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.
An order of strictly anaerobic, thermophilic archaea, in the kingdom EURYARCHAEOTA. Members exhibit heterotropic growth by sulfur respiration. There is a single family THERMOCOCCACEAE.
A genus of strictly anaerobic ultrathermophilic archaea, in the family THERMOCOCCACEAE, occurring in heated seawaters. They exhibit heterotrophic growth at an optimum temperature of 100 degrees C.
An enzyme that activates arginine with its specific transfer RNA. EC 6.1.1.19.
A procedure consisting of a sequence of algebraic formulas and/or logical steps to calculate or determine a given task.
Large HYALURONAN-containing proteoglycans found in articular cartilage (CARTILAGE, ARTICULAR). They form into aggregates that provide tissues with the capacity to resist high compressive and tensile forces.
A class of unsegmented helminths with fundamental bilateral symmetry and secondary triradiate symmetry of the oral and esophageal structures. Many species are parasites.
Proteins that are involved in the peptide chain termination reaction (PEPTIDE CHAIN TERMINATION, TRANSLATIONAL) on RIBOSOMES. They include codon-specific class-I release factors, which recognize stop signals (TERMINATOR CODON) in the MESSENGER RNA; and codon-nonspecific class-II release factors.
A species of gram-negative bacteria in the genus PSEUDOMONAS, containing multiple genomovars. It is distinguishable from other pseudomonad species by its ability to use MALTOSE and STARCH as sole carbon and energy sources. It can degrade ENVIRONMENTAL POLLUTANTS and has been used as a model organism to study denitrification.
A genus of gram-negative, aerobic, rod-shaped bacteria widely distributed in nature. Some species are pathogenic for humans, animals, and plants.
A species of gram-negative, aerobic, rod-shaped bacteria commonly isolated from clinical specimens (wound, burn, and urinary tract infections). It is also found widely distributed in soil and water. P. aeruginosa is a major agent of nosocomial infection.
The degree of 3-dimensional shape similarity between proteins. It can be an indication of distant AMINO ACID SEQUENCE HOMOLOGY and used for rational DRUG DESIGN.
Macromolecular molds for the synthesis of complementary macromolecules, as in DNA REPLICATION; GENETIC TRANSCRIPTION of DNA to RNA, and GENETIC TRANSLATION of RNA into POLYPEPTIDES.
The state of weariness following a period of exertion, mental or physical, characterized by a decreased capacity for work and reduced efficiency to respond to stimuli.
An enzyme that activates methionine with its specific transfer RNA. EC 6.1.1.10.
Databases containing information about PROTEINS such as AMINO ACID SEQUENCE; PROTEIN CONFORMATION; and other properties.
A process that includes the determination of AMINO ACID SEQUENCE of a protein (or peptide, oligopeptide or peptide fragment) and the information analysis of the sequence.
The procedures involved in combining separately developed modules, components, or subsystems so that they work together as a complete system. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
A loose confederation of computer communication networks around the world. The networks that make up the Internet are connected through several backbone networks. The Internet grew out of the US Government ARPAnet project and was designed to facilitate information exchange.
Family of the suborder HAPLORHINI (Anthropoidea) comprising bipedal primate MAMMALS. It includes modern man (HOMO SAPIENS) and the great apes: gorillas (GORILLA GORILLA), chimpanzees (PAN PANISCUS and PAN TROGLODYTES), and orangutans (PONGO PYGMAEUS).
An infraorder of PRIMATES comprised of the families CERCOPITHECIDAE (old world monkeys); HYLOBATIDAE (siamangs and GIBBONS); and HOMINIDAE (great apes and HUMANS). With the exception of humans, they all live exclusively in Africa and Asia.
An order of the class MAMMALS that consists of one family, TUPAIIDAE (tree shrews), 5 genera (one of which is TUPAIA), and 16 species. Their recent distribution is from India to the Philippines, southern China to Java, Borneo, Sumatra, Bali, and other islands in those regions.
The largest family of snakes, comprising five subfamilies: Colubrinae, Natricinae, Homalopsinae, Lycodontinae, and Xenodontinae. They show a great diversity of eating habits, some eating almost anything, others having a specialized diet. They can be oviparous, ovoviviparous, or viviparous. The majority of North American snakes are colubrines. Among the colubrids are king snakes, water moccasins, water snakes, and garter snakes. Some genera are poisonous. (Goin, Goin, and Zug, Introduction to Herpetology, 3d ed, pp321-29)
The relationships of groups of organisms as reflected by their genetic makeup.
Phylum in the domain Eukarya, comprised of animals either with fully developed backbones (VERTEBRATES), or those with notochords only during some developmental stage (CHORDATA, NONVERTEBRATE).
A group of cold-blooded, aquatic vertebrates having gills, fins, a cartilaginous or bony endoskeleton, and elongated bodies covered with scales.

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)

The SCOP classification for the Arginyl-tRNA synthetase (ArgRS), N-terminal additional domain superfamily including the families contained in it. Additional information provided includes InterPro annotation (if available), Functional annotation, and SUPERFAMILY links to genome assignments, alignments, domain combinations, taxonomic visualisation and hidden Markov model information.
SWISS-MODEL Template Library (SMTL) entry for 5b63.1. Crystal structures of E.coli arginyl-tRNA synthetase (ArgRS) in complex with substrate tRNA(Arg)
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Arginyl tRNA synthetase (ArgRS), a class I aminoacyl tRNA synthetase, is a monomer which aminoacylates the 2-OH of the nucleotide at the 3 of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. There are at least three subgroups of ArgRS. One type contains both characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. The second subtype lacks the KMSKS motif; however, it has a lysine N-terminal to the HIGH motif, which serves as the functional counterpart to the second lysine of the KMSKS motif. A third group, which is found primarily in archaea and a few bacteria, lacks both the KMSKS motif and the HIGH loop lysine [PUBMED:11106639].. ...
CAMCONTROL(8) BSD System Managers Manual CAMCONTROL(8) NAME camcontrol -- CAM control program SYNOPSIS camcontrol ,command, [device id] [generic args] [command args] camcontrol devlist [-v] camcontrol periphlist [device id] [-n dev_name] [-u unit_number] camcontrol tur [device id] [generic args] camcontrol inquiry [device id] [generic args] [-D] [-S] [-R] camcontrol start [device id] [generic args] camcontrol stop [device id] [generic args] camcontrol load [device id] [generic args] camcontrol eject [device id] [generic args] camcontrol rescan ,all , bus[:target:lun], camcontrol reset ,all , bus[:target:lun], camcontrol defects [device id] [generic args] ,-f format, [-P] [-G] camcontrol modepage [device id] [generic args] ,-m page , -l, [-P pgctl] [-b , -e] [-d] camcontrol cmd [device id] [generic args] ,-c cmd [args], [-i len fmt] [-o len fmt [args]] camcontrol debug [-I] [-P] [-T] [-S] [-X] [-c] ,all,off,bus[:target[:lun]], camcontrol tags [device id] [generic args] [-N tags] [-q] [-v] ...
This module implements {{listen}}. local mFileLink = require(Módulo:Link de arquivo) local mTableTools = require(Módulo:TableTools) local mSideBox = require(Módulo:Caixa lateral) local p = {} local hasMidi, hasMissing -- Trackers for categories function p.main(frame) local origArgs = frame:getParent().args local args = {} for k, v in pairs(origArgs) do v = v:match(^%s*(.-)%s*$) if v ~= then args[k] = v end end return p._main(args) end function p._main(args) -- Organise the arguments by number. local numArgs = {} do local origNumArgs = mTableTools.numData(args) origNumArgs[1] = origNumArgs.other -- Overwrite args.filename1 etc. with args.filename etc. origNumArgs = mTableTools.compressSparseArray(origNumArgs) for i, t in ipairs(origNumArgs) do -- Check if the files exist. local obj = (t.filename and mw.title.new(Media: .. t.filename) or t.arquivo and mw.title.new(Media: .. t.arquivo) or t.ficheiro and mw.title.new(Media: .. t.ficheiro)) if obj and obj.exists then ...
swig_c++.tcl # Provides a simple object oriented interface using # SWIGs low level interface. # proc new {objectType handle_r args} { # Creates a new SWIG object of the given type, # returning a handle in the variable handle_r. # # Also creates a procedure for the object and a trace on # the handle variable that deletes the object when the # handle variable is overwritten or unset upvar $handle_r handle # # Create the new object # eval set handle \[new_$objectType $args\] # # Set up the object procedure # proc $handle {cmd args} eval ${objectType}_\$cmd $handle \$args # # And the trace ... # uplevel trace variable $handle_r uw {deleteObject $objectType $handle} # # Return the handle so that new can be used as an argument to a procedure # return $handle } proc deleteObject {objectType handle name element op} { # # Check that the object handle has a reasonable form # if {![regexp {_[0-9a-f]*_(.+)_p} $handle]} { error deleteObject: not a valid object handle: $handle } # # Remove the ...
I got args halfway into my season and i only got to ride them five times or so, since i do not have a place in the mountains i feel like this may be just to muc
mikelove: trying out: alias rhelp=Rscript -e args ,- commandArgs(TRUE); help(args[2], package=args[3], help_type=\html\); Sys.sleep(5) --args (5 Aug ...
11:05:18] ,Darke, So far every file has been named by the primary class inside it, so Args.cc,h has a class Args { definition, etc. The problem is what to do with files that lack class? Ive got the holdover from exult common_types.h, now logically I should rename it to CommonTypes.hpp, just because its the same capitalisation as the other files. But it doesnt contain a CommonTypes class ...
File lib/spec/example/example_group_factory.rb, line 23 def create_shared_example_group(*args, &example_group_block) # :nodoc: ::Spec::Example::SharedExampleGroup.register(*args, &example_group_block) end ...
File lib/spec/example/shared_example_group.rb, line 49 def initialize(*args, &example_group_block) set_description(*args) @example_group_block = example_group_block end ...
Historically, PHP allows calling functions with fewer actual parameters than required by the function definition. These non-passed arguments lead to warning emission and continuation of function execution with uninitialized arguments. ...
I was so disappointed last night! First, I was shocked that there was no clear plan of action given to Raelyn by her doctor. Was she ever even tested for food allergies? Yes, I know her dx, but perhaps if she were tested she would know some of her definitive triggers. Everytime I saw her eat gluten and dairy I would cringe, knowing what was coming. Also, that chiropractor didnt tell her to start food challenges, he said she still needed to wait. (I know there is no cure, Im just saying...lets not blame the chiro here) the family and herself made an irresponsible choice and did not do a proper food challenge. As for Zeke, those food challenges were crazy! A food challenge should not consist of that much food. His mom was complaining about the few extra carrots he snuck in at the office, but at home gave him 4-5 tuna steaks. That is a bit excessive. I felt that these parents didnt have the proper guidance and were just winging it as best they could. They need the help of these blogs and ...
TSEN54-related pontocerebellar hypoplasia (PCH) includes three PCH types (PCH2, 4, and 5) that share characteristic neuroradiologic and neurologic findings. The three types (which differ mainly in life expectancy) were thought to be distinct entities before their molecular basis was known. Children with PCH2 usually succumb before age ten years, whereas those with PCH4 and 5 usually succumb as neonates. Children with PCH2 have generalized clonus, incoordination of sucking and swallowing, impaired motor and cognitive development with lack of voluntary motor development, central visual impairment, and an increased risk for rhabdomyolysis complicating severe infections. Epilepsy is present in approximately 50%. Neonates with PCH4 often have seizures, multiple joint contractures (arthrogryposis), generalized clonus, and central respiratory impairment. PCH5, which resembles PCH4, has been described in one family.
Information on Pontocerebellar hypoplasia type 3, which may include symptoms, causes, inheritance, treatments, orphan drugs, associated orgs, and other relevant data.
As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
ID SYR_LISW6 Reviewed; 556 AA. AC A0ALP7; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 28-NOV-2006, sequence version 1. DT 20-DEC-2017, entry version 72. DE RecName: Full=Arginine--tRNA ligase {ECO:0000255,HAMAP-Rule:MF_00123}; DE EC=6.1.1.19 {ECO:0000255,HAMAP-Rule:MF_00123}; DE AltName: Full=Arginyl-tRNA synthetase {ECO:0000255,HAMAP-Rule:MF_00123}; DE Short=ArgRS {ECO:0000255,HAMAP-Rule:MF_00123}; GN Name=argS {ECO:0000255,HAMAP-Rule:MF_00123}; GN OrderedLocusNames=lwe2511; OS Listeria welshimeri serovar 6b (strain ATCC 35897 / DSM 20650 / OS SLCC5334). OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=386043; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35897 / DSM 20650 / SLCC5334; RX PubMed=16936040; DOI=10.1128/JB.00758-06; RA Hain T., Steinweg C., Kuenne C.T., Billion A., Ghai R., RA Chatterjee S.S., Domann E., Kaerst U., Goesmann A., Bekel T., RA Bartels D., Kaiser O., Meyer F., Puehler A., Weisshaar B., Wehland ...
The intracellular distribution of various components of the protein translational machinery was visualized in mouse oligodendrocytes in culture using high resolution fluorescence in situ hybridization and immunofluorescence in conjunction with dual channel confocal laser scanning microscopy. Arginyl-tRNA synthetase, elongation factor 1a, ribosomal RNA, and myelin basic protein mRNA were all co-localized in granules in the processes, veins and membrane sheets of the cell. Colocalization was evaluated by dual channel cross correlation analysis to determine the correlation index (% colocalization) and correlation distance (granule radius), and by single granule ratiometric analysis to determine the distribution of the different components in individual granules. Most granules contained synthetase, elongation factor, ribosomal RNA and myelin basic protein mRNA. These results indicate that several different components of the protein synthetic machinery, including aminoacyl-tRNA synthetases, ...
The RARS2 gene provides instructions for making an enzyme called mitochondrial arginyl-tRNA synthetase. Learn about this gene and related health conditions.
Order TSEN2 ELISA Kits for many Reactivities. and more. Compare TSEN2 ELISA Kits and find the right product on antibodies-online.com.
src/Elasticsearch/Query/QueryBuilder.php public function addFilter(\Elastica\Query\AbstractQuery $filter) public function addPostFilter(\Elastica\Query\AbstractQuery $postFilter) ./src/Elasticsearch/Provider/Visibility/StrategyInterface.php public function elasticAddFilters(User $user, \Elastica\Query\BoolQuery $filter, Visibility $provider); ./clients/base/api/BulkApi.php public function bulkCall(ServiceBase $api, array $args) ./clients/base/api/CalendarEventsApi.php public function updateCalendarEvent(ServiceBase $api, array $args) public function deleteCalendarEvent(ServiceBase $api, array $args) public function updateRecurringCalendarEvent(SugarBean $bean, ServiceBase $api, array &$args) public function deleteRecordAndRecurrences(ServiceBase $api, array $args) public function deleteRecurrences(SugarBean $bean) protected function initializeArgs(array $args, SugarBean $bean = null) protected function adjustStartDate(array &$args) protected function filterOutRecurrenceFields(array $args) ...
Complete information for TSEN2 gene (Protein Coding), TRNA Splicing Endonuclease Subunit 2, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Is there a way to have a metaclass similar to our ClasscallMetaclass at all, in Python3?? I just tested, having class Classcall(type): def __call__(cls, *args, **opts): try: classcall = cls.__classcall__ except AttributeError: return type.__call__(cls, *args, **opts) return classcall(cls, *args, **opts) class MyUniqueRepresentation: __metaclass__ = Classcall @staticmethod def __classcall__(cls, *args, **opts): out = super(cls,cls).__new__(cls, *args, **opts) print(classcall got,type(out), cls) cls.__init__(out,*args,**opts) out._reduction = (type(out), args, opts) return out Loading the above into python2, I get ,,, class Foo(MyUniqueRepresentation): ... def __init__(self, a,b): ... self.a = a ... self.b = b ... ,,, A = Foo(A,B) (classcall got, ,class __main__.Foo,, ,class __main__.Foo,) ,,, A._reduction (,class __main__.Foo,, (A, B), {}) But doing the same in python3, it gives ,,, class Foo(MyUniqueRepresentation): ... def __init__(self, a,b): ... self.a = a ... self.b = b ... ...
p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.,/p> ,p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.,/p> ,p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).,/p> ,p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x,sup>64,/sup> + x,sup>4,/sup> + x,sup>3,/sup> + x + 1. The algorithm is described in the ISO 3309 standard. ,/p> ,p class=publication>Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.,br /> ,strong>Cyclic redundancy and other checksums,/strong>,br /> ,a href=http://www.nrbook.com/b/bookcpdf.php>Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993),/a>),/p> Checksum:i ...
in obj) { if (obj.hasOwnProperty(key)) { obj[key]; } } --‐(void)dictEnumerator:(id)args { ENSURE_SINGLE_ARG(args, NSDictionary); for (id i in [args keyEnumerator]) { args[i ...
Large search returns make our pages slow to load. Therefore, some functionality has been disabled until you refine your search to bring the number of returned assay results under TBD ...
Large search returns make our pages slow to load. Therefore, some functionality has been disabled until you refine your search to bring the number of returned assay results under TBD ...
usr/bin/env desres-exec #{ # exec desres-cleanenv -c --user-env \ # -m Python/2.7.1-06A/bin \ # -m destro/0.6.2/lib-python \ # -m scipy/0.12.0-01/lib-python \ # -m destiny/0.4.47-3/lib-python \ # -m molpro/2012.1.12-desres-3-02/serial/bin \ # -m psi4/4.0b5-desres-2-01/bin \ # -- python -u $0 [email protected] #} import sys sys.path.append(/u/en/donchev/pyprogs) sys.path.append(/u/en/donchev/pyprogs/chemsys) sys.path.append(/d/en/ffdevel-0/bin/pyqmdata) sys.path.append(/u/en/donchev/playground/qmdata6/) import math, numpy import subprocess import time import copy import string import units import prepmpr import pth4 as pth import frame import class_qmjob import class_scannmer class MultiScanNmer(object): def __init__(self, finput, opts, molpro_args=[]): self.molpro_args = molpro_args self.opts = opts #self.basopt = self.opts.basopt #self.basene = self.opts.basene #self.basesl = self.opts.basesl self.ncores = self.opts.ncores self.verbose = self.opts.verbose self.rerun = self.opts.rerun self.pinput = ...
from genshi.core import Markup from trac.wiki.macros import WikiMacroBase class HelloWorldMacro(WikiMacroBase): Simple HelloWorld macro. Note that the name of the class is meaningful: - it must end with Macro - what comes before Macro ends up being the macro name The documentation of the class (i.e. what youre reading) will become the documentation of the macro, as shown by the !MacroList macro (usually used in the WikiMacros page). revision = $Rev$ url = $URL$ def expand_macro(self, formatter, name, text, args): Return some output that will be displayed in the Wiki content. `name` is the actual name of the macro (no surprise, here itll be `HelloWorld`), `text` is the text enclosed in parenthesis at the call of the macro. Note that if there are no parenthesis (like in, e.g. [[HelloWorld]]), then `text` is `None`. `args` are the arguments passed when HelloWorld is called using a `#!HelloWorld` code block. return Hello World, text = %s, args = %s % \ ...
from genshi.core import Markup from trac.wiki.macros import WikiMacroBase class HelloWorldMacro(WikiMacroBase): Simple HelloWorld macro. Note that the name of the class is meaningful: - it must end with Macro - what comes before Macro ends up being the macro name The documentation of the class (i.e. what youre reading) will become the documentation of the macro, as shown by the !MacroList macro (usually used in the WikiMacros page). revision = $Rev$ url = $URL$ def expand_macro(self, formatter, name, text, args): Return some output that will be displayed in the Wiki content. `name` is the actual name of the macro (no surprise, here itll be `HelloWorld`), `text` is the text enclosed in parenthesis at the call of the macro. Note that if there are no parenthesis (like in, e.g. [[HelloWorld]]), then `text` is `None`. `args` are the arguments passed when HelloWorld is called using a `#!HelloWorld` code block. return Hello World, text = %s, args = %s % \ ...
the closed group correspond to the closed tickets closed = closed # .order: sequence number in the progress bar closed.order = 0 # .query_args: optional parameters for the corresponding # query. In this example, the changes from the # default are two additional columns (created and # modified), and sorting is done on created. closed.query_args = group=resolution,order=time,col=id,col=summary,col=owner,col=type,col=priority,col=component,col=severity,col=time,col=changetime # .overall_completion: indicates groups that count for overall # completion percentage closed.overall_completion = true new = new new.order = 1 new.css_class = new new.label = new # Note: one catch-all group for other statuses is allowed active = * active.order = 2 # .css_class: CSS class for this interval active.css_class = open # .label: displayed label for this group active.label = in progress ...
O esperado é algo assim? [09-Nov-2017 04:51:35 UTC] hook http_request_args: 1510203095 [09-Nov-2017 04:51:46 UTC] hook… 2 months ago. ...
Looking for online definition of pontocerebellar hypoplasia type 2A in the Medical Dictionary? pontocerebellar hypoplasia type 2A explanation free. What is pontocerebellar hypoplasia type 2A? Meaning of pontocerebellar hypoplasia type 2A medical term. What does pontocerebellar hypoplasia type 2A mean?
Pontocerebellar hypoplasia type 1 (PCH1) is characterized by cerebellar and anterior horn motor neuron degeneration and loss, signs of spinal muscular atrophy plus. Patients manifest severe perinatal weakness, hypotonia, and respiratory insufficiency, causing death frequently before the age of 1 yea …
Rajab et al. (2003) reported the clinical features of three affected children born to consanguineous Omani parents with a novel form of pontocerebellar hypoplasia with microcephaly, and conducted genetic studies to identify the genetic locus of this disorder. The first case was a 12-year old boy, born with occipito-frontal circumference (OFC), length, and weight in the 10th percentile. During infancy, he was floppy, not interested in his surroundings, had motor developmental delay as he had no head control, did not roll over or sit, and had a history of recurrent respiratory tract infection. By the age of eight months, his anterior fontanelles were closed and fundoscopic examination revealed pale optic discs. He developed generalized tonic clonic seizures after an episode of febrile convulsions at one year of age, and was on sodium valoproate. Clinically, he had microcephaly (OFC was 45 cm, increased by 5 cm only since he was 18 months), was below the third percentile in weight and height, ...
Minuscule event, far-reaching consequences. During the time of the Ottoman Empire, one person experienced a single mutation in a certain gene. Centuries later, children descended from that unknown individual still suffer the consequences: a deadly form of degeneration of the brain that is called pontocerebellar hypoplasia (PCH).. The mutation was discovered by Yale genetics, neurosurgery, and neurobiology professor Murat Günel 94Grd, working with researchers in Turkey and several other countries. PCH is a collection of disorders caused by various genetic mishaps. But this mutation and the surrounding genomic areas were identical in the affected patients, who came from four families with a history of intermarriage. The researchers deduced, from the nature of the mutation, that all of the children share a common ancestor who lived roughly 16 generations ago. The findings appeared in the April 24 issue of Cell.. Specific mutations can tell us a lot about normal function; this one, the researchers ...
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In the project root set the following alias $: alias render=mvn exec:java -Dexec.mainClass=Main # Using OPSIN to load porphyrin and generate a PDF $: render -Dexec.args=-name porphyrin -pdf # Highlight one of the pyrrole in porphyrin $: render -Dexec.args=-name porphyrin -pdf -sma n1cccc1 # Show atom numbers $: render -Dexec.args=-name porphyrin -pdf -atom-numbers # Show CIP labels $: render -Dexec.args=-name (2R)-butan-2-ol -pdf -cip-labels # Generate a PDF / SVG for ethanol SMILES $: render -Dexec.args=-smi CCO -pdf ethanol.pdf -svg ethanol.svg # Load a molfile $: render -Dexec.args=-mol ChEBI_6701.mol -pdf chebi-6701.pdf ...
In the project root set the following alias $: alias render=mvn exec:java -Dexec.mainClass=Main # Using OPSIN to load porphyrin and generate a PDF $: render -Dexec.args=-name porphyrin -pdf # Highlight one of the pyrrole in porphyrin $: render -Dexec.args=-name porphyrin -pdf -sma n1cccc1 # Show atom numbers $: render -Dexec.args=-name porphyrin -pdf -atom-numbers # Show CIP labels $: render -Dexec.args=-name (2R)-butan-2-ol -pdf -cip-labels # Generate a PDF / SVG for ethanol SMILES $: render -Dexec.args=-smi CCO -pdf ethanol.pdf -svg ethanol.svg # Load a molfile $: render -Dexec.args=-mol ChEBI_6701.mol -pdf chebi-6701.pdf ...
p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.,/p> ,p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.,/p> ,p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).,/p> ,p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x,sup>64,/sup> + x,sup>4,/sup> + x,sup>3,/sup> + x + 1. The algorithm is described in the ISO 3309 standard. ,/p> ,p class=publication>Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.,br /> ,strong>Cyclic redundancy and other checksums,/strong>,br /> ,a href=http://www.nrbook.com/b/bookcpdf.php>Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993),/a>),/p> Checksum:i ...
This graph shows the total number of publications written about Canavanine by people in this website by year, and whether Canavanine was a major or minor topic of these publications ...
Cobbler CHANGELOG (all entries [email protected] unless noted otherwise) * Thu Nov 15 2007 - 0.7.0 - Testing branch - Fix bug related to ,,inherit,, and kickstart args - Make CLI functions modular and use optparse - Quote wget args to avoid creating stray files on target system - Support Xen FV as virt type (requires F8+) - ... * Wed Nov 14 2007 - 0.6.4 - Changed permissions of auth.conf - Fixes for working with rhn_yum_plugin - still allow repo configuration for distro repos that have just 1 repo (like C5.1) - disable CGI weblogging by default (backend logging TBA) - fix WebUI handling of keep_updated (repo field) and netboot_enabled (system field) - disable the blender_cache as its running afoul of the sync code - update htaccess file to only authenticate the webui, not nopxe.cgi and findks.cgi * Wed Nov 07 2007 - 0.6.3 - Be able to define and use Multiple NICs per system - Add --virt-cpus to profile editing - Fix bug where WUI (XMLRPC) auth wasnt supported on EL4 - Add --virt-bridge to ...
We just purchased a solar cover for our pool after mice destroyed the one we stored for the winter in my moms shed. We have a free form pool so I purchased a rectangular shaped cover and plan to trim. We laid it out over the pool for three days and then did a rough trim. I could have sworn that I read somewhere that you should let your cover sit for two weeks before doing a final fitted trim but now I cannot find that. Does anyone know if that is the case or are we ok to go ahead and do
sys_var (sys_var_chain *chain, const char *name_arg, const char *comment, int flag_args, ptrdiff_t off, int getopt_id, enum get_opt_arg_type getopt_arg_type, SHOW_TYPE show_val_type_arg, longlong def_val, PolyLock *lock, enum binlog_status_enum binlog_status_arg, on_check_function on_check_func, on_update_function on_update_func, const char *substitute, int parse_flag ...
Title : seqname Usage : $obj-,seq_id($newval) Function: There are many cases when you make a feature that you do know the sequence name, but do not know its actual sequence. This is an attribute such that you can store the seqname. This attribute should *not* be used in GFF dumping, as that should come from the collection in which the seq feature was found. Returns : value of seqname Args : newvalue (optional ...
Anybody ever use this function? It looks like exactly what I need. Im trying to get the content of a couple of resources into fred windows. In classic style, there is no documentation and C-x C-a says the args are named arg-1 arg-2 &key key-1 key-2 key-3 key-4 key-5. Maybe they figure what we dont know cant hurt us? Blake Meike [email protected] ...
At least 16 mutations in the EXOSC3 gene have been identified in people with a disorder of brain development called pontocerebellar hypoplasia. The major features of this condition include delayed development overall, an unusually small head size (microcephaly), and intellectual disability. EXOSC3 gene mutations cause about half of all cases of a form of the disorder designated pontocerebellar hypoplasia type 1 (PCH1). When PCH1 results from EXOSC3 gene mutations, it is sometimes categorized more specifically as PCH1B. In addition to the features listed above, PCH1B causes problems with muscle movement resulting from a loss of specialized nerve cells called motor neurons in the spinal cord.. The EXOSC3 gene mutations that cause PCH1B result in an exosome component 3 protein with reduced or no function. The most common mutation alters a single protein building block (amino acid) in exosome component 3; it replaces the amino acid aspartic acid with the amino acid alanine at protein position 132 ...
From UniProt:. Spastic paraplegia 63, autosomal recessive (SPG63): A form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body. [MIM:615686]. Pontocerebellar hypoplasia 9 (PCH9): A form of pontocerebellar hypoplasia, a disorder characterized by structural defects of the pons and cerebellum, evident upon brain imaging. PCH9 features include severely delayed psychomotor development, progressive microcephaly, spasticity, seizures, and brain abnormalities, including brain atrophy, thin corpus callosum, and delayed myelination. [MIM:615809]. ...
TY - JOUR. T1 - Molecular analysis of gene expression in the developing pontocerebellar projection system. AU - Diaz, Elva D. AU - Ge, Yongchao. AU - Yang, Yee Hwa. AU - Loh, Kenneth C.. AU - Serafini, Tito A.. AU - Okazaki, Yasushi. AU - Hayashizaki, Yoshihide. AU - Speed, Terence P.. AU - Ngai, John. AU - Scheiffele, Peter. PY - 2002/10/24. Y1 - 2002/10/24. N2 - As an approach toward understanding the molecular mechanisms of neuronal differentiation, we utilized DNA microarrays to elucidate global patterns of gene expression during pontocerebellar development. Through this analysis, we identified groups of genes specific to neuronal precursor cells, associated with axon outgrowth, and regulated in response to contact with synaptic target cells. In the cerebellum, we identified a phase of granule cell differentiation that is independent of interactions with other cerebellar cell types. Analysis of pontine gene expression revealed that distinct programs of gene expression, correlated with axon ...
Rabbit monoclonal antibody raised against a human TSEN15 peptide using ARM Technology. A synthetic peptide of human TSEN15 is used for rabbit immunization.Customer or Abnova will decide on the preferred peptide sequence. (H00116461-K) - Products - Abnova
hellogtk.c generated by valac 0.34.4, the Vala compiler * generated from hellogtk.vala, do not modify */ #include ,glib.h, #include ,glib-object.h, #include ,stdlib.h, #include ,string.h, #include ,gtk/gtk.h, #define _g_object_unref0(var) ((var == NULL) ? NULL : (var = (g_object_unref (var), NULL))) gint _vala_main (gchar** args, int args_length1); static void _gtk_main_quit_gtk_widget_destroy (GtkWidget* _sender, gpointer self); static void _gtk_main_quit_gtk_widget_destroy (GtkWidget* _sender, gpointer self) { gtk_main_quit (); } gint _vala_main (gchar** args, int args_length1) { gint result = 0; GtkWindow* window = NULL; GtkWindow* _tmp0_ = NULL; GtkLabel* label = NULL; GtkLabel* _tmp1_ = NULL; gtk_init (&args_length1, &args); _tmp0_ = (GtkWindow*) gtk_window_new (GTK_WINDOW_TOPLEVEL); g_object_ref_sink (_tmp0_); window = _tmp0_; gtk_window_set_title (window, Hello, World!); gtk_container_set_border_width ((GtkContainer*) window, (guint) 10); g_object_set (window, window-position, ...
Use Bio-Rads PrimePCR assays, controls, templates for your target gene. Every primer pair is optimized, experimentally validated, and performance guaranteed.
Use Bio-Rads PrimePCR assays, controls, templates for your target gene. Every primer pair is optimized, experimentally validated, and performance guaranteed.
The rest of the documentation details each of the object methods. Internal methods are usually preceded with a _ id Title : id Usage : $obj-,id(3); $id_integer = $obj-,id(); Function: Sets or returns the id of the translation table. IDs are integers from 0 (special ATG-only start) to 25, excluding 7-8 and 17-20 which have been removed. If an invalid ID is given the method returns 1, the standard table. Example : Returns : value of id, a scalar, warn and fall back to 1 (standard table) if specified id is not valid Args : newvalue (optional) name Title : name Usage : $obj-,name() Function: returns the descriptive name of the translation table Example : Returns : A string Args : None tables Title : tables Usage : $obj-,tables() or Bio::Tools::CodonTable-,tables() Function: returns a hash reference where each key is a valid codon table id() number, and each value is the corresponding codon table name() string Example : Returns : A hashref Args : None translate Title : translate Usage : ...
def ConvertJson(json_str): Convert json string to a python object. Args: json_str: string, json response. Returns: dictionary of deserialized json string. j = {} try: j = json.loads(json_str) j[json] = True except ValueError, e: # This means the format from json_str is probably bad. logger.error(Error parsing json string %s\n%s, json_str, e) j[json] = False j[error] = e return j def GetKeyValue(line, sep=:): Return value from a key value pair string. Args: line: string containing key value pair. sep: separator of key and value. Returns: string: value from key value string. s = line.split(sep) return StripPunc(s[1]) def StripPunc(s): Strip puncuation from string, except for - sign. Args: s: string. Returns: string with puncuation removed. for c in string.punctuation: if c == -: # Could be negative number, so dont remove -. continue else: s = s.replace(c, ) return s.strip() def Validate(response): Determine if JSON response indicated success. if ...
Warning: Declaration of Walker_Category_List_With_Slashes::start_el(&$output, $category, $depth, $args) should be compatible with Walker_Category::start_el(&$output, $category, $depth = 0, $args = Array, $id = 0) in /home/type/public_html/wp-content/themes/typetoken/functions.php on line 102 ...
Nma-Ile-His-Pro-Phe-His-Leu-Val-Ile-His-Thr-Lys(DNP)-D-Arg-D-Arg-NH2 3229-v 1 mg | 135.00 EUR[2- (Methylamino)benzoyl]- L- isoleucyl- L- ...
class BubbleSort { public static void sort(int[] a) { int i; int j; for (i = 0 ; i , a.length; i++) { /* move the largest number up */ for (j = 0 ; j , a.length - i - 1; j++) { if (a[j] , a[j+1]) ArrayUtil.swap(a, j, j + 1); } } } } public class BubbleSortTest { public static void main(String[] args) { int[] a = ArrayUtil.randomIntArray(20, 100); ArrayUtil.print(a); BubbleSort.sort(a); ArrayUtil.print(a ...
1, post_type => kwlogos, post_status => publish, orderby => rand, taxonomy => kwlogos-carousel, term => banner); $banner=get_posts($args); $thumbnail_id = get_post_thumbnail_id($banner[0]->ID); $image = wp_get_attachment_image_src($thumbnail_id, full ...
Where To Order Gabapentin Brand Pills Online Rating 4.5 stars, based on 348 comments Pharmacy Online Canada. Neurontin Best Order Reading and comprehensionA good option for coursework is to therapist suggests because it comes from the client themselves. Unique to the curriculum, students take professionally-oriented capstone courses classes graduate students may find in a program: … ...
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- ...
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 ...
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- ...
... 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 ...
... 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 ...
... 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 (2007). "A single residue in leucyl-tRNA synthetase affecting amino acid specificity and tRNA aminoacylation ...
... 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 ...
Ferber, S. dan Ciechanover, A. (1987) Role of Arginine-tRNA in Protein Degradation by the Ubiquitin Pathway. Nature 326,808-811 ... Hershko, A., Heller, H., Elias, S. dan Ciechanover, A. (1983) Components of ubiquitin-protein ligase system: resolution, ... Purification and characterization of arginyl-tRNA-protein transferase from rabbit reticulocytes: its involvement in ...
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. ... through initiator tRNA(fMet) aminoacylation. An important paralog of this gene is ENSG00000248235. Orthologs of the human gene ...
Aminoacyl tRNA synthetase *Alanine. *Arginine. *Asparagine. *Aspartate. *Cysteine. *D-alanine-poly(phosphoribitol) ligase ... 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 ... All four Mur ligases are topologically similar to one another, even though they display low sequence identity. They are each ...
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. ...
Protein arginine methyltransferase 6 PSRC1: Proline/serine-rich coiled-coil protein 1 RAD54L: RAD54-like RAP1A (1p13) RBM15 ( ... 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 ZMYM1 ... also known as arginine decarboxylase (ADC) BCAS2: Breast carcinoma amplified sequence 2 BCL10 (1p22) BCL2L15 (1p13) LRIF1: ...
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- ...
UBR4: E3 ubiquitin-protein ligase component n-recognin 4. *UROD: uroporphyrinogen decarboxylase (the gene for porphyria cutanea ... AZIN2: encoding enzyme Antizyme inhibitor 2 (AzI2) also known as arginine decarboxylase (ADC) ... "genetype trna"[Properties] OR "genetype scrna"[Properties] OR "genetype snrna"[Properties] OR "genetype snorna"[Properties]) ...
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 ... Delarue, M (1995). "Aminoacyl-tRNA synthetases". Structural Biology. 5: 48-55.. *^ "Molecule of the Month: Aminoacyl-tRNA ...
... 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 (ligase) has been shown to interact with: Alpha-synuclein, CASK, CUL1, FBXW7 and GPR37, HSPA1A, HSPA8, Multisynthetase ...
Ferber, S. lan Ciechanover, A. (1987) Role of Arginine-tRNA in Protein Degradation by the Ubiquitin Pathway. Nature 326,808-811 ... Hershko, A., Heller, H., Elias, S. lan Ciechanover, A. (1983) Components of ubiquitin-protéin ligase system: resolution, ... Purification and characterization of arginyl-tRNA-protéin transferase from rabbit reticulocytes: its involvement in ...
... queuine tRNA-ribosyltransferase EC 2.4.2.30: NAD+ ADP-ribosyltransferase EC 2.4.2.31: NAD(P)+-protein-arginine ADP- ... protein ligase EC 2.7.7.64: UTP-monosaccharide-1-phosphate uridylyltransferase EC 2.7.7.65: diguanylate cyclase EC 2.7.7.66: ... tRNA (cytosine-5-)-methyltransferase EC 2.1.1.30: deleted EC 2.1.1.31: tRNA (guanine-N1-)-methyltransferase EC 2.1.1.32: tRNA ( ... arginine N-methyltransferase EC 2.1.1.125: histone-arginine N-methyltransferase EC 2.1.1.126: (myelin basic protein)-arginine N ...
Aminoacyl tRNA synthetase *Alanine. *Arginine. *Asparagine. *Aspartate. *Cysteine. *D-alanine-poly(phosphoribitol) ligase ... glutamate-ammonia ligase. Active site between two monomers of glutamine synthetase from Salmonella typhimurium. Cation binding ...
Aminoacyl tRNA synthetase *Alanine. *Arginine. *Asparagine. *Aspartate. *Cysteine. *D-alanine-poly(phosphoribitol) ligase ... It represents the first committed step in pyrimidine and arginine biosynthesis in prokaryotes and eukaryotes, and in the urea ... cycle in most terrestrial vertebrates.[2] Most prokaryotes carry one form of CPSase that participates in both arginine and ...
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 ...
Aminoacyl tRNA synthetase *Alanine. *Arginine. *Asparagine. *Aspartate. *Cysteine. *D-alanine-poly(phosphoribitol) ligase ... L-glutamine amido-ligase (AMP-forming).[1][2][3][4][5][6] This enzyme catalyses the following chemical reaction ...
... 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]) ...
... if a tRNA synthases loaded an incorrect amino acid onto a tRNA, the resulting peptide would have unexpectedly altered ... "The primordial metabolism: an ancestral interconnection between leucine, arginine, and lysine biosynthesis". BMC Evolutionary ... Perona JJ, Hadd A (November 2012). "Structural diversity and protein engineering of the aminoacyl-tRNA synthetases". ... properties, consequently to enhance fidelity several additional domains are present.[27] Similar in reaction to tRNA synthases ...
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 ...
"TRDMT1 tRNA aspartic acid methyltransferase 1 (Homo sapiens)". Entrez Gene. NCBI. 2010-11-01. Retrieved 2010-11-07.. ... 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 ...
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- ...
arginine→. *Ornithine aminotransferase. *Ornithine decarboxylase. *Agmatinase. →alpha-ketoglutarate→TCA. *Glutamate ...
arginine→. *Ornithine aminotransferase. *Ornithine decarboxylase. *Agmatinase. →alpha-ketoglutarate→TCA. *Glutamate ...
Category:Ligases (EC 6) (Ligase)Edit. Category:EC 6.1 (form carbon-oxygen bonds)Edit. 6-carboxytetrahydropterin synthase ... EC 2.9.1.2: O-phospho-L-seryl-tRNA(Sec):L-selenocysteinyl-tRNA synthase ... EC 3.9.1.2: Protein arginine phosphatase. *EC 3.9.1.3: Phosphohistidine phosphatase. Category:EC 3.10 (act on sulfur-nitrogen ... 6 Category:Ligases (EC 6) (Ligase) *6.1 Category:EC 6.1 (form carbon-oxygen bonds) ...
WARS2 tryptophanyl tRNA synthetase 2, mitochondrial [ Homo sapiens (human) ]». Gene. NCBI. 4. juni 2017. Henta 26. juni 2017.. ... PRMT6 protein arginine methyltransferase 6 [ Homo sapiens (human) ]». Gene. NCBI. 8. juni 2017. Henta 26. juni 2017.. ... UBR4 ubiquitin protein ligase E3 component n-recognin 4 [ Homo sapiens (human) ]». Gene. NCBI. 4. juni 2017. Henta 26. juni ... TRIT1 tRNA isopentenyltransferase 1 [ Homo sapiens (human) ]». Gene. NCBI. 8. juni 2017. Henta 26. juni 2017.. ...
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 (September 2017). "Histone arginine demethylase JMJD6 is linked to stress ...
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- ...
IPR001412. aa-tRNA-synth_I_CS. IPR001278. Arg-tRNA-ligase. IPR005148. Arg-tRNA-synth_N. IPR036695. Arg-tRNA-synth_N_sf. ... IPR001412. aa-tRNA-synth_I_CS. IPR001278. Arg-tRNA-ligase. IPR005148. Arg-tRNA-synth_N. IPR036695. Arg-tRNA-synth_N_sf. ... Arginine--tRNA ligaseUniRule annotation. ,p>Information which has been generated by the UniProtKB automatic annotation system, ... ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg).UniRule annotation. ,p>Information which has been ...
IPR001412. aa-tRNA-synth_I_CS. IPR001278. Arg-tRNA-ligase. IPR005148. Arg-tRNA-synth_N. IPR035684. ArgRS_core. IPR008909. DALR_ ... IPR001412. aa-tRNA-synth_I_CS. IPR001278. Arg-tRNA-ligase. IPR005148. Arg-tRNA-synth_N. IPR035684. ArgRS_core. IPR008909. DALR_ ... Arginine--tRNA ligaseUniRule annotation. ,p>Manual validated information which has been generated by the UniProtKB automatic ... ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg).UniRule annotation. ,p>Manual validated information ...
... where it catalyzes the transfer of L-arginine to its cognate tRNA, an important step in translation of mitochondrially-encoded ...
Crystal structures of E.coli arginyl-tRNA synthetase (ArgRS) in complex with substrate tRNA(Arg) ... in complex with substrate tRNA(Arg). To Be Published Release Date. 2017-05-31. Peptides. Arginine--tRNA ligase: AC. SMTL:PDB. ... Crystal structures of E.coli arginyl-tRNA synthetase (ArgRS) in complex with substrate tRNA(Arg). Coordinates. PDB Format ... Zhou, M. et al., Crystal structures of E.coli arginyl-tRNA synthetase (ArgRS) ...
Arginine--tRNA ligase. Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 / 8081). Loading... ... Arginine--tRNA ligase. Listeria welshimeri serovar 6b (strain ATCC 35897 / DSM 20650 / SLCC5334). Loading... ... Arginine--tRNA ligase. Methanosaeta thermophila (strain DSM 6194 / JCM 14653 / NBRC 101360 / PT). Loading... ... Arginine--tRNA ligase. Magnetococcus marinus (strain ATCC BAA-1437 / JCM 17883 / MC-1). Loading... ...
Buy our Recombinant Human Arginyl tRNA synthetase protein. Ab114873 is a full length protein produced in Wheat germ and has ... Arginine tRNA ligase. *Arginine tRNA ligase 1, cytoplasmic. *Arginine--tRNA ligase. *Arginyl tRNA synthetase 1 ... Forms part of a macromolecular complex that catalyzes the attachment of specific amino acids to cognate tRNAs during protein ...
... arginine-tRNA ligase activity; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0006420; P:arginyl-tRNA ...
L-arginine supplements may improve the quality of life and erectile function in men who are prostate cancer surv... ... Arginine-trna Ligase. An enzyme that activates arginine with its specific transfer RNA. EC 6.1.1.19. ... Arginine Kinase. An enzyme that catalyzes the phosphorylation of the guanidine nitrogen of arginine in the presence of ATP and ... L-Arginine Supplements in Treating Women Who Are Cancer Survivors. RATIONALE: L-arginine supplements may improve the quality of ...
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 (inferred); ATP binding (inferred); INVOLVED IN arginyl-tRNA aminoacylation (inferred); tRNA ... ENCODES a protein that exhibits aminoacyl-tRNA ligase activity (inferred); ... ENCODES a protein that exhibits aminoacyl-tRNA ligase activity (inferred); arginine-tRNA ligase activity (inferred); ATP ... arginine-tRNA ligase activity IEA. InterPro:IPR008909. 2290270. UniProtKB. GO_REF:0000002, MGI:MGI:2152098. ...
BP] arginyl-tRNA aminoacylation *[CC] cytoplasm *[MF] ATP binding *[MF] arginine-tRNA ligase activity ...
Probable arginine--tRNA ligase, cytoplasmic. Organism. Caenorhabditis elegans (AnAge). Potential relevance to longevity and/or ...
Arginine--tRNA ligase. LOC108228760. AN1-type zinc finger protein 2A-like. TbgDal_XI17510. hypothetical protein, unlikely. ...
0913900 a putative arginine-tRNA ligase. When considering drug-resistant candidate polymorphism, crt mutations (K76T, Q271E, ...
3, Last annotation update) DE RecName: Full=Arginyl-tRNA synthetase 2; EC=6.1.1 19;AltName: DE Full=Arginine--tRNA ligase 2; ( ... arginine-tRNA ligase activity; IEA:HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:HAMAP. DR GO; GO:0006420; P:arginyl-tRNA ... DR HAMAP; MF_00123; Arg_tRNA_synth; 1; -. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR001278; Arg-tRNA-synth_Ia ... tRNA-synt_1c; 1. DR Pfam; PF03485; Arg_tRNA_synt_N; 1. DR Pfam; PF05746; DALR_1; 1. DR Pfam; PF00750; tRNA-synt_1d; 1. DR ...
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- ...
Ligase; Nucleotide-binding; Protein biosynthesis. FT CHAIN 1 556 Arginine--tRNA ligase. FT /FTId=PRO_1000018054. FT MOTIF 132 ... DR InterPro; IPR001278; Arg-tRNA-ligase. DR InterPro; IPR005148; Arg-tRNA-synth_N. DR InterPro; IPR036695; Arg-tRNA-synth_N_sf ... DE RecName: Full=Arginine--tRNA ligase {ECO:0000255,HAMAP-Rule:MF_00123}; DE EC=6.1.1.19 {ECO:0000255,HAMAP-Rule:MF_00123}; DE ... DR GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:UniProtKB-EC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO ...
Arginine-trna Ligase. An enzyme that activates arginine with its specific transfer RNA. EC 6.1.1.19. ... L-arginine add-on Therapy in Patients With Schizophrenia. This study evaluates the addition of L-Arginine to the usual regimen ... Study of Arginine and Nitric Oxide in Patients With Diabetes. This study will test the effect of arginine versus citrulline ... Arginine Kinase. An enzyme that catalyzes the phosphorylation of the guanidine nitrogen of arginine in the presence of ATP and ...
arginine-tRNA ligase activity. 1.50161401062914. bayes_pls_golite062009. *tryptophan-tRNA ligase activity ... Glutamyl-tRNA synthetase (GluRS), forms a complex with methionyl-tRNA synthetase (Mes1p) and Arc1p; complex formation increases ... Gln-tRNA synthetase (GlnRS), C-terminal (anticodon-binding) domain; Glutaminyl-tRNA synthetase (GlnRS) ... the catalytic efficiency of both tRNA synthetases and ensures their correct localization to the cytoplasm [SGD] ...
arginine-tRNA ligase activity (GO:0004814), nucleotide binding (GO:0000166), ATP binding (GO:0005524). ... The aminoacyl-tRNA synthetase (also known as aminoacyl-tRNA ligase) catalyse the attachment of an amino acid to its cognate ... Crystal Structure of E.coli Arginyl-tRNA Synthetase and Ligand Binding Studies Revealed Key Residues in Arginine Recognition. ... THERMUS THERMOPHILUS ARGINYL-TRNA SYNTHETASE. 2zue. Crystal structure of Pyrococcus horikoshii arginyl-tRNA synthetase ...
aja:AJAP_29485 Arginine-tRNA ligase K01887 574 104 ( -) 30 0.309 110 -, 1 apr:Apre_0153 Beta-glucosidase K01223 457 104 ( -) 30 ... lagg:B0E33_25740 glutamate--tRNA ligase K01885 474 106 ( -) 30 0.312 77 -, 1 lth:KLTH0D11902g KLTH0D11902p K04648 819 106 ( -) ... ahm:TL08_00170 arginyl-tRNA synthetase K01887 582 103 ( -) 29 0.305 105 -, 1 amo:Anamo_1277 urocanate hydratase K01712 679 103 ... aht:ANTHELSMS3_04207 DNA ligase B K10747 530 100 ( -) 29 0.307 140 -, 1 amed:B224_3976 sensor kinase CitA, putative 521 100 ...
jal:BZG29_04770 arginine--tRNA ligase K01887 569 103 ( -) 29 0.300 100 -, 1 jan:Jann_0374 Chromosome segregation protein SMC ... tRNA ligase, beta subun K01890 788 100 ( -) 29 0.303 122 -, 1 echs:ECHOSC_0381 phenylalanine--tRNA ligase, beta subun K01890 ... echw:ECHWAK_0680 phenylalanine--tRNA ligase, beta subun K01890 788 100 ( -) 29 0.303 122 -, 1 fgi:OP10G_3733 enolase K01689 432 ... abf:AMK58_11325 histidine--tRNA ligase K01892 449 110 ( -) 31 0.333 78 -, 1 bamf:U722_06060 ABC transporter ATP-binding protein ...
arginyl-tRNA aminoacylation (GO:0006420). GO function:. arginine-tRNA ligase activity (GO:0004814), ATP binding (GO:0005524). ... Crystal Structure of E.coli Arginyl-tRNA Synthetase and Ligand Binding Studies Revealed Key Residues in Arginine Recognition. ... THERMUS THERMOPHILUS ARGINYL-TRNA SYNTHETASE. 2zue. Crystal structure of Pyrococcus horikoshii arginyl-tRNA synthetase ... CRYSTAL STRUCTURE OF THE ARGINYL-TRNA SYNTHETASE COMPLEXED WITH THE TRNA(ARG) AND L-ARG. ...
Arginyi-tRNA synthetase Current Synonym true false 2971785015 Arginine-transfer ribonucleic acid ligase Current Synonym true ... Arginine-transfer ribonucleic acid ligase (substance). Code System Preferred Concept Name. Arginine-transfer ribonucleic acid ... Arginine-tRNA ligase Current Synonym true false 108295010 ... Substance with ligase mechanism of action (substance) {1672007 ...
A basic NH2-terminal extension of rat liver arginyl-tRNA synthetase required for its association with high molecular weight ...
Amino Acyl-tRNA Synthetases * Arginine-tRNA Ligase * Methionine-tRNA Ligase * Lysine-tRNA Ligase ... Fingerprint Dive into the research topics of Hierarchical network between the components of the multi-tRNA synthetase complex ... Hierarchical network between the components of the multi-tRNA synthetase complex: Implications for complex formation. ...
... hydroxyl of the tRNA, while, in class II reactions, the 3-hydroxyl site is preferred. The synthetases specific for arginine, ... Isoleucine-tRNA ligase (IPR002301). Short name: Ile-tRNA-ligase Family relationships *Isoleucine-tRNA ligase (IPR002301) * ... Isoleucine-tRNA ligase (also known as Isoleucyl-tRNA synthetase)(EC:6.1.1.5) is an alpha monomer that belongs to class Ia. The ... The aminoacyl-tRNA synthetase (also known as aminoacyl-tRNA ligase) catalyse the attachment of an amino acid to its cognate ...
Buy online RARS-arginyl-tRNA synthetase Gene from ProteoGenix cat# PTXBC000528. Shop among our wide range of DNA & ... arginyl-tRNA synthetase. Synonyms: ArgRS; DALRD1; HLD9; arginine--tRNA ligase, cytoplasmic; arginine tRNA ligase 1, cytoplasmic ... arginyl-tRNA synthetase, cytoplasmic; arginyl-tRNA synthetase. Sequence primers: Forward primer M13R (5→3): GTAAAACGACGGCCAGT ... More info about RARS-arginyl-tRNA synthetase Gene. Availability: PRODUCT NOT AVAILABLE. ...
Bacteriophage T4 RNA ligase 2 (gp24.1) exemplifies a family of RNA ligases found in all phylogenetic domains ... in addition to tRNA2Gln, tRNALys, and tRNAGlu. This is also the case for tRNACys, tRNATrp, tRNA3Ser, tRNA2Gly, and tRNA3Gly, ... for tRNAArgCCU (18). The DNA probes for control RNAs, tRNATyr, tRNAHis, tRNAAsn tRNAAsp, tRNA2Gln, tRNALys, tRNAGlu, and 16S- ... tRNAArgCCG, tRNAArgU*CU, and tRNAArgCCU. As shown in Fig. 3, not only tRNAArgICG but also tRNAArgCCG, tRNAArgU*CU, and tRNAArg ...
  • Alanine-tRNA Ligase" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (harvard.edu)
  • This graph shows the total number of publications written about "Alanine-tRNA Ligase" by people in Harvard Catalyst Profiles by year, and whether "Alanine-tRNA Ligase" was a major or minor topic of these publication. (harvard.edu)
  • Below are the most recent publications written about "Alanine-tRNA Ligase" by people in Profiles. (harvard.edu)
  • This nuclear gene encodes a protein that localizes to the mitochondria, where it catalyzes the transfer of L-arginine to its cognate tRNA, an important step in translation of mitochondrially-encoded proteins. (nih.gov)
  • To build new proteins, tRNA must collect different amino acids and then attach them to one another in the correct order. (medlineplus.gov)
  • Specifically, this enzyme links the amino acid arginine to the tRNA molecule, which then incorporates it into new proteins in mitochondria. (medlineplus.gov)
  • Methods are described for determination of arginine-specific mono-ADP-ribosyltransferase activity of purified proteins and intact cells by monitoring the transfer of ADP-ribose from NAD to a model sub. (bioportfolio.com)
  • Enzymes that catalyze the methylation of arginine residues of proteins to yield N-mono- and N,N-dimethylarginine. (bioportfolio.com)
  • The mechanism of canavanine's toxicity is that organisms that consume it typically mistakenly incorporate it into their own proteins in place of L-arginine, thereby producing structurally aberrant proteins that may not function properly. (wikipedia.org)
  • These larvae fastidiously avoid incorporation of L-canavanine into their nascent proteins (presumably by virtue of highly discriminatory Arginine-tRNA ligase, the enzyme responsible for the first step in the incorporation of arginine into proteins). (wikipedia.org)
  • There are 26085 Arg_tRNA_synt_N domains in 26083 proteins in SMART's nrdb database. (embl.de)
  • Taxonomic distribution of proteins containing Arg_tRNA_synt_N domain. (embl.de)
  • The complete taxonomic breakdown of all proteins with Arg_tRNA_synt_N domain is also avaliable . (embl.de)
  • Click on the protein counts, or double click on taxonomic names to display all proteins containing Arg_tRNA_synt_N domain in the selected taxonomic class. (embl.de)
  • 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. (mssm.edu)
  • Proteins of the herpes simplex virus are rich in L-arginine, and tissue culture studies indicate an enhancing effect on viral replication when the amino acid ratio of L-arginine to L-lysine is high in the tissue culture media. (drugbank.ca)
  • The amino acid serves as a precursor for synthesis of proteins, oligopeptides, purines, pyrimidines, nucleic acids and L-arginine. (drugbank.ca)
  • Some ligases associate with biological membranes as peripheral membrane proteins or anchored through a single transmembrane helix , [2] for example certain ubiquitin ligase related proteins. (wikipedia.org)
  • 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)
  • phase II trial is studying how well L-arginine supplementation works with or without enzyme inhibitors in treating erectile function and quality of life of prostate cancer survivors previously treated with radiation therapy. (bioportfolio.com)
  • The RARS2 gene provides instructions for making an enzyme called mitochondrial arginyl-tRNA synthetase. (medlineplus.gov)
  • An enzyme that activates arginine with its specific transfer RNA. (bioportfolio.com)
  • 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. (bioportfolio.com)
  • Aminoacyl-tRNA synthetase (aaRS) is a key enzyme during protein biosynthesis. (embl-heidelberg.de)
  • The enzyme, isoleucine-tRNA ligase, activates not only the cognate substrate L-isoleucine but also the minimally distinct L-valine in the first, aminoacylation step. (ebi.ac.uk)
  • Escherichia coli 4-fluorotryptophan-substituted arginyl-tRNA synthetase was biosynthetically prepared and purified from a tryptophan auxotroph which could overproduce this enzyme. (elsevier.com)
  • We may conclude that the substitution of 4-fluorotryptophan in arginyl-tRNA synthetase had no substantial effect on the structure and function of the enzyme. (elsevier.com)
  • It is a mitochondrial enzyme that specifically aminoacylates aspartyl-tRNA. (mssm.edu)
  • Most (107 kb) of plasmid pHSAL1 (91-R6) is very closely related to part of plasmid pHS3 (R1) and codes for essential genes (e.g. arginine-tRNA ligase and the pyrimidine biosynthesis enzyme aspartate carbamoyltransferase). (archives-ouvertes.fr)
  • The conserved sequence motifs found in the four Mur enzymes also map to other members of the Mur ligase family, including folylpolyglutamate synthetase, cyanophycin synthetase and the capB enzyme from Bacillales. (wikipedia.org)
  • In biochemistry , a ligase is an enzyme that can catalyze the joining of two large molecules by forming a new chemical bond , usually with accompanying hydrolysis of a small pendant chemical group on one of the larger molecules or the enzyme catalyzing the linking together of two compounds, e.g., enzymes that catalyze joining of C-O, C-S, C-N, etc. (wikipedia.org)
  • The common names of ligases often include the word "ligase", such as DNA ligase , an enzyme commonly used in molecular biology laboratories to join together DNA fragments. (wikipedia.org)
  • It is also said that a synthase is a lyase (a lyase is an enzyme that catalyzes the breaking of various chemical bonds by means other than hydrolysis and oxidation, often forming a new double bond or a new ring structure) and does not require any energy, whereas a synthetase is a ligase (a ligase is an enzyme that binds two chemicals or compounds) and thus requires energy. (wikipedia.org)
  • The second enzyme in the arginine succinyltransferase (AST) pathway for the catabolism of arginine. (cathdb.info)
  • Each aaRS contains a catalytic central domain (CCD), responsible for activating amino acid, and an anticodon-binding domain (ABD), necessary for binding the anticodon in cognate tRNA. (embl-heidelberg.de)
  • The arginyl-tRNA synthetase (ArgRS) catalyzes the esterification reaction between L-arginine and its cognate tRNA(Arg) . (bvsalud.org)
  • ARSs are ubiquitously expressed, essential enzymes that ligate amino acids to cognate tRNA molecules. (ox.ac.uk)
  • Aminoacyl-tRNA syntheses (AARS) can catalyze the adenosine triphosphate (ATP)-dependent acylation of their cognate tRNA(s) with a specific amino acid. (bvsalud.org)
  • Aminoacyl tRNA synthetase (aaRS) or tRNA ligase catalyzes the esterification of a specific amino acid to its cognate tRNA to form an aminoacyl-tRNA. (proteopedia.org)
  • Previously reported structures of ArgRS shed considerable light on the tRNA recognition mechanism, while the aspect of amino acid binding in ArgRS remains largely unexplored. (bvsalud.org)
  • Here we report the first crystal structure of E. coli ArgRS (eArgRS) complexed with L-arginine , and a series of mutational studies using isothermal titration calorimetry (ITC). (bvsalud.org)
  • The expression changes of Rars gene in ischemia-injured neurons were investigated by detecting its translational product arginyl-tRNA synthetase (ArgRS), and the inhibitory effects of ischemic preconditioning (IPC) on Rars gene were explored. (bvsalud.org)
  • This study examined the relationship between arginyl-tRNA synthetase (ArgRS), one of the AARS, and cerebral ischemia in rats. (bvsalud.org)
  • Several unexpected evolutionaryconnections were identified, including the apparent origin of thebeta-subunit of bacterial GlyRS from the HD superfamily of hydrolases, adomain shared by bacterial AspRS and the B subunit of archaealglutamyl-tRNA amidotransferases, and another previously undetected domainthat is conserved in a subset of ThrRS, guanosine polyphosphate hydrolasesand synthetases, and a family of GTPases. (embl-heidelberg.de)
  • Two mecillinam resistant mutants, lov-1 and lovB, both able to dispense entirely with PBP2, are shown here to be affected in the aminoacyl-tRNA synthetase genes argS and alaS, respectively. (microbialphenotypes.org)
  • Four genes encoding an aminoacyl-tRNA synthetase (ARS) have been implicated in CMT disease. (ox.ac.uk)
  • Localization of two human autoantigen genes by PCR screening and in situ hybridization--glycyl-tRNA synthetase locates to 7p15 and alanyl-tRNA synthetase locates to 16q22. (harvard.edu)
  • Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase. (ebi.ac.uk)
  • ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys). (cathdb.info)
  • From Cysteine (C) to Arginine (R) at position 76 (C76R, p.Cys76Arg). (expasy.org)
  • Mitochondrial arginyl-tRNA synthetase is one of several enzymes that link amino acids to tRNA. (medlineplus.gov)
  • The aminoacyl-tRNA synthetases (AARS) are a family of heterogenous enzymes responsible protein synthesis and whose secondary functions include a role in autoimmune myositis. (usda.gov)
  • Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. (mssm.edu)
  • Ligases are classified as EC 6 in the EC number classification of enzymes. (wikipedia.org)
  • Mitochondrial arginyl-tRNA synthetase interacts with a molecule called transfer RNA (tRNA). (medlineplus.gov)
  • The RARS2 gene mutations that cause pontocerebellar hypoplasia significantly reduce or eliminate the function of mitochondrial arginyl-tRNA synthetase. (medlineplus.gov)
  • This gene encodes a mitochondrial aminoacyl-tRNA synthetase, which catalyzes the attachment of valine to tRNA(Val) for mitochondrial translation. (mssm.edu)
  • This all alpha helical domain is the anticodon binding domain (ABD) of arginyl tRNA synthetase, and also matches the ABD of some glycine tRNA synthetases. (embl-heidelberg.de)
  • Protein biosynthesis is a universally conserved three-step process that occurs on ribosomes and provides a platform for tRNA mediated amino acid delivery. (frontiersin.org)
  • Evolution of aminoacyl-tRNA synthetases--analysis of unique domainarchitectures and phylogenetic trees reveals a complex history ofhorizontal gene transfer events. (embl-heidelberg.de)
  • Encodes a type I protein arginine methyltransferase based on the At1g04870.2 gene model. (gifu-u.ac.jp)
  • The protein encoded by this gene belongs to class-I aminoacyl-tRNA synthetase family and is located in the class III region of the major histocompatibility complex. (mssm.edu)
  • This gene encodes a member of a multienzyme complex that functions in mediating the attachment of amino acids to their cognate tRNAs. (mssm.edu)
  • The protein encoded by this gene belongs to the class-II aminoacyl-tRNA synthetase family. (mssm.edu)
  • The protein encoded by this gene is a multifunctional aminoacyl-tRNA synthetase that catalyzes the aminoacylation of glutamic acid and proline tRNA species. (mssm.edu)
  • Belongs to the class-I aminoacyl-tRNA synthetase family. (abcam.com)
  • Forms part of a macromolecular complex that catalyzes the attachment of specific amino acids to cognate tRNAs during protein synthesis. (abcam.com)
  • Catalyzes the attachment of serine to tRNA(Ser). (string-db.org)
  • Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction- L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). (string-db.org)
  • Catalyzes the attachment of valine to tRNA(Val). (string-db.org)
  • ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg). (uniprot.org)
  • 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)
  • This domain is found at the amino terminus of Arginyl tRNA synthetase, also called additional domain 1 (Add-1). (embl.de)
  • Crystal structure of arginyl-tRNA synthetase from Klebsiella pneumoniae subsp. (embl.de)
  • This all alpha helical domain is the anticodon binding domain of Arginyl tRNA synthetase. (embl-heidelberg.de)
  • A basic NH2-terminal extension of rat liver arginyl-tRNA synthetase required for its association with high molecular weight complexes. (elsevier.com)
  • It was confirmed that more than 95% of the tryptophan residues in the purified 4-fluorotryptophan- substituted arginyl-tRNA synthetase were replaced by 4-fluorotryptophan. (elsevier.com)
  • The 20 aminoacyl-tRNA synthetases are divided into two classes, I and II. (embl.de)
  • However, tRNA binding involves an alpha-helical structure that is conserved between class I and class II synthetases. (embl.de)
  • In reactions catalysed by the class I aminoacyl-tRNA synthetases, the aminoacyl group is coupled to the 2'-hydroxyl of the tRNA, while, in class II reactions, the 3'-hydroxyl site is preferred. (embl.de)
  • Phylogenetic analysis of aminoacyl-tRNA synthetases (aaRSs) of all 20specificities from completely sequenced bacterial, archaeal, andeukaryotic genomes reveals a complex evolutionary picture. (embl-heidelberg.de)
  • Aminoacyl-tRNA synthetases, the genetic code, and the evolutionary process. (ebi.ac.uk)
  • Aminoacyl-tRNA synthetases: versatile players in the changing theater of translation. (ebi.ac.uk)
  • Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs. (ebi.ac.uk)
  • Classes of aminoacyl-tRNA synthetases and the establishment of the genetic code. (ebi.ac.uk)
  • Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases. (ebi.ac.uk)
  • Aminoacyl-tRNA synthetases catalyze the aminoacylation of tRNA by their cognate amino acid. (mssm.edu)
  • Cavarelli J, Moras D. Recognition of tRNAs by aminoacyl-tRNA synthetases. (proteopedia.org)
  • This domain is the core catalytic domain of tRNA synthetases and includes glycyl, prolyl, seryl and threonyl tRNA synthetases. (xfam.org)
  • Asparaginyl-tRNA synthetase (AsnRS) is a member of the class-II aminoacyl-tRNA synthetases, and is responsible for catalyzing the specific aminoacylation of tRNA(Asn) with asparagine. (rcsb.org)
  • This domain is about 140 residues long and it has been suggested that it is involved in tRNA recognition. (wikipedia.org)
  • CDC64 encodes cytoplasmic alanyl-tRNA synthetase, Ala1p, of Saccharomyces cerevisiae. (harvard.edu)
  • A major determinant for binding and aminoacylation of tRNA(Ala) in cytoplasmic Alanyl-tRNA synthetase is mutated in dominant axonal Charcot-Marie-Tooth disease. (expasy.org)
  • The argS and alaS mutants have high pools of the nucleotide ppGpp (effector of the stringent response) and the mecillinam resistance of both mutations is suppressed by a relA mutation, inactivating the ribosome-associated ppGpp synthetase and preventing ppGpp synthesis in response to aminoacyl-tRNA starvation. (microbialphenotypes.org)
  • Furthermore, based on a docking model of AsnRS and tRNA, a single arginine residue (Arg83) in the AsnRS was postulated to be involved in the recognition of the third position of the tRNA(Asn) anticodon (U36). (rcsb.org)
  • This water-assisted asparagine recognition by the AsnRS strikingly contrasts with the fact that the aspartic acid recognition by the closely related aspartyl-tRNA synthetase is achieved exclusively through extensive interactions with protein amino acid residues. (rcsb.org)
  • Misacylation of pyrrolysine tRNA in vitro and in vivo. (harvard.edu)
  • For pyrrolysyl-RS of pyrrolysine-tRNA ligase details see Pyrrolysyl-tRNA synthetase . (proteopedia.org)
  • L-Lysine is a base, as are arginine and histidine. (drugbank.ca)
  • When the ratio of L-lysine to L-arginine is high, viral replication and the cytopathogenicity of herpes simplex virus have been found to be inhibited. (drugbank.ca)
  • A seven amino acids long loop between beta-strands β3/β4 is crucial for EF-P function and modified at its tip by lysylation of lysine or rhamnosylation of arginine. (frontiersin.org)
  • [4] These four Mur ligases are responsible for the successive additions of L-alanine, D-glutamate, meso- diaminopimelate or L-lysine, and D-alanyl-D-alanine to UDP- N-acetylmuramic acid . (wikipedia.org)
  • A recurrent loss-of-function alanyl-tRNA synthetase (AARS) mutation in patients with Charcot-Marie-Tooth disease type 2N (CMT2N). (ox.ac.uk)
  • Together, our data suggest that impaired tRNA charging plays a role in the molecular pathology of CMT2N, and that patients with CMT should be directly tested for the p.Arg329His AARS mutation. (ox.ac.uk)
  • Furthermore, we generated a single mutation of histidine in the C-terminal possible catalytic domain, which caused the loss of the killing activity in vivo together with the tRNA Arg -cleaving activity both in vivo and in vitro . (pnas.org)
  • From Arginine (R) to Histidine (H) at position 329 (R329H, p.Arg329His). (expasy.org)
  • Here, we show that colicin D specifically cleaves tRNAs Arg including four isoaccepting molecules both in vivo and in vitro . (pnas.org)
  • Other common names for ligases include the word "synthetase", because they are used to synthesize new molecules. (wikipedia.org)
  • The encoded protein ligates L-aspartate to tRNA(Asp). (mssm.edu)
  • Despite these apparently similar actions on tRNAs and cells, colicins D and E5 not only exhibit no sequence homology but also have different molecular mechanisms as to both substrate recognition and catalytic reaction. (pnas.org)
  • Bi-allelic mutations in Phe-tRNA synthetase associated with a multi-system pulmonary disease support non-translational function. (expasy.org)
  • We performed a mutational analysis of this particular arginine residue, and confirmed its significance in the tRNA recognition. (rcsb.org)
  • This family includes UDP-N-acetylmuramate-L-alanine ligase (MurC), UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase (MurE), and UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase (MurF). (wikipedia.org)
  • This pathway converts the carbon skeleton of arginine into glutamate, with the concomitant production of ammonia and conversion of succinyl-CoA into succinate and CoA. (cathdb.info)
  • Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. (string-db.org)
  • Consistent with the cleavage of tRNAs Arg , the RNA fraction of colicin-treated cells significantly reduced the amino acid-accepting activity only for arginine. (pnas.org)
  • Deficient activity of alanyl-tRNA synthetase underlies an autosomal recessive syndrome of progressive microcephaly, hypomyelination, and epileptic encephalopathy. (harvard.edu)
  • A protein complex that includes a ubiquitin-protein ligase and enables ubiquitin protein ligase activity. (leibniz-fli.de)
  • Shimizu T, Yoshiura H, Nagano H, Hirasawa I. Effect of Specific Amino Acids on Controlling Crystal Pseudopolymorphism of L -Arginine Hydrochloride. (kyowahakko-bio.co.jp)