNA which is specific for carrying asparagine to sites on the ribosomes in preparation for protein synthesis.Transcription, Genetic: The biosynthesis of RNA carried out on a template of DNA. The biosynthesis of DNA from an RNA template is called REVERSE TRANSCRIPTION.Lysine: An essential amino acid. It is often added to animal feed.Cell Line: Established cell cultures that have the potential to propagate indefinitely.Pyridoxal Phosphate: 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).Plasmids: 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.Crystallography, X-Ray: The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)RNA Processing, Post-Transcriptional: 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.Structure-Activity Relationship: 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.Bacterial Proteins: 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)
Characterization of a thermosensitive Escherichia coli aspartyl-tRNA synthetase mutant. - Semantic Scholar
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DARS (gene)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 ... isoleucine-trna ligase MeSH D08.811.464.263.200.500 --- leucine-trna ligase MeSH D08.811.464.263.200.550 --- lysine-trna ligase ... tyrosine-tRNA ligase MeSH D08.811.464.263.200.950 --- valine-tRNA ligase MeSH D08.811.464.267.500 --- coenzyme a ligases MeSH ... glutamate-trna ligase MeSH D08.811.464.263.200.350 --- glycine-trna ligase MeSH D08.811.464.263.200.400 --- histidine-trna ...
... 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) IFNGR: interferon-γ receptor gene (6q23-q24) IGF2R ...
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 ...
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 ...
... 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-)- ...
... 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 ...
"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.. ...
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. ...
"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 ...
These experiments have revealed that this single site alternates between two forms, which participate in ligase and hydrolase ... Glutamate aspartate transporter. *Glycerol-3-phosphate dehydrogenase. *ATP synthase. *Carnitine palmitoyltransferase II ...
Active Human Glutamic-Oxaloacetic Transaminase 2, Mitochondrial (Aspartate Aminotransferase 2) (GOT2) Protein (His tag),...Aspartate Aminotransferase 2) (GOT2) Protein (His tag). Species: Human. Source: Escherichia coli (E. coli). Order product ... Glutamate-Cysteine Ligase, Catalytic Subunit Proteins * Glutamate-Ammonia Ligase Proteins * Glutamate Receptor, Metabotropic 8 ... Glutaminyl-tRNA Synthetase Proteins * Glutamyl Aminopeptidase (Aminopeptidase A) Proteins * Glutamyl Prolyl TRNA Synthetase ... Glutamate Receptor, Ionotropic, N-Methyl-D-Aspartate 3A Proteins * Glutamate Receptor, Ionotropic, N-Methyl D-Aspartate-Like 1A ...
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 ...
... aspartate-tRNA ligase activity, aspartate-tRNA(Asn) ligase activity, ATP binding, protein homodimerization activity, tRNA ... IPR004364. aa-tRNA-synt_II. IPR006195. aa-tRNA-synth_II. IPR004524. Asp-tRNA-ligase_1. IPR002312. Asp/Asn-tRNA-synth_IIb. ... IPR004364. aa-tRNA-synt_II. IPR006195. aa-tRNA-synth_II. IPR004524. Asp-tRNA-ligase_1. IPR002312. Asp/Asn-tRNA-synth_IIb. ... Aspartate--tRNA ligase, mitochondrialAdd BLAST. 598. Amino acid modifications. Feature key. Position(s). DescriptionActions. ...
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 ...
C3JYT1 | aspS | Aspartate--tRNA(Asp/Asn) ligase | Druggability | Cancer... tRNA(Asp/Asn) ligase - Also known as SYDND_PSEFS, 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 ...
Chlamydia trachomatis serovar L2b Aspartate--tRNA ligase (aspS) GENTAUR-58b8178e76174 | Gentaursearch... 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* ...
Aspartic acid - DrugBankTrna 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), ...
Browse ORF cDNA clones by species Saccharomyces cerevisiae S288C, page 38aspartate--tRNA ligase DPS1. protein-coding. GLE1. nucleoporin GLE1. protein-coding. YHL050C. hypothetical protein. protein- ...
KEGG SSDB Best Search Result: pbl:PAAG 03986spet: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 ...
ENZYME entry 6.1.1.12Aspartate--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 ...
BRENDA - Information on EC 6.3.1.1 - aspartate-ammonia ligaseCrystal 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 ...
... 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-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 ...
... "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 ...
Thomas Fath - Research Outputs
- Macquarie UniversityExpression 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 ...
BiosynthesisCytoplasmicAminoacylationAlanyl-tRNA synthetaseAspRSAsparaginyl-tRNA synthetaseEnzymeMetabolismSubunitPhenylalanineValineCatalyzesClass-II aminoacyl-tRNA synthetase fSerineLysineSynthetase complexRibonucleate synthetaseGlycineAspartylLysyl-tRNA synthetaseMethionyl-tRNA synthetaseAmino acidGenesPathwaysMagnesium
- This enzyme participates in alanine and aspartate metabolism and aminoacyl-trna biosynthesis. (wikipedia.org)
- Aspartyl-tRNA synthetase charges its cognate tRNA with aspartate during protein biosynthesis. (wikipedia.org)
- 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)
- Aspartyl-tRNA synthetase, cytoplasmic is an enzyme that in humans is encoded by the DARS gene. (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)
- The tRNA for Asn can be produced in either of two ways: direct aminoacylation with Asn, and misacylation with Asp that is subsequently amidated to Asn. (jcvi.org)
- This property describes a single polypeptide chain tRNA ligase responsible for direct aminoacylation with Asn. (jcvi.org)
- Recombinant alanyl-tRNA synthetase Protein, Mouse (His Tag) Recombinant Proteins The mouse AARS (Q8BGQ7) (Met 1-Asn 968) was fused with a polyhistidine tag at the C-terminus The secreted recombinant mouse AARS consists of 978a.a and has a calculated molecular weight of 108.3 kDa. (thebiotek.com)
- Alanyl-tRNA synthetase (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)
- The structure of an AspRS-tRNA(Asp) complex reveals a tRNA-dependent control mechanism. (nih.gov)
- This enzyme is also called nondiscriminating asparaginyl-tRNA synthetase. (wikipedia.org)
- However, despite encoding asparaginyl-tRNA synthetase and glutaminyl-tRNA synthetase, B. bacteriovorus also contains the amidotransferase GatCAB. (nih.gov)
- 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 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)
- The systematic name of this enzyme class is L-asparagine:tRNAAsn ligase (AMP-forming). (wikipedia.org)
- The overall structure of the enzyme is remarkably similar to that of the catalytic domain of yeast aspartyl-tRNA synthetase despite low sequence similarity. (nih.gov)
- In enzymology, an asparaginyl-tRNA synthase (glutamine-hydrolysing) (EC 6.3.5.6) is an enzyme that catalyzes the chemical reaction ATP + aspartyl-tRNAAsn + L-glutamine ⇌ {\displaystyle \rightleftharpoons } ADP + phosphate + asparaginyl-tRNAAsn + L-glutamate The 3 substrates of this enzyme are ATP, aspartyl-tRNA(Asn), and L-glutamine, whereas its 4 products are ADP, phosphate, asparaginyl-tRNA(Asn), and L-glutamate. (wikipedia.org)
- This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds carbon-nitrogen ligases with glutamine as amido-N-donor. (wikipedia.org)
- The systematic name of this enzyme class is aspartyl-tRNAAsn:L-glutamine amido-ligase (ADP-forming). (wikipedia.org)
- This enzyme participates in glutamate metabolism and alanine and aspartate metabolism. (wikipedia.org)
- 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)
- 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)
- Although phenylalanine-tRNA synthetase is class II, it aminoacylates at the 2'-OH. (wikipedia.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)
- Catalyzes the attachment of valine to tRNA(Val). (string-db.org)
- 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 attachment of isoleucine to tRNA(Ile). (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)
- The protein encoded by this gene belongs to the class-II aminoacyl-tRNA synthetase family. (genecards.org)
- Now included with EC 3.4.16.5, carboxypeptidase C EC 3.4.16.4: serine-type D-Ala-D-Ala carboxypeptidase EC 3.4.16.5: carboxypeptidase c EC 3.4.16.6: carboxypeptidase D EC 3.4.17.1: carboxypeptidase A EC 3.4.17.2: carboxypeptidase B EC 3.4.17.3: lysine carboxypeptidase EC 3.4.17.4: Gly-X carboxypeptidase EC 3.4.17.5: Deleted entry: aspartate carboxypeptidase EC 3.4.17.6: alanine carboxypeptidase EC 3.4.17.7: Transferred entry: acylmuramoyl-alanine carboxypeptidase. (wikipedia.org)
- 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)
- Structural analysis of the high molecular mass aminoacyl-tRNA synthetase complex. (wikipedia.org)
- aminoacyl-tRNA synthetase complex. (cbrc.jp)
- Yeast tRNA(Asp)-aspartyl-tRNA synthetase complex: low resolution crystal structure. (cbrc.jp)
- 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)
- In contrast, glycine- and L-amino acid-containing cross-links are synthesized by the Fem ligases of the GCN5-like acetyltransferase (GNAT) fold. (biomedcentral.com)
- Studies on aspartyl-tRNA synthetase from Baker's yeast. (wikipedia.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)
- ATP + L-aspartate + tRNA Asp = AMP + diphosphate + L-aspartyl-tRNA Asp . (rcsb.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)
- ATP + L-aspartate + tRNA Asx = AMP + diphosphate + L-aspartyl-tRNA Asx . (rcsb.org)
- It has, however, diminished discrimination, so that it can also form aspartyl-tRNA(Asn). (expasy.org)
- Expression of human aspartyl-tRNA synthetase in Escherichia coli. (wikipedia.org)
- 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)
- Synthesis of aspartyl-tRNA(Asp) in Escherichia coli--a snapshot of the second step. (nagahama-i-bio.ac.jp)
- The predatory bacterium Bdellovibrio bacteriovorus aspartyl-tRNA synthetase recognizes tRNAAsn as a substrate. (nih.gov)
- Both also code for a second aspartyl-tRNA synthetase and use the additional aspartyl-tRNA synthetase with GatCAB to synthesize asparagine on tRNAAsn. (nih.gov)
- Unlike those two bacteria, B. bacteriovorus encodes only one aspartyl-tRNA synthetase. (nih.gov)
- 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. (nih.gov)
- 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)
- 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. (nih.gov)
- Other names in common use include Asp-AdT, Asp-tRNAAsn amidotransferase, aspartyl-tRNAAsn amidotransferase, and Asn-tRNAAsn:L-glutamine amido-ligase (ADP-forming). (wikipedia.org)
- NG1489 is paralogously related to NG1454 (lysyl-tRNA synthetase (LysRS)) (1e-11). (northwestern.edu)
- 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)
- L-aspartate is considered a non-essential amino acid, meaning that, under normal physiological conditions, sufficient amounts of the amino acid are synthesized in the body to meet the body's requirements. (drugbank.ca)
- This is sometimes called "charging" or "loading" the tRNA with the amino acid. (wikipedia.org)
- Once the tRNA is charged, a ribosome can transfer the amino acid from the tRNA onto a growing peptide , according to the genetic code. (wikipedia.org)
- 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)
- 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)
- 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)
- 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)