A transfer RNA which is specific for carrying arginine to sites on the ribosomes in preparation for protein synthesis.
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.
The sequential set of three nucleotides in TRANSFER RNA that interacts with its complement in MESSENGER RNA, the CODON, during translation in the ribosome.
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.
A large superfamily of transcription factors that contain a region rich in BASIC AMINO ACID residues followed by a LEUCINE ZIPPER domain.
A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement.
Enzymes that catalyze the S-adenosyl-L-methionine-dependent methylation of ribonucleotide bases within a transfer RNA molecule. EC 2.1.1.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
A diverse class of enzymes that interact with UBIQUITIN-CONJUGATING ENZYMES and ubiquitination-specific protein substrates. Each member of this enzyme group has its own distinct specificity for a substrate and ubiquitin-conjugating enzyme. Ubiquitin-protein ligases exist as both monomeric proteins multiprotein complexes.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
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).
An enzyme that catalyzes the phosphorylation of the guanidine nitrogen of arginine in the presence of ATP and a divalent cation with formation of phosphorylarginine and ADP. EC 2.7.3.3.
The predominant form of mammalian antidiuretic hormone. It is a nonapeptide containing an ARGININE at residue 8 and two disulfide-linked cysteines at residues of 1 and 6. Arg-vasopressin is used to treat DIABETES INSIPIDUS or to improve vasomotor tone and BLOOD PRESSURE.
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.
The spatial arrangement of the atoms of a nucleic acid or polynucleotide that results in its characteristic 3-dimensional shape.
A transfer RNA which is specific for carrying serine to sites on the ribosomes in preparation for protein synthesis.
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).
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 transfer RNA which is specific for carrying tryptophan to sites on the ribosomes in preparation for protein synthesis.
NATIONAL LIBRARY OF MEDICINE service for health professionals and consumers. It links extensive information from the National Institutes of Health and other reviewed sources of information on specific diseases and conditions.
An enzyme that activates arginine with its specific transfer RNA. EC 6.1.1.19.
Value of all final goods and services produced in a country in one year.
This amino acid is formed during the urea cycle from citrulline, aspartate and ATP. This reaction is catalyzed by argininosuccinic acid synthetase.
An agency of the NATIONAL INSTITUTES OF HEALTH concerned with overall planning, promoting, and administering programs pertaining to advancement of medical and related sciences. Major activities of this institute include the collection, dissemination, and exchange of information important to the progress of medicine and health, research in medical informatics and support for medical library development.

tRNA synthetase mutants of Escherichia coli K-12 are resistant to the gyrase inhibitor novobiocin. (1/72)

In previous studies we demonstrated that mutations in the genes cysB, cysE, and cls (nov) affect resistance of Escherichia coli to novobiocin (J. Rakonjac, M. Milic, and D. J. Savic, Mol. Gen. Genet. 228:307-311, 1991; R. Ivanisevic, M. Milic, D. Ajdic, J. Rakonjac, and D. J. Savic, J. Bacteriol. 177:1766-1771, 1995). In this work we expand this list with mutations in rpoN (the gene for RNA polymerase subunit sigma54) and the tRNA synthetase genes alaS, argS, ileS, and leuS. Similarly to resistance to the penicillin antibiotic mecillinam, resistance to novobiocin of tRNA synthetase mutants appears to depend upon the RelA-mediated stringent response. However, at this point the overlapping pathways of mecillinam and novobiocin resistance diverge. Under conditions of stringent response induction, either by the presence of tRNA synthetase mutations or by constitutive production of RelA protein, inactivation of the cls gene diminishes resistance to novobiocin but not to mecillinam.  (+info)

Precursor of pro-apoptotic cytokine modulates aminoacylation activity of tRNA synthetase. (2/72)

Endothelial monocyte activating polypeptide II (EMAPII) is a cytokine that is specifically induced by apoptosis. Its precursor (pro-EMAPII) has been suggested to be identical to p43, which is associated with the multi-tRNA synthetase complex. Herein, we have demonstrated that the N-terminal domain of pro-EMAPII interacts with the N-terminal extension of human cytoplasmic arginyl-tRNA synthetase (RRS) using genetic and immunoprecipitation analyses. Aminoacylation activity of RRS was enhanced about 2.5-fold by the interaction with pro-EMAPII but not with its N- or C-terminal domains alone. The N-terminal extension of RRS was not required for enzyme activity but did mediate activity stimulation by pro-EMAPII. Pro-EMAPII reduced the apparent Km of RRS to tRNA, whereas the kcat value remained unchanged. Therefore, the precursor of EMAPII is a multi-functional protein that assists aminoacylation in normal cells and releases the functional cytokine upon apoptosis.  (+info)

In vivo selection of lethal mutations reveals two functional domains in arginyl-tRNA synthetase. (3/72)

Using random mutagenesis and a genetic screening in yeast, we isolated 26 mutations that inactivate Saccharomyces cerevisiae arginyl-tRNA synthetase (ArgRS). The mutations were identified and the kinetic parameters of the corresponding proteins were tested after purification of the expression products in Escherichia coli. The effects were interpreted in the light of the crystal structure of ArgRS. Eighteen functional residues were found around the arginine-binding pocket and eight others in the carboxy-terminal domain of the enzyme. Mutations of these residues all act by strongly impairing the rates of tRNA charging and arginine activation. Thus, ArgRS and tRNA(Arg) can be considered as a kind of ribonucleoprotein, where the tRNA, before being charged, is acting as a cofactor that activates the enzyme. Furthermore, by using different tRNA(Arg) isoacceptors and heterologous tRNA(Asp), we highlighted the crucial role of several residues of the carboxy-terminal domain in tRNA recognition and discrimination.  (+info)

Active aminoacyl-tRNA synthetases are present in nuclei as a high molecular weight multienzyme complex. (4/72)

Recent studies suggest that aminoacylation of tRNA may play an important role in the transport of these molecules from the nucleus to the cytoplasm. However, there is almost no information regarding the status of active aminoacyl-tRNA synthetases within the nuclei of eukaryotic cells. Here we show that at least 13 active aminoacyl-tRNA synthetases are present in purified nuclei of both Chinese hamster ovary and rabbit kidney cells, although their steady-state levels represent only a small percentage of those found in the cytoplasm. Most interestingly, all the nuclear aminoacyl-tRNA synthetases examined can be isolated as part of a multienzyme complex that is more stable, and consequently larger, than the comparable complex isolated from the cytoplasm. These data directly demonstrate the presence of active aminoacyl-tRNA synthetases in mammalian cell nuclei. Moreover, their unexpected structural organization raises important questions about the functional significance of these multienzyme complexes and whether they might play a more direct role in nuclear to cytoplasmic transport of tRNAs.  (+info)

Effect of sodium bisulfite modification on the arginine acceptance of E. coli tRNA Arg. (5/72)

Escherichia coli tRNA Arg was treated with sodium bisulfite to convert exposed cytosine residues to uracil. This treatment resulted in the loss of amino acid acceptance of the tRNA Arg with pseudo first-order reaction kinetics. The active and inactive molecules were separated after about 60e active and inactive molecules were separated after about 60 percent inactivation and analyzed for U in various positions by finger-printing of the oligonucleotides produced by nucleases. The results show that C to U base transitions in the dihydrouridine loop and in the CCA terminus have no effect on the aminoacylation of this tRNA. Deamination of a cytosine residue at the second position of the anticodon resulted in the loss of amino acid acceptor activity of arginine transfer RNA.  (+info)

Studies on arginyl-tRNA synthetase from Escherichia coli B. Dual role of metals in enzyme catalysis. (6/72)

Studies carried out in arginyl-tRNA synthetase from Escherichia coli indicate that metals may have two functional roles in the catalytic mechanism. Complete metal activation is observed when MgCl2, MnCl2, CoCl2, or FeCl2 is present at a concentration (5.0 mM) in excess of the total ATP concentration (2.0 mM). When CaCl2 is substituted for MgCl2, activity is not observed unless a small amount (0.1 mM) of MgCl2, MnCl2, CoCl2, FeCl2, or ZnCl2 (unable to produce activity alone at 5.0 mM) is added. A model, based on kinetic data, is proposed in which the enzyme possesses a site for free metal, which, when filled, lowers the Km for all three substrates (arginine, tRNAArg, and metal-ATP) and increases the Vmax of the reaction.  (+info)

tRNA aminoacylation by arginyl-tRNA synthetase: induced conformations during substrates binding. (7/72)

The 2.2 A crystal structure of a ternary complex formed by yeast arginyl-tRNA synthetase and its cognate tRNA(Arg) in the presence of the L-arginine substrate highlights new atomic features used for specific substrate recognition. This first example of an active complex formed by a class Ia aminoacyl-tRNA synthetase and its natural cognate tRNA illustrates additional strategies used for specific tRNA selection. The enzyme specifically recognizes the D-loop and the anticodon of the tRNA, and the mutually induced fit produces a conformation of the anticodon loop never seen before. Moreover, the anticodon binding triggers conformational changes in the catalytic center of the protein. The comparison with the 2.9 A structure of a binary complex formed by yeast arginyl-tRNA synthetase and tRNA(Arg) reveals that L-arginine binding controls the correct positioning of the CCA end of the tRNA(Arg). Important structural changes induced by substrate binding are observed in the enzyme. Several key residues of the active site play multiple roles in the catalytic pathway and thus highlight the structural dynamics of the aminoacylation reaction.  (+info)

Crucial role of the high-loop lysine for the catalytic activity of arginyl-tRNA synthetase. (8/72)

The presence of two short signature sequence motifs (His-Ile-Gly-His (HIGH) and Lys-Met-Ser-Lys (KMSK)) is a characteristic of the class I aminoacyl-tRNA synthetases. These motifs constitute a portion of the catalytic site in three dimensions and play an important role in catalysis. In particular, the second lysine of the KMSK motif (K2) is the crucial catalytic residue for stabilization of the transition state of the amino acid activation reaction (aminoacyl-adenylate formation). Arginyl-tRNA synthetase (ArgRS) is unique among all of the class I enyzmes, as the majority of ArgRS species lack canonical KMSK sequences. Thus, the mechanism by which this group of ArgRSs achieves the catalytic reaction is not well understood. Using three-dimensional modeling in combination with sequence analysis and site-directed mutagenesis, we found a conserved lysine in the KMSK-lacking ArgRSs upstream of the HIGH sequence motif, which is likely to be a functional counterpart of the canonical class I K2 lysine. The results suggest a plausible partition of the ArgRSs into two major groups, on the basis of the conservation of the HIGH lysine.  (+info)

I'm happy to help! However, it seems like the term you're looking for is "Transfer RNA arginine," not "Arg." Transfer RNA (tRNA) is a type of RNA molecule that plays a crucial role in protein synthesis. Specifically, tRNAs are responsible for delivering amino acids to the ribosome, where they are joined together to form proteins.

Each tRNA molecule contains a specific anticodon sequence that can base-pair with a complementary codon sequence on messenger RNA (mRNA). When a tRNA molecule encounters an mRNA codon that matches its anticodon, it binds to the mRNA and delivers the amino acid associated with that tRNA.

In the case of tRNA arginine, this type of tRNA is responsible for delivering the amino acid arginine to the ribosome during protein synthesis. Arginine is a positively charged amino acid that plays important roles in various cellular processes, including protein structure and function, signal transduction, and gene regulation.

Therefore, Transfer RNA arginine refers to the specific tRNA molecule that delivers the amino acid arginine during protein synthesis.

An anticodon is a sequence of three ribonucleotides (RNA bases) in a transfer RNA (tRNA) molecule that pair with a complementary codon in a messenger RNA (mRNA) molecule during protein synthesis. This interaction occurs within the ribosome during translation, where the genetic code in the mRNA is translated into an amino acid sequence in a polypeptide. Specifically, each tRNA carries a specific amino acid that corresponds to its anticodon sequence, allowing for the accurate and systematic addition of amino acids to the growing polypeptide chain.

In summary, an anticodon is a crucial component of the translation machinery, facilitating the precise decoding of genetic information and enabling the synthesis of proteins according to the instructions encoded in mRNA molecules.

Polynucleotide ligases are enzymes that catalyze the formation of phosphodiester bonds between the 3'-hydroxyl and 5'-phosphate ends of two adjacent nucleotides in a polynucleotide chain, such as DNA. These enzymes play a crucial role in the repair and replication of DNA, by sealing breaks or gaps in the sugar-phosphate backbone of the DNA molecule. They are essential for maintaining genomic integrity and stability, and have been widely used in molecular biology research and biotechnological applications, including DNA sequencing, cloning, and genetic engineering. Polynucleotide ligases can be found in various organisms, from bacteria to humans, and they typically require ATP or NAD+ as a cofactor for the ligation reaction.

Polynucleotide 5'-Hydroxyl-Kinase (PNK) is an enzyme that catalyzes the addition of a phosphate group to the 5'-hydroxyl end of a polynucleotide strand, such as DNA or RNA. This enzyme plays a crucial role in the repair and maintenance of DNA ends during various cellular processes, including DNA replication, recombination, and repair.

PNK has two distinct activities: 5'-kinase activity and 3'-phosphatase activity. The 5'-kinase activity adds a phosphate group to the 5'-hydroxyl end of a polynucleotide strand, while the 3'-phosphatase activity removes a phosphate group from the 3'-end of a strand. These activities enable PNK to process and repair DNA ends with missing or damaged phosphate groups, ensuring their proper alignment and ligation during DNA repair and recombination.

PNK is involved in several essential cellular pathways, including base excision repair (BER), nucleotide excision repair (NER), and double-strand break (DSB) repair. Dysregulation or mutations in PNK can lead to genomic instability and contribute to the development of various diseases, such as cancer and neurodegenerative disorders.

Transfer RNA (tRNA) is a type of RNA molecule that plays a crucial role in protein synthesis, the process by which cells create proteins. In protein synthesis, tRNAs serve as adaptors, translating the genetic code present in messenger RNA (mRNA) into the corresponding amino acids required to build a protein.

Each tRNA molecule has a distinct structure, consisting of approximately 70-90 nucleotides arranged in a cloverleaf shape with several loops and stems. The most important feature of a tRNA is its anticodon, a sequence of three nucleotides located in one of the loops. This anticodon base-pairs with a complementary codon on the mRNA during translation, ensuring that the correct amino acid is added to the growing polypeptide chain.

Before tRNAs can participate in protein synthesis, they must be charged with their specific amino acids through an enzymatic process involving aminoacyl-tRNA synthetases. These enzymes recognize and bind to both the tRNA and its corresponding amino acid, forming a covalent bond between them. Once charged, the aminoacyl-tRNA complex is ready to engage in translation and contribute to protein formation.

In summary, transfer RNA (tRNA) is a small RNA molecule that facilitates protein synthesis by translating genetic information from messenger RNA into specific amino acids, ultimately leading to the creation of functional proteins within cells.

Aminoacyl-tRNA synthetases (also known as aminoacyl-tRNA ligases) are a group of enzymes that play a crucial role in protein synthesis. They are responsible for attaching specific amino acids to their corresponding transfer RNAs (tRNAs), creating aminoacyl-tRNA complexes. These complexes are then used in the translation process to construct proteins according to the genetic code.

Each aminoacyl-tRNA synthetase is specific to a particular amino acid, and there are 20 different synthetases in total, one for each of the standard amino acids. The enzymes catalyze the reaction between an amino acid and ATP to form an aminoacyl-AMP intermediate, which then reacts with the appropriate tRNA to create the aminoacyl-tRNA complex. This two-step process ensures the fidelity of the translation process by preventing mismatching of amino acids with their corresponding tRNAs.

Defects in aminoacyl-tRNA synthetases can lead to various genetic disorders and diseases, such as Charcot-Marie-Tooth disease type 2D, distal spinal muscular atrophy, and leukoencephalopathy with brainstem and spinal cord involvement and lactate acidosis (LBSL).

RNA splicing is a post-transcriptional modification process in which the non-coding sequences (introns) are removed and the coding sequences (exons) are joined together in a messenger RNA (mRNA) molecule. This results in a continuous mRNA sequence that can be translated into a single protein. Alternative splicing, where different combinations of exons are included or excluded, allows for the creation of multiple proteins from a single gene.

Basic-leucine zipper (bZIP) transcription factors are a family of transcriptional regulatory proteins characterized by the presence of a basic region and a leucine zipper motif. The basic region, which is rich in basic amino acids such as lysine and arginine, is responsible for DNA binding, while the leucine zipper motif mediates protein-protein interactions and dimerization.

BZIP transcription factors play important roles in various cellular processes, including gene expression regulation, cell growth, differentiation, and stress response. They bind to specific DNA sequences called AP-1 sites, which are often found in the promoter regions of target genes. BZIP transcription factors can form homodimers or heterodimers with other bZIP proteins, allowing for combinatorial control of gene expression.

Examples of bZIP transcription factors include c-Jun, c-Fos, ATF (activating transcription factor), and CREB (cAMP response element-binding protein). Dysregulation of bZIP transcription factors has been implicated in various diseases, including cancer, inflammation, and neurodegenerative disorders.

"Saccharomyces cerevisiae" is not typically considered a medical term, but it is a scientific name used in the field of microbiology. It refers to a species of yeast that is commonly used in various industrial processes, such as baking and brewing. It's also widely used in scientific research due to its genetic tractability and eukaryotic cellular organization.

However, it does have some relevance to medical fields like medicine and nutrition. For example, certain strains of S. cerevisiae are used as probiotics, which can provide health benefits when consumed. They may help support gut health, enhance the immune system, and even assist in the digestion of certain nutrients.

In summary, "Saccharomyces cerevisiae" is a species of yeast with various industrial and potential medical applications.

tRNA (transfer RNA) methyltransferases are a group of enzymes that catalyze the transfer of a methyl group (-CH3) to specific positions on the tRNA molecule. These enzymes play a crucial role in modifying and regulating tRNA function, stability, and interaction with other components of the translation machinery during protein synthesis.

The addition of methyl groups to tRNAs can occur at various sites, including the base moieties of nucleotides within the anticodon loop, the TψC loop, and the variable region. These modifications help maintain the structural integrity of tRNA molecules, enhance their ability to recognize specific codons during translation, and protect them from degradation by cellular nucleases.

tRNA methyltransferases are classified based on the type of methylation they catalyze:

1. N1-methyladenosine (m1A) methyltransferases: These enzymes add a methyl group to the N1 position of adenosine residues in tRNAs. An example is TRMT6/TRMT61A, which methylates adenosines at position 58 in human tRNAs.
2. N3-methylcytosine (m3C) methyltransferases: These enzymes add a methyl group to the N3 position of cytosine residues in tRNAs. An example is Dnmt2, which methylates cytosines at position 38 in various organisms.
3. N7-methylguanosine (m7G) methyltransferases: These enzymes add a methyl group to the N7 position of guanosine residues in tRNAs, primarily at position 46 within the TψC loop. An example is Trm8/Trm82, which catalyzes this modification in yeast and humans.
4. 2'-O-methylated nucleotides (Nm) methyltransferases: These enzymes add a methyl group to the 2'-hydroxyl group of ribose sugars in tRNAs, which can occur at various positions throughout the molecule. An example is FTSJ1, which methylates uridines at position 8 in human tRNAs.
5. Pseudouridine (Ψ) synthases: Although not technically methyltransferases, pseudouridine synthases catalyze the isomerization of uridine to pseudouridine, which can enhance tRNA stability and function. An example is Dyskerin (DKC1), which introduces Ψ at various positions in human tRNAs.

These enzymes play crucial roles in modifying tRNAs, ensuring proper folding, stability, and function during translation. Defects in these enzymes can lead to various diseases, including neurological disorders, cancer, and premature aging.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

'Escherichia coli' (E. coli) is a type of gram-negative, facultatively anaerobic, rod-shaped bacterium that commonly inhabits the intestinal tract of humans and warm-blooded animals. It is a member of the family Enterobacteriaceae and one of the most well-studied prokaryotic model organisms in molecular biology.

While most E. coli strains are harmless and even beneficial to their hosts, some serotypes can cause various forms of gastrointestinal and extraintestinal illnesses in humans and animals. These pathogenic strains possess virulence factors that enable them to colonize and damage host tissues, leading to diseases such as diarrhea, urinary tract infections, pneumonia, and sepsis.

E. coli is a versatile organism with remarkable genetic diversity, which allows it to adapt to various environmental niches. It can be found in water, soil, food, and various man-made environments, making it an essential indicator of fecal contamination and a common cause of foodborne illnesses. The study of E. coli has contributed significantly to our understanding of fundamental biological processes, including DNA replication, gene regulation, and protein synthesis.

Ubiquitin-protein ligases, also known as E3 ubiquitin ligases, are a group of enzymes that play a crucial role in the ubiquitination process. Ubiquitination is a post-translational modification where ubiquitin molecules are attached to specific target proteins, marking them for degradation by the proteasome or for other regulatory functions.

Ubiquitin-protein ligases catalyze the final step in this process by binding to both the ubiquitin protein and the target protein, facilitating the transfer of ubiquitin from an E2 ubiquitin-conjugating enzyme to the target protein. There are several different types of ubiquitin-protein ligases, each with their own specificity for particular target proteins and regulatory functions.

Ubiquitin-protein ligases have been implicated in various cellular processes such as protein degradation, DNA repair, signal transduction, and regulation of the cell cycle. Dysregulation of ubiquitination has been associated with several diseases, including cancer, neurodegenerative disorders, and inflammatory responses. Therefore, understanding the function and regulation of ubiquitin-protein ligases is an important area of research in biology and medicine.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

DNA ligases are enzymes that catalyze the formation of a phosphodiester bond between two compatible ends of DNA molecules, effectively joining or "ligating" them together. There are several types of DNA ligases found in nature, each with specific functions and preferences for the type of DNA ends they can seal.

The most well-known DNA ligase is DNA ligase I, which plays a crucial role in replicating and repairing DNA in eukaryotic cells. It seals nicks or gaps in double-stranded DNA during replication and participates in the final step of DNA excision repair by rejoining the repaired strand to the original strand.

DNA ligase IV, another important enzyme, is primarily involved in the repair of double-strand breaks through a process called non-homologous end joining (NHEJ). This pathway is essential for maintaining genome stability and preventing chromosomal abnormalities.

Bacterial DNA ligases, such as T4 DNA ligase, are often used in molecular biology techniques due to their ability to join various types of DNA ends with high efficiency. These enzymes have been instrumental in the development of recombinant DNA technology and gene cloning methods.

Arginine kinase is an enzyme that catalyzes the phosphorylation of arginine, a basic amino acid, to form phosphoarginine. This reaction plays a crucial role in energy metabolism in various organisms, including invertebrates and microorganisms. Phosphoarginine serves as an energy storage molecule, similar to how phosphocreatine is used in vertebrate muscle tissue. Arginine kinase is not typically found in mammals, but it is present in other animals such as insects, crustaceans, and mollusks. The enzyme helps facilitate rapid energy transfer during high-intensity activities, supporting the organism's physiological functions.

Arginine vasopressin (AVP), also known as antidiuretic hormone (ADH), is a hormone produced in the hypothalamus and stored in the posterior pituitary gland. It plays a crucial role in regulating water balance and blood pressure in the body.

AVP acts on the kidneys to promote water reabsorption, which helps maintain adequate fluid volume and osmotic balance in the body. It also constricts blood vessels, increasing peripheral vascular resistance and thereby helping to maintain blood pressure. Additionally, AVP has been shown to have effects on cognitive function, mood regulation, and pain perception.

Deficiencies or excesses of AVP can lead to a range of medical conditions, including diabetes insipidus (characterized by excessive thirst and urination), hyponatremia (low sodium levels in the blood), and syndrome of inappropriate antidiuretic hormone secretion (SIADH).

Transfer RNA (tRNA) are small RNA molecules that play a crucial role in protein synthesis. They are responsible for translating the genetic code contained within messenger RNA (mRNA) into the specific sequence of amino acids during protein synthesis.

Amino acid-specific tRNAs are specialized tRNAs that recognize and bind to specific amino acids. Each tRNA has an anticodon region that can base-pair with a complementary codon on the mRNA, which determines the specific amino acid that will be added to the growing polypeptide chain during protein synthesis.

Therefore, a more detailed medical definition of "RNA, Transfer, Amino Acid-Specific" would be:

A type of transfer RNA (tRNA) molecule that is specific to a particular amino acid and plays a role in translating the genetic code contained within messenger RNA (mRNA) into the specific sequence of amino acids during protein synthesis. The anticodon region of an amino acid-specific tRNA base-pairs with a complementary codon on the mRNA, which determines the specific amino acid that will be added to the growing polypeptide chain during protein synthesis.

Transfer RNA (tRNA) is a type of RNA molecule that plays a crucial role in protein synthesis. It serves as the adaptor molecule that translates the genetic code present in messenger RNA (mRNA) into the corresponding amino acids, which are then linked together to form a polypeptide chain during protein synthesis.

Aminoacyl tRNA is a specific type of tRNA molecule that has been charged or activated with an amino acid. This process is called aminoacylation and is carried out by enzymes called aminoacyl-tRNA synthetases. Each synthetase specifically recognizes and attaches a particular amino acid to its corresponding tRNA, ensuring the fidelity of protein synthesis. Once an amino acid is attached to a tRNA, it forms an aminoacyl-tRNA complex, which can then participate in translation and contribute to the formation of a new protein.

A base sequence in the context of molecular biology refers to the specific order of nucleotides in a DNA or RNA molecule. In DNA, these nucleotides are adenine (A), guanine (G), cytosine (C), and thymine (T). In RNA, uracil (U) takes the place of thymine. The base sequence contains genetic information that is transcribed into RNA and ultimately translated into proteins. It is the exact order of these bases that determines the genetic code and thus the function of the DNA or RNA molecule.

Nucleic acid conformation refers to the three-dimensional structure that nucleic acids (DNA and RNA) adopt as a result of the bonding patterns between the atoms within the molecule. The primary structure of nucleic acids is determined by the sequence of nucleotides, while the conformation is influenced by factors such as the sugar-phosphate backbone, base stacking, and hydrogen bonding.

Two common conformations of DNA are the B-form and the A-form. The B-form is a right-handed helix with a diameter of about 20 Å and a pitch of 34 Å, while the A-form has a smaller diameter (about 18 Å) and a shorter pitch (about 25 Å). RNA typically adopts an A-form conformation.

The conformation of nucleic acids can have significant implications for their function, as it can affect their ability to interact with other molecules such as proteins or drugs. Understanding the conformational properties of nucleic acids is therefore an important area of research in molecular biology and medicine.

Transfer RNA (tRNA) is a type of RNA molecule that plays a crucial role in protein synthesis in the cell. It carries and transfers specific amino acids to the growing polypeptide chain during translation, the process by which the genetic code in mRNA is translated into a protein sequence.

tRNAs have a characteristic cloverleaf-like secondary structure and a stem-loop tertiary structure, which allows them to bind both to specific amino acids and to complementary codon sequences on the messenger RNA (mRNA) through anticodons. This enables the precise matching of the correct amino acid to its corresponding codon in the mRNA during protein synthesis.

Ser, or serine, is one of the 20 standard amino acids that make up proteins. It is encoded by six different codons (UCU, UCC, UCA, UCG, AGU, and AGC) in the genetic code. The corresponding tRNA molecule that carries serine during protein synthesis is called tRNASer. There are multiple tRNASer isoacceptors, each with a different anticodon sequence but all carrying the same amino acid, serine.

Ubiquitination is a post-translational modification process in which a ubiquitin protein is covalently attached to a target protein. This process plays a crucial role in regulating various cellular functions, including protein degradation, DNA repair, and signal transduction. The addition of ubiquitin can lead to different outcomes depending on the number and location of ubiquitin molecules attached to the target protein. Monoubiquitination (the attachment of a single ubiquitin molecule) or multiubiquitination (the attachment of multiple ubiquitin molecules) can mark proteins for degradation by the 26S proteasome, while specific types of ubiquitination (e.g., K63-linked polyubiquitination) can serve as a signal for nonproteolytic functions such as endocytosis, autophagy, or DNA repair. Ubiquitination is a highly regulated process that involves the coordinated action of three enzymes: E1 ubiquitin-activating enzyme, E2 ubiquitin-conjugating enzyme, and E3 ubiquitin ligase. Dysregulation of ubiquitination has been implicated in various diseases, including cancer, neurodegenerative disorders, and inflammatory conditions.

Transfer RNA (tRNA) is a type of RNA molecule that helps translate genetic information from messenger RNA (mRNA) into proteins. Each tRNA carries a specific amino acid to the growing polypeptide chain during protein synthesis, based on the anticodon sequence in its variable loop region that recognizes and binds to a complementary codon sequence in the mRNA.

Phenylalanine (Phe) is one of the twenty standard amino acids found in proteins. It has a hydrophobic side chain, which means it tends to repel water and interact with other non-polar molecules. In tRNA, phenylalanine is attached to a specific tRNA molecule known as tRNAPhe. This tRNA recognizes the mRNA codons UUC and UUU, which specify phenylalanine during protein synthesis.

Ubiquitin-Protein Ligase Complexes, also known as E3 ubiquitin ligases, are a group of enzymes that play a crucial role in the ubiquitination process. Ubiquitination is a post-translational modification where ubiquitin molecules are attached to specific target proteins, marking them for degradation by the proteasome or altering their function, localization, or interaction with other proteins.

The ubiquitination process involves three main steps:

1. Ubiquitin activation: Ubiquitin is activated by an E1 ubiquitin-activating enzyme in an ATP-dependent reaction.
2. Ubiquitin conjugation: The activated ubiquitin is then transferred to an E2 ubiquitin-conjugating enzyme.
3. Ubiquitin ligation: Finally, the E2 ubiquitin-conjugating enzyme interacts with a specific E3 ubiquitin ligase complex, which facilitates the transfer and ligation of ubiquitin to the target protein.

Ubiquitin-Protein Ligase Complexes are responsible for recognizing and binding to specific substrate proteins, ensuring that ubiquitination occurs on the correct targets. They can be divided into three main categories based on their structural features and mechanisms of action:

1. Really Interesting New Gene (RING) finger E3 ligases: These E3 ligases contain a RING finger domain, which directly interacts with both the E2 ubiquitin-conjugating enzyme and the substrate protein. They facilitate the transfer of ubiquitin from the E2 to the target protein by bringing them into close proximity.
2. Homologous to E6-AP C terminus (HECT) E3 ligases: These E3 ligases contain a HECT domain, which interacts with the E2 ubiquitin-conjugating enzyme and forms a thioester bond with ubiquitin before transferring it to the substrate protein.
3. RING-between-RING (RBR) E3 ligases: These E3 ligases contain both RING finger and HECT-like domains, which allow them to function similarly to both RING finger and HECT E3 ligases. They first form a thioester bond with ubiquitin using their RING1 domain before transferring it to the substrate protein via their RING2 domain.

Dysregulation of Ubiquitin-Protein Ligase Complexes has been implicated in various diseases, including cancer and neurodegenerative disorders. Understanding their mechanisms and functions can provide valuable insights into disease pathogenesis and potential therapeutic strategies.

A mutation is a permanent change in the DNA sequence of an organism's genome. Mutations can occur spontaneously or be caused by environmental factors such as exposure to radiation, chemicals, or viruses. They may have various effects on the organism, ranging from benign to harmful, depending on where they occur and whether they alter the function of essential proteins. In some cases, mutations can increase an individual's susceptibility to certain diseases or disorders, while in others, they may confer a survival advantage. Mutations are the driving force behind evolution, as they introduce new genetic variability into populations, which can then be acted upon by natural selection.

Transfer RNA (tRNA) for tryptophan (Trp) is a specific type of tRNA molecule that plays a crucial role in protein synthesis. In the process of translation, genetic information from messenger RNA (mRNA) is translated into a corresponding sequence of amino acids to form a protein.

Tryptophan is one of the twenty standard amino acids found in proteins. Each tRNA molecule carries a specific amino acid that corresponds to a particular codon (a sequence of three nucleotides) on the mRNA. The tRNA with tryptophan attached to it recognizes and binds to the mRNA codon UGG, which is the only codon that specifies tryptophan in the genetic code.

The tRNA molecule has a characteristic cloverleaf-like structure, composed of a stem region made up of base pairs and loop regions containing unpaired nucleotides. The anticodon loop contains the complementary sequence to the mRNA codon, allowing for specific recognition and binding. The other end of the tRNA molecule carries the amino acid, in this case tryptophan, which is attached via an ester linkage to a specific nucleotide called the 3'-end of the tRNA.

In summary, tRNA (Trp) is a key player in protein synthesis, responsible for delivering tryptophan to the ribosome during translation, where it can be incorporated into the growing polypeptide chain according to the genetic information encoded in mRNA.

MedlinePlus is not a medical term, but rather a consumer health website that provides high-quality, accurate, and reliable health information, written in easy-to-understand language. It is produced by the U.S. National Library of Medicine, the world's largest medical library, and is widely recognized as a trusted source of health information.

MedlinePlus offers information on various health topics, including conditions, diseases, tests, treatments, and wellness. It also provides access to drug information, medical dictionary, and encyclopedia, as well as links to clinical trials, medical news, and patient organizations. The website is available in both English and Spanish and can be accessed for free.

Arginine-tRNA ligase is an enzyme that plays a crucial role in protein synthesis. Its primary function is to join arginine, an essential amino acid, to its corresponding transfer RNA (tRNA) molecule. This enzyme catalyzes the formation of a peptide bond between the arginine and the tRNA during translation, the process by which genetic information encoded in messenger RNA (mRNA) is converted into a protein sequence.

The reaction catalyzed by arginine-tRNA ligase involves two main steps:

1. Activation of arginine: The enzyme binds to and activates an arginine molecule by attaching adenosine triphosphate (ATP) to it, forming an arginine-AMP intermediate.
2. Transfer of arginine to tRNA: The activated arginine is then transferred from the arginine-AMP complex onto the appropriate tRNA molecule, releasing AMP and forming an ester bond between the carboxyl group of arginine and the 3'-hydroxyl group of the ribose moiety in the tRNA.

The resulting arginine-tRNA complex is now ready to participate in protein synthesis, where it will contribute to the formation of a polypeptide chain under the direction of mRNA. The enzyme's role in ensuring accurate amino acid attachment to their corresponding tRNAs is essential for maintaining proper protein folding and function.

There are two main types of arginine-tRNA ligases, based on their structure and mechanism:

1. Class I arginine-tRNA ligase (also known as ArgRS): This enzyme contains an alpha/beta Rossmann-fold domain that binds ATP and a catalytic domain with a characteristic HIGH motif. It follows the standard two-step reaction mechanism for class I aminoacyl-tRNA synthetases.
2. Class II arginine-tRNA ligase (also known as ArgQ): This enzyme has an alpha/beta/alpha sandwich fold and a distinct catalytic mechanism compared to Class I enzymes. It follows the three-step reaction mechanism for class II aminoacyl-tRNA synthetases, which includes an intermediate step of adenylate formation before transferring arginine to tRNA.

Both types of arginine-tRNA ligases are found in various organisms, including bacteria and eukaryotes. In humans, the Class I enzyme is encoded by the RARS gene, while the Class II enzyme is encoded by the QARS gene. Dysfunction or mutations in these genes can lead to neurological disorders and other health issues due to impaired protein synthesis and folding.

I'm sorry for any confusion, but "Gross Domestic Product" (GDP) is an economic term, not a medical one. GDP is the total monetary or market value of all the finished goods and services produced within a country's borders in a specific time period. It serves as a comprehensive measure of a nation’s overall economic activity.

If you have any medical questions or terms you would like defined, I would be happy to help!

Argininosuccinic acid is a chemical compound that is an intermediate in the metabolic pathway for the synthesis of arginine, an essential amino acid. This process occurs in the urea cycle, which is responsible for removing excess nitrogen from the body in the form of urea.

In the urea cycle, citrulline reacts with aspartate to form argininosuccinic acid, which is then converted into arginine and fumarate by the enzyme argininosuccinate lyase. Arginine is a semi-essential amino acid that plays important roles in various physiological processes, including protein synthesis, nitric oxide production, and hormone secretion.

Argininosuccinic aciduria is a rare inherited metabolic disorder caused by a deficiency of the enzyme argininosuccinate lyase. This results in an accumulation of argininosuccinic acid in the blood and urine, leading to hyperammonemia (elevated levels of ammonia in the blood), neurological symptoms, and developmental delay. Treatment typically involves a low-protein diet, supplementation with arginine and citrulline, and nitrogen scavenging medications to reduce ammonia levels.

In enzymology, an arginine-tRNA ligase (EC 6.1.1.19) is an enzyme that catalyzes the chemical reaction ATP + L-arginine + ... arginine-tRNA synthetase, and arginine translase. This enzyme participates in arginine and proline metabolism and aminoacyl- ... L-arginine, and tRNA(Arg), whereas its 3 products are AMP, diphosphate, and L-arginyl-tRNA(Arg). This enzyme belongs to the ... The systematic name of this enzyme class is L-arginine:tRNAArg ligase (AMP-forming). Other names in common use include arginyl- ...
Overview of all the structural information available in the PDB for UniProt: P54136 (Human Arginine--tRNA ligase, cytoplasmic) ... McCune SA, Yu PL, Nance WE (1977). "A genetic study of erythrocyte arginine-tRNA synthetase activity in man". Acta Geneticae ... Arginyl-tRNA synthetase, cytoplasmic is an enzyme that in humans is encoded by the RARS gene. Aminoacyl-tRNA synthetases ... Arginyl-tRNA synthetase belongs to the class-I aminoacyl-tRNA synthetase family. Mutations in RARS cause hypomyelination. RARS ...
The beetle Caryedes brasiliensis is able to tolerate this however as it has the most highly discriminatory arginine-tRNA ligase ... presumably by virtue of highly discriminatory arginine-tRNA ligase, the enzyme responsible for the first step in the ... of dietary canavanine because their arginine-tRNA ligase has little, if any, discriminatory capacity. No one has examined ... experimentally the arginine-tRNA synthetase of these organisms. But comparative studies of the incorporation of radiolabeled L- ...
... and tRNA(Pro), whereas its 3 products are AMP, diphosphate, and L-prolyl-tRNA(Pro). This enzyme participates in arginine and ... This enzyme belongs to the family of ligases, to be specific those forming carbon-oxygen bonds in aminoacyl-tRNA and related ... In enzymology, a proline-tRNA ligase (EC 6.1.1.15) is an enzyme that catalyzes the chemical reaction ATP + L-proline + tRNAPro ... and prolinyl-tRNA ligase. Norton SJ (July 1964). "Purification and Properties of the Prolyl RNA Synthetase of Escherichia Coli ...
... histidine-tRNA ligase, and N-acetylmuramoyl-L-alanine amidase. These molecular signatures provide a novel and reliable means of ... These bacteria are oxidase-negative, and negative for arginine decarboxylase and Voges-Proskauer test. Seven conserved ...
... 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 ...
... cysteine-tRNA ligase EC 6.1.1.17: glutamate-tRNA ligase EC 6.1.1.18: glutamine-tRNA ligase EC 6.1.1.19: arginine-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. ... 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 ... 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 ...
... cysteine-tRNA ligase, coproporphyrinogen III oxidase, and PBP1A family penicillin-binding protein. These molecular signatures ... arginine-binding extracellular protein ArtP precursor, oxygen-independent coproporphyrinogen III oxidase, putative hydrolase ... MhqD, helix-turn-helix transcriptional regulator, tRNA preQ1(34)S-adenosylmethionine ribosyltransferase-isomerase QueA, DNA ...
... has been shown to interact with EEF1G. BC-LI-0186 Tavaborole Leucine-tRNA ligase GRCh38: Ensembl release ... It is found in the cytoplasm as part of a multisynthetase complex and interacts with the arginine tRNA synthetase through its C ... This gene encodes a cytosolic leucine-tRNA synthetase, a member of the class I aminoacyl-tRNA synthetase family. The encoded ... Lue SW, Kelley SO (April 2007). "A single residue in leucyl-tRNA synthetase affecting amino acid specificity and tRNA ...
... encoding enzyme tRNA pseudouridine synthase A PUS7L: encoding enzyme Pseudouridylate synthase 7 homolog-like protein PZP: ... encoding protein Protein arginine methyltransferase 8 PRR4: encoding protein Proline-rich protein 4 PTMS: encoding protein ... encoding enzyme E3 ubiquitin-protein ligase RNF34 SARNP: SAP domain-containing ribonucleoprotein Serpina3f: encoding protein ... "genetype trna"[Properties] OR "genetype scrna"[Properties] OR "genetype snrna"[Properties] OR "genetype snorna"[Properties]) ...
... glutamate-tRNA ligase, EC 1.2.1.70, glutamyl-tRNA reductase and EC 5.4.3.8 glutamate-1-semialdehyde 2,1-aminomutase EC 2.7.2.14 ... tRNA-guanosine34 preQ1 transglycosylase EC 2.4.2.30: NAD+ ADP-ribosyltransferase EC 2.4.2.31: NAD+-protein-arginine ADP- ... 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/ ...
MetG1 (Methionine-tRNA ligase) is required for elongation of protein synthesis and the initiation of all mRNA translation ... It is proline and arginine rich and isoleucine, asparagine, phenylalanine, and tyrosine poor. The predicted secondary structure ... tRNA ligase GeneCard. 8orf58 Gene(Protein Coding) Chromosome 8 Open Reading Frame 58. [5]. v t e (Articles with short ... through initiator tRNA(fMet) aminoacylation. An important paralog of this gene is ENSG00000248235. Orthologs of the human gene ...
An aminoacyl-tRNA synthetase (aaRS or ARS), also called tRNA-ligase, is an enzyme that attaches the appropriate amino acid onto ... "Backbone Brackets and Arginine Tweezers delineate Class I and Class II aminoacyl tRNA synthetases". PLOS Computational Biology ... If the incorrect tRNA is added (aka. the tRNA is found to be improperly charged), the aminoacyl-tRNA bond is hydrolyzed. This ... tRNA + ATP → Aminoacyl-tRNA + AMP + PPi Some synthetases also mediate an editing reaction to ensure high fidelity of tRNA ...
... also known as arginine decarboxylase (ADC) BCAS2: Breast carcinoma amplified sequence 2 BCL10 (1p22) LRIF1: encoding protein ... E3 ubiquitin-protein ligase component n-recognin 4 UROD: uroporphyrinogen decarboxylase (the gene for porphyria cutanea tarda) ... Tryptophanyl-tRNA synthetase, mitochondrial WDR77 (1p13) YBX1 (1p34) ZCCHC17: zinc finger CCHC-type containing 17 ZFP69: ... Protein arginine methyltransferase 6 PRXL2B: encoding protein Peroxiredoxin like 2B PSRC1: Proline/serine-rich coiled-coil ...
In eukaryotic cells, these N-terminal residues are recognized and targeted by ubiquitin ligases, mediating ubiquitination ... such as arginine, lysine, leucine, phenylalanine, tyrosine, and tryptophan, have short half-lives of around 2-minutes and are ... destabilising residues are modified by the attachment of a Primary destabilising residue by the enzyme leucyl/phenylalanyl-tRNA ... but inefficient when it is bulky and charged such as arginine. Once the f-Met is removed, the second residue becomes the N- ...
... addition of an arginine moiety to acidic NH2 termini of proteins is required for their recognition by ubiquitin-protein ligase ... Balzi E, Choder M, Chen WN, Varshavsky A, Goffeau A (May 1990). "Cloning and functional analysis of the arginyl-tRNA-protein ... It has also been observed that a variety of physiological compounds and drugs are able to affect the incorporation of arginine ... Enzymes such as Aminopeptidase B and Carboxypeptidase B are able to remove arginine from a proteins N-terminus and from side ...
... p38 tRNA synthase, Pael-R, synaptotagmin XI, sp22 and parkin itself (see also ubiquitin ligase). Additionally, parkin contains ... crystallisation of parkin revealed a cationic pocket in RING0 formed by lysine and arginine residues Lys161, Arg163 and Lys211 ... "Structure and function of Parkin E3 ubiquitin ligase reveals aspects of RING and HECT ligases". Nature Communications. 4: 1982 ... Parkin is a 465-amino acid residue E3 ubiquitin ligase, a protein that in humans and mice is encoded by the PARK2 gene. Parkin ...
... ligase) HMGN1: encoding non-histone chromosomal protein HMG-14 HSPA13: encoding heat shock 70 kDa protein 13 ICOSLG: encoding ... encoding tRNA (guanine-N(7)-)-methyltransferase non-catalytic subunit WDR4 ZBTB21: encoding zinc finger and BTB domain- ... encoding enzyme protein arginine N-methyltransferase 2 PSMG1: encoding protein proteasome assembly chaperone 1 PTTG1IP: ... "genetype trna"[Properties] OR "genetype scrna"[Properties] OR "genetype snrna"[Properties] OR "genetype snorna"[Properties]) ...
... tRNA) Triacsin C Thyroid-stimulating hormone (TSH) Thyrotropin-releasing hormone (TRH) Thyroxine (T4) Tocopherol (Vitamin E) ... Arabinose Arginine Argonaute Ascomycin Ascorbic acid (vitamin C) Asparagine Aspartic acid Asymmetric dimethylarginine ATP ... Lactase Lactic acid Lactose Lanolin Lauric acid Lectin Leptin Leptomycin B Leucine Leukotriene Ligase Lignin Limonene Linalool ... Dextran Dextrin Dicer Dihydrotestosterone DNA DNA polymerase DNA ligase Dopamine Endonuclease Enzyme Ephedrine Epinephrine - ...
... arginine/serine-rich 14 SFRS16: encoding protein Splicing factor, arginine/serine-rich 16 SLC5A5: Solute carrier family 5 ( ... Gene map locus 19q13.2 FCGBP: Fc fragment of IgG binding protein SARS2: seryl-tRNA synthetase 2, mitochondrial. Gene map locus ... encoding enzyme Long-chain-fatty-acid-CoA ligase ANKRD24: encoding protein Ankyrin repeat domain-containing protein 24 ARMC6: ... "genetype trna"[Properties] OR "genetype scrna"[Properties] OR "genetype snrna"[Properties] OR "genetype snorna"[Properties]) ...
002884 arginyl-tRNA synthetase RARS2 NM_020320 arginyl-tRNA synthetase 2, mitochondrial SARS NM_006513 Homo sapiens seryl-tRNA ... arginine/serine-rich EIF1 aka SUI1 EIF1AD EIF1B EIF2A EIF2AK1 EIF2AK3 EIF2AK4 EIF2AK1 EIF2B2 EIF2B3 EIF2B4 EIF2S2 EIF3A EIF3B ... 021178 E3 ubiquitin-protein ligase. Modulates cyclin B levels and participates in the regulation of cell cycle progression ... 001261434 alanyl-tRNA synthetase domain containing 1 CARS NM_001751 cysteinyl-tRNA synthetase CARS2 NM_024537 cysteinyl-tRNA ...
... the phenylalanine-tRNA ligase beta-subunit, VARS, elongation factor Tu, the RNA polymerase beta-subunit, and the ribosomal ... arginine, phenylalanine, and tryptophan. Some strains of "Ca. K. muelleri" are incapable of making the amino acid, tryptophan. ... K. muelleri" lacks a full set of Aminoacyl tRNA synthetases; surprisingly, however, it possesses all of the genes necessary to ... The proteins used were the DNA polymerase III beta-subunit, initiation factor IF-2, leucyl-tRNA synthetase, ...
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 ... Protein arginine phosphatase EC 3.9.1.3: Phosphohistidine phosphatase EC 3.10.1.1: N-sulfoglucosamine sulfohydrolase EC 3.10. ... ligase EC 6.2.1.23: Dicarboxylate-CoA ligase EC 6.2.1.24: Phytanate-CoA ligase EC 6.2.1.25: Benzoate-CoA ligase EC 6.2.1.26: o- ...
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 ...
... tRNA ↽ − − ⇀ aminoacyl − tRNA + AMP {\displaystyle {\ce {{Aminoacyl-AMP}+ tRNA <=> {aminoacyl-tRNA}+ AMP}}} The combination of ... Okazaki fragments are covalently joined by DNA ligase to form a continuous strand. Then, to complete DNA replication, RNA ... In the first step of arginine biosynthesis in bacteria, glutamate is acetylated by transferring the acetyl group from acetyl- ... This reaction, called tRNA charging, is catalyzed by aminoacyl tRNA synthetase. A specific tRNA synthetase is responsible for ...
Ubiquitin ligase PLGLB2: Plasminogen-related protein B POLR1A: DNA-directed RNA polymerase I subunit RPA1 PREPL: Prolyl ... "genetype trna"[Properties] OR "genetype scrna"[Properties] OR "genetype snrna"[Properties] OR "genetype snorna"[Properties]) ... Protein arginine methyltransferase NDUFAF7, mitochondrial NRBP1: Nuclear receptor-binding protein 1 ODC1: Ornithine ... encoding protein Neuralized E3 ubiquitin protein ligase 3 NCL: Nucleolin NR4A2: nuclear receptor subfamily 4, group A, member 2 ...
Mitochondrial tRNA genes have different sequences from the nuclear tRNAs, but lookalikes of mitochondrial tRNAs have been found ... In higher plants, it was thought that CGG encoded for tryptophan and not arginine; however, the codon in the processed RNA was ... 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 ...
Narayanan N, Wang Z, Li L, Yang Y (2017). "Arginine methylation of USP9X promotes its interaction with TDRD3 and its anti- ... eIF2-GTP-tRNA(i)(Met))-deficient preinitiation complexes are core constituents of mammalian stress granules". Molecular Biology ... "Pivotal role of RNA-binding E3 ubiquitin ligase MEX3C in RIG-I-mediated antiviral innate immunity". Proceedings of the National ... Tsai WC, Reineke LC, Jain A, Jung SY, Lloyd RE (November 2017). "Histone arginine demethylase JMJD6 is linked to stress granule ...
... site contains an aminoacyl-tRNA (a tRNA esterified to an amino acid on the 3' end). The P (peptidyl) site contains a tRNA ... Mms1p and Rtt101p are found to bind together and Rtt101p is believed to recruit a ubiquitin E3 ligase complex, allowing for the ... lysine and arginine). All ribosomal proteins (including the specific sequences that bind to rRNA) have been identified. These ... In the SSU, the mRNA interacts with the anticodons of the tRNA. In the LSU, the amino acid acceptor stem of the tRNA interacts ...
... 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 ... arginine decarboxylase EC 4.1.1.20: diaminopimelate decarboxylase EC 4.1.1.21: phosphoribosylaminoimidazole carboxylase EC 4.1. ... tRNA 4-demethylwyosine synthase (AdoMet-dependent) * EC 4.1.3.45: 3-hydroxybenzoate synthase * EC 4.1.3.46: (R)-citramalyl-CoA ...
In enzymology, an arginine-tRNA ligase (EC 6.1.1.19) is an enzyme that catalyzes the chemical reaction ATP + L-arginine + ... arginine-tRNA synthetase, and arginine translase. This enzyme participates in arginine and proline metabolism and aminoacyl- ... L-arginine, and tRNA(Arg), whereas its 3 products are AMP, diphosphate, and L-arginyl-tRNA(Arg). This enzyme belongs to the ... The systematic name of this enzyme class is L-arginine:tRNAArg ligase (AMP-forming). Other names in common use include arginyl- ...
Learn about Arginine-tRNA Ligase at online-medical-dictionary.org ... Arg tRNA Ligase. Arg-tRNA Ligase. Arginine tRNA Ligase. Arginyl ... Arginyl tRNA Synthetase. Arginyl-tRNA Synthetase. L-Arginine:tRNA(Arg)ligase (AMP-forming). Ligase, Arg-tRNA. Ligase, Arginine- ... An enzyme that activates arginine with its specific transfer RNA. EC 6.1.1.19. ... Arginine-tRNA Ligase. Synonyms. ...
Arginine--tRNA ligase (ArgS). Q99W05. 1.87 ↓. 1.80 ↓. 6. Transketolase (Tkt). P99161. 1.67 ↓. ... Glutamate----tRNA ligase (GltX). P99170. 1.74 ↓. 1.72 ↓. 2. 1-pyrroline-5-carboxylate dehydrogenase (RocA). P99076. 1.96 ↓. ... Succinate--CoA ligase (ADP-forming) subunit α (SucD). P99070. 1.55 ↓. 3. Putative peptidyl-prolyl cis-trans isomerase (PpiB). ... Formate--tetrahydrofolate ligase (FHS). Q7A535. 3.41 ↓. 2.75 ↓. 18. Phosphoenolpyruvate-protein phosphotransferase (PtsI). ...
The RARS2 gene provides instructions for making an enzyme called mitochondrial arginyl-tRNA synthetase. Learn about this gene ... arginine-tRNA ligase. *arginyl-tRNA synthetase 2, mitochondrial precursor. *arginyl-tRNA synthetase-like ... Specifically, this enzyme links the amino acid arginine to the tRNA molecule, which then incorporates it into new proteins in ... Mitochondrial arginyl-tRNA synthetase interacts with a molecule called transfer RNA (tRNA). This molecule, which is a chemical ...
arginine-tRNA ligase activity GO:0004814 * adipate-CoA ligase activity GO:0034796 ...
arginine-tRNA ligase activity. IEP. Enrichment. MF. GO:0005215. transporter activity. IEP. Enrichment. ... acid-amino acid ligase activity. IEP. Enrichment. MF. GO:0016886. ligase activity, forming phosphoric ester bonds. IEP. ... ligase activity, forming carbon-sulfur bonds. None. Extended. BP. GO:0034641. cellular nitrogen compound metabolic process. ... D-alanine-D-alanine ligase activity. IEP. Enrichment. MF. GO:0008759. UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine ...
arginine-tRNA ligase activity. IEP. Enrichment. CC. GO:0005839. proteasome core complex. IEP. Enrichment. ... ubiquitin-like protein ligase binding. None. Extended. BP. GO:0051603. proteolysis involved in cellular protein catabolic ...
aminoacyl-tRNA ligase activity. IEP. Enrichment. MF. GO:0004814. arginine-tRNA ligase activity. IEP. Enrichment. ...
Arginine-tRNA Ligase Medicine & Life Sciences 100% * Complementary DNA Chemical Compounds 36% ... Human cytoplasmic arginyl-tRNA synthetase (ArgRS) is a component of a macromolecular complex consisting of at least nine tRNA ... Zheng, Y. G., Wei, H., Ling, C., Xu, M. G., & Wang, E. D. (2006). Two forms of human cytoplasmic arginyl-tRNA synthetase ... Zheng, YG, Wei, H, Ling, C, Xu, MG & Wang, ED 2006, Two forms of human cytoplasmic arginyl-tRNA synthetase produced from two ...
Arginyl-tRNA synthetase(arginine--tRNA ligase) (ARGRS).... 0.04. OrthoFinder. AAL20825. STM1909, argS. arginine tRNA synthetase ... Arginine--tRNA ligase [Ensembl]. tRNA synthetases class.... 0.03. OrthoFinder. CBI66803. argS, HPB8_1246. arginyl-tRNA ... Description : Arginyl-tRNA synthetase (Arginine--tRNA ligase) (ArgRS) [Ensembl]. Arginyl tRNA synthetase N terminal domain, ... arginyl-tRNA synthetase [Ensembl]. Arginyl tRNA.... 0.04. OrthoFinder. AKI50491. argS, L2625_02681. arginyl-tRNA synthetase [ ...
F:nucleotide binding, aminoacyl-tRNA ligase activity, arginine-tRNA ligase activity, ATP binding;P:embryonic development ending ... arginyl-tRNA synthetase, putative / arginine--tRNA ligase, putative. C.G.. S.X.. Please select. ... The process of coupling arginine to arginyl-tRNA, catalyzed by arginyl-tRNA synthetase. In tRNA aminoacylation, the amino acid ... Arginyl-tRNA synthetase, class Ic family protein. 2e-20. At4g26300. emb1027 (embryo defective 1027). S.X.. H.G.. Please select ...
Arginine-tRNA Ligase Medicine & Life Sciences 100% * Canavanine Medicine & Life Sciences 87% ... Arginyl-tRNA synthetase (ArgRS) is a tRNA-binding protein that catalyzes the esterification of l-arginine to its cognate tRNA. ... N2 - Arginyl-tRNA synthetase (ArgRS) is a tRNA-binding protein that catalyzes the esterification of l-arginine to its cognate ... AB - Arginyl-tRNA synthetase (ArgRS) is a tRNA-binding protein that catalyzes the esterification of l-arginine to its cognate ...
Probable arginine--tRNA ligase, mitochondrial. RARS2. 6q16.1. Q5T160 details. Carnosine synthase 1. CARNS1. 11q13.2. A5YM72 ... 3. Arginine--tRNA ligase, cytoplasmic. General function:. Involved in nucleotide binding. Specific function:. Forms part of a ... L-Arginine. Description. Arginine or l-arginine, abbreviated Arg or R, is an essential amino acid that is physiologically ... Protein-arginine deiminase type-4. PADI4. 1p36.13. Q9UM07 details. Protein-arginine deiminase type-3. PADI3. 1p36.13. Q9ULW8 ...
tRNA ligase. Fumaric acid. L-Aspartic acid. Ornithine. L-Arginine. Citrulline. Citrulline. Ornithine. ATP. AMP. PP. i. ... D-Arginine and. D-Ornithine. Metabolism. D-Arginine and. D-Ornithine. Metabolism. Pyridoxal. 5-phosphate. FAD. Heme. Flavin. ... tRNA(Arg). L-Arginyl-. tRNA(Arg). tRNA(Pro). L-Prolyl-. tRNA(Pro). Citric Acid. Cycle. Alanine. Metabolism. ... arginine--tRNA. ligase,. mitochondrial. Glycine. amidinotransferase,. mitochondrial. Guanidinoacetate. N-. methyltransferase. ...
arginine--tRNA. ligase,. mitochondrial. Glycine. amidinotransferase,. mitochondrial. Guanidinoacetate. N-. methyltransferase. ... D-Arginine and. D-Ornithine. Metabolism. D-Arginine and. D-Ornithine. Metabolism. Urea Cycle. Intracellular Space. ... L-Arginine. Ornithine. Citrulline. Citrulline. ATP. AMP. PP. i. Argininosuccinic acid. ATP. NH. 3. CO. 2. H. 2. O. ADP. ... tRNA(Pro). L-Prolyl-. tRNA(Pro). tRNA(Arg). L-Arginyl-. tRNA(Arg). Citric Acid. Cycle. Alanine. Metabolism. ...
tRNA ligase. Fumaric acid. L-Aspartic acid. Ornithine. L-Arginine. Citrulline. Citrulline. Ornithine. ATP. AMP. PP. i. ... D-Arginine and. D-Ornithine. Metabolism. D-Arginine and. D-Ornithine. Metabolism. Pyridoxal. 5-phosphate. FAD. Heme. Flavin. ... tRNA(Arg). L-Arginyl-. tRNA(Arg). tRNA(Pro). L-Prolyl-. tRNA(Pro). Citric Acid. Cycle. Alanine. Metabolism. ... arginine--tRNA. ligase,. mitochondrial. Glycine. amidinotransferase,. mitochondrial. Guanidinoacetate. N-. methyltransferase. ...
alanine--tRNA ligase amine oxidase (flavin-containing) apoptosis inhibitor arginine--tRNA ligase ...
Aminoacyl-tRNA Synthetase Multienzyme Complex. *Extracellular Exosome. Molecular Function. *TRNA Binding. *Arginine-tRNA Ligase ...
... and asparagine-tRNA ligase (6.1.1.22) were also present with 3.2 and 9.2% of abundance, respectively. Among the total of genes ... The genes involved in the cysteine metabolic pathway (1.3.11.20, 4.2.1.22) account for 15% while for arginine and proline ... Glutamyl-tRNA reductase (1.2.1.70), encoded by another enriched gene at T1, makes up the first part of the metabolic pathway ... In addition, 1 gene encoding a ligase from the metabolism of lipoic acid was also evidenced. Thiamine and lipoic acid are ...
... and tRNA) were removed by aligning clean reads and cluster reads with the Rfam database [44]. Because whole genome sequencing ... E3 ubiquitin-protein ligase SDIR1), and Sugarcane_Unigene_BMK.62668 (MLO-like protein 13) were shared between continuously ... serine/arginine repetitive matrix protein 2) were shared between continuously differentially expressed predicted target genes ... tRNAs, snoRNAs, and snRNA (except for miRNAs), the remaining sequences were aligned with the reference sequence of sugarcane to ...
Patent 6255090: Plant aminoacyl-tRNA synthetase. (CHEMISTRY: MOLECULAR BIOLOGY AND MICROBIOLOGY : ENZYME (E.G., LIGASES (6. ), ... Patent 6255086: Carbamoyl-phosphate synthetase gene of coryneform bacteria and method for producing L-arginine. (CHEMISTRY: ... CHEMISTRY: MOLECULAR BIOLOGY AND MICROBIOLOGY : ENZYME (E.G., LIGASES (6. ), ETC.), PROENZYME; COMPOSITIONS THEREOF; PROCESS ... CHEMISTRY: MOLECULAR BIOLOGY AND MICROBIOLOGY : ENZYME (E.G., LIGASES (6. ), ETC.), PROENZYME; COMPOSITIONS THEREOF; PROCESS ...
Arginine-tRNA-protein transferase 1; P, phosphorylation site; Immunoglobulin-like domains (white bars); Fibronectin-like ... T-CAP interacts with the E3-ligase Mdm2 (Tian et al., 2006). Titin M-band domains A168-170 interact with MuRF-1 and 2, E3 ... ligases, which have been shown to bind to several muscle proteins including troponin I, troponin T, nebulin, and telethonin, ...
peptidyl-arginine hydroxylation to peptidyl-4-hydroxy-L-arginine GO:0018102 * enzyme active site formation via O4\-phospho-L ... conversion of aspartyl-tRNA to asparaginyl-tRNA GO:0043688 * peptidyl-aspartic acid reduction to form L-aspartyl aldehyde ... trans-methoxy-C60-meroacyl-AMP ligase activity GO:0103061 * galactoside O-acetyltransferase activity ...
Methionyl-tRNA formyltransferase. 95.74%. PM0084036. 56. A0A6M2Y0Y4. Tyrosine--tRNA ligase. 95.75%. PM0084046. ... Arginine deiminase. 95.30%. PM0083641. 26. A0A6M2Y013. DNA ligase. 95.30%. PM0083537. 27. A0A0C5H0S4. Macrolide-lincosamide- ...
... with GTP and methionyl-initiator tRNA (Met-tRNAi) [42]. The TC binds to the 40S ribosomal subunit to form the pre-initiation ... pegylated arginine deiminase (ADI-PEG20), a modified enzyme which can be administered to degrade arginine and thus activate ... ATF4 degradation relies on a phosphorylation-dependent interaction with the SCFβTrCPUbiquitin ligase. Mol Cell Biol. 2001;21(6 ... histidyl-tRNA synthetase (HisRS) domain and kinase domains. Amino acid depletion causes an increase in levels of uncharged tRNA ...
Identify tRNA Mutants Subject to Alternative RNA Processing - Shape 0. Investigation of Alternative Human tRNA Structures - ... Codon riboswitch [arginine]. Class I ligase. MedLoop resurrected. Un-stable. M-stable ...
Depending on the organism and availability, mt-tRNAVal or mt-tRNAPhe are incorporated, most likely due to their genomic ... and either 0.398 mM L-arginine and 0.798 mM L-lysine, or 0.398 mM 13C6,15N4-L-arginine and 0.798 mM 13C6,15N2-L-lysine. Cell ... The resulting cDNA was subjected to a 3′ ligation with adaptor 2 using T4 ligase. The single-stranded cDNA product was then PCR ... 9b). Most particles (~85%) lack mL40, mL46, mL48 and present a poorly defined structural mt-tRNA, similar to the consensus map ...
1) Modified DNA ligase. (2) A heated alkaline solution. (3) The same enzyme that cleave the donor DNA. (4) The different enzyme ... 4) T-RNA. 97. Syntonemal complex helps in:. (1) Gamete formation. (2) Recombination during cell division. (3) Production of ... 2) Tryptophaii (4) Arginine. 96. Where is the enzyme that catalyzes peptide bonding located?. (1) Largersub-unitofthe ribosome ...
Shu K, Yang W. E3 Ubiquitin Ligases: Ubiquitous Actors in Plant Development and Abiotic Stress Responses. Plant and Cell ... Serine/arginine-rich (SR): delays flowering time [8], Sugar transporter: acts downstream of FLT during the floral transition [ ... tRNAs) and ribosomal RNAs (rRNAs). Fifth, remaining transcript sequences were then inputted into CREMA (available at www.github ... E3 ubiquitin-protein ligase ORTHRUS 2 (ORTH2:Spo05660), Casein kinase II subunit beta-3 (CKB3:Spo06583), PHYTOCHROME-DEPENDENT ...
  • Other names in common use include arginyl-tRNA synthetase, arginyl-transfer ribonucleate synthetase, arginyl-transfer RNA synthetase, arginyl transfer ribonucleic acid synthetase, arginine-tRNA synthetase, and arginine translase. (wikipedia.org)
  • It contains a conserved domain at the N terminus called arginyl tRNA synthetase N terminal domain or additional domain 1 (Add-1). (wikipedia.org)
  • The RARS2 gene provides instructions for making an enzyme called mitochondrial arginyl-tRNA synthetase. (medlineplus.gov)
  • Mitochondrial arginyl-tRNA synthetase interacts with a molecule called transfer RNA (tRNA). (medlineplus.gov)
  • Mitochondrial arginyl-tRNA synthetase is one of several enzymes that link amino acids to tRNA. (medlineplus.gov)
  • The RARS2 gene mutations that cause pontocerebellar hypoplasia significantly reduce or eliminate the function of mitochondrial arginyl-tRNA synthetase. (medlineplus.gov)
  • Human cytoplasmic arginyl-tRNA synthetase (ArgRS) is a component of a macromolecular complex consisting of at least nine tRNA synthetases and three auxiliary proteins. (elsevierpure.com)
  • Arginyl-tRNA synthetase (Arginine--tRNA ligase) (ArgRS) [Ensembl]. (ntu.edu.sg)
  • Arginyl tRNA synthetase N terminal domain, tRNA synthetases class I (R), DALR anticodon binding domain [Interproscan]. (ntu.edu.sg)
  • Arginyl-tRNA synthetase (ArgRS) is a tRNA-binding protein that catalyzes the esterification of l-arginine to its cognate tRNA. (korea.ac.kr)
  • Here, we determined the crystal structures of the apo, l-arginine-complexed, and l-canavanine-complexed forms of the cytoplasmic free isoform of human ArgRS (hArgRS). (korea.ac.kr)
  • In enzymology, an arginine-tRNA ligase (EC 6.1.1.19) is an enzyme that catalyzes the chemical reaction ATP + L-arginine + tRNAArg ⇌ {\displaystyle \rightleftharpoons } AMP + diphosphate + L-arginyl-tRNAArg The 3 substrates of this enzyme are ATP, L-arginine, and tRNA(Arg), whereas its 3 products are AMP, diphosphate, and L-arginyl-tRNA(Arg). (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-arginine:tRNAArg ligase (AMP-forming). (wikipedia.org)
  • This enzyme participates in arginine and proline metabolism and aminoacyl-trna biosynthesis. (wikipedia.org)
  • An enzyme that activates arginine with its specific transfer RNA . (online-medical-dictionary.org)
  • Specifically, this enzyme links the amino acid arginine to the tRNA molecule, which then incorporates it into new proteins in mitochondria. (medlineplus.gov)
  • tRNA synthetases. (ntu.edu.sg)
  • Nonetheless,some of the putatively disrupted genes, such as isoleucyl andtyrosyl-tRNA synthetases (MG345 & MG455), DNA replication gene dnaA(MG469), and DNA polymerase HI, subunit alpha (MG261) are thought toperform essential functions. (fullblog.com.ar)
  • Arginine is a known inducer of mTOR (mammalian target of rapamycin) and is responsible for inducing protein synthesis through the mTOR pathway. (cannabisdatabase.ca)
  • Background: Serine/arginine-rich (SR) proteins regulate pre-mRNA splicing. (bvsalud.org)
  • Furthermore, instead of 5S rRNA, structurally similar mtDNA-encoded tRNAs occupy an equivalent region in the central protuberance of the mtLSU. (nature.com)
  • Arginine or l-arginine, abbreviated Arg or R, is an essential amino acid that is physiologically active in the L-form. (cannabisdatabase.ca)
  • In mammals, arginine is formally classified as a semi-essential or conditionally essential amino acid, depending on the developmental stage and health status of the individual. (cannabisdatabase.ca)
  • Arginine is a basic amino acid as its side chain contains a positively charged guanidinium group, which is highly polar, at the end of a hydrophobic¬†aliphatic¬†hydrocarbon chain. (cannabisdatabase.ca)
  • L-Arginine is an amino acid that has numerous functions in the body. (cannabisdatabase.ca)
  • To build new proteins, tRNA must collect different amino acids and then attach them to one another in the correct order. (medlineplus.gov)
  • the smaller subunit of a ribosome has a binding site for mRNA and the larger subunit has two binding sites for two tRNA . (brainkart.com)
  • Arginine methylation is required to understand crucial biochemical activities and biological functions, like gene regulation, signal transduction, etc. (bvsalud.org)
  • Depending on the organism and availability, mt-tRNA Val or mt-tRNA Phe are incorporated, most likely due to their genomic proximity to mt-rRNA genes and consequent near stoichiometric presence of their transcripts 4 , 8 . (nature.com)
  • 20841502 ). Catabolic disease states such as sepsis, injury, and cancer cause an increase in arginine utilization, which can exceed normal body production, leading to arginine depletion. (cannabisdatabase.ca)
  • Similar interactions were formed upon binding to l-canavanine or l-arginine, but the interaction between Tyr312 and the oxygen of the oxyguanidino group was a little bit different. (korea.ac.kr)
  • As a result, computational methods based on machine learning play an efficient role in predicting arginine methylation sites. (bvsalud.org)
  • RESULTS: In this research, a novel method called PRMxAI has been proposed to predict arginine methylation sites. (bvsalud.org)
  • CONCLUSIONS: The proposed PRMxAI shows the effectiveness of the features for predicting arginine methylation sites. (bvsalud.org)
  • Pre-term infants are unable to effectively synthesize arginine, making it nutritionally essential for them. (cannabisdatabase.ca)
  • Aminoacyl-tRNA synthetases catalyze the aminoacylation of tRNA by their cognate amino acid. (nih.gov)
  • Because of their central role in linking amino acids with nucleotide triplets contained in tRNAs, aminoacyl-tRNA synthetases are thought to be among the first proteins that appeared in evolution. (nih.gov)
  • 2008) Characterization of Human GTPBP3, a GTP-Binding Protein Involved in Mitochondrial tRNA Modification. (jenabioscience.com)
  • tRNA methyltransferase 2 homolog A [S. (gsea-msigdb.org)
  • protein_coding" "Cz03g05060.t1","No alias","Chromochloris zofingiensis","tRNA methyltransferase TRMD/TRM10-type domain [Interproscan]. (ntu.edu.sg)
  • protein_coding" "Cz08g16110.t1","No alias","Chromochloris zofingiensis","tRNA (1-methyladenosine) methyltransferase catalytic subunit Gcd14 [Interproscan]. (ntu.edu.sg)
  • The exquisite specificity of human protein arginine methyltransferase 7 (PRMT7) toward Arg-X-Arg sites. (ucla.edu)
  • Human Protein-l-isoaspartate O-Methyltransferase Domain-Containing Protein 1 (PCMTD1) Associates with Cullin-RING Ligase Proteins. (ucla.edu)
  • creatine from the protein building blocks (amino acids) glycine , arginine, and methionine. (nih.gov)
  • gene provides instructions for making an enzyme called glycine --tRNA ligase. (nih.gov)
  • Here, we synthesized the c9orf72 DPRs poly-glycine-arginine (poly-GR), poly-proline-arginine (poly-PR), poly-glycine-proline (poly-GP), poly-proline-alanine (poly-PA), and poly-glycine-alanine (poly-GA) using automated fast-flow peptide synthesis (AFPS) and achieved single-domain chemical synthesis of proteins with up to 200 amino acids. (bvsalud.org)
  • In enzymology, an arginine-tRNA ligase (EC 6.1.1.19) is an enzyme that catalyzes the chemical reaction ATP + L-arginine + tRNAArg ⇌ {\displaystyle \rightleftharpoons } AMP + diphosphate + L-arginyl-tRNAArg The 3 substrates of this enzyme are ATP, L-arginine, and tRNA(Arg), whereas its 3 products are AMP, diphosphate, and L-arginyl-tRNA(Arg). (wikipedia.org)
  • peptidyl-tRNA hydrolase, ribosome-attached [Ensembl]. (ntu.edu.sg)
  • This enzyme participates in arginine and proline metabolism and aminoacyl-trna biosynthesis. (wikipedia.org)
  • Guided by this finding, 4 novel genes (cynX, cynT, pyrB, and rhaB) for L-arginine biosynthesis were identified via reverse engineering. (bvsalud.org)
  • The results of the combined analysis showed that purine metabolism, arginine biosynthesis, and arachidonic acid metabolism were changed in patients with ARC. (bvsalud.org)
  • Human protein arginine methyltransferases (PRMTs) can be optimally active under nonphysiological conditions. (ucla.edu)
  • Ligase catalyzes the formation of covalent bonds between the Okazaki fragments. (notesforshs.com)
  • 2005) Effects of Mutagenesis in Switch I Region and Conserved Arginines of Escherichia coli MnmE Protein, A GTPase Involved in tRNA Modification. (jenabioscience.com)
  • protein_coding" "Cz06g09040.t1","No alias","Chromochloris zofingiensis","Tubulin-tyrosine ligase/Tubulin polyglutamylase [Interproscan]. (ntu.edu.sg)
  • Forms part of a macromolecular complex that catalyzes the attachment of specific amino acids to cognate tRNAs during protein synthesis (PubMed:25288775). (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)
  • We speculate that the occurrence of ARC may be related to the alteration of renal blood perfusion by LTB4R, ARG1, ALOX5, arginine and prostaglandins E2 through inflammatory response, as well as the effects of CA4, PFKFB2, PFKFB3, PRKACB, NMDAR, glutamate and cAMP on renal capillary wall permeability. (bvsalud.org)
  • An enzyme that activates arginine with its specific transfer RNA. (nih.gov)
  • This study revealed the molecular mechanism of gene transcription regulation by betaine and developed a superior L-arginine overproducer that does not require betaine. (bvsalud.org)
  • Here we report that Tel2 and Tti1 are targeted for degradation within mTORC1 by the SCFFbxo9 ubiquitin ligase to adjust mTOR signalling to growth factor availability. (cipsm.de)
  • This domain is about 140 residues long and it has been suggested that it is involved in tRNA recognition. (wikipedia.org)