CDD An aminoacyltRNAsynthetase aaRS is an enzyme that catalyzes the esterification of a specific amino acid or its precursor to one of all its compatible cognate tRNA s to form an aminoacyltRNA . This is sometimes ... charged, the aminoacyltRNA bond is hydrolyzed. Reaction Reaction amino acid ATP aminoacyl AMP PP sub i sub aminoacyl AMP tRNAaminoacyltRNA AMP Sum of 1 and 2 amino acid tRNA ATP aminoacyltRNA AMP PP sub i sub Classes There are two classes of aminoacyltRNAsynthetase ref cite web url ... cs AminoacyltRNA syntet za de AminoacyltRNASynthetase fr Aminoacyl ARNt synth tase gl Aminoacil ... width caption leucyl trnasynthetase from thermus thermophilus complexed with a post transfer editing ... 1 image PDB 1iq0 EBI.jpg width caption thermus thermophilus arginyl trnasynthetase Pfam PF05746 ... width caption crystal structure of cysteinyl trnasynthetase binary complex with trnacys Pfam PF09190 ... 18 work ref AminoacyltRNA synthetases, class I Class I has two highly conserved sequence motifs. It aminoacylation ... dimer dimeric one or two subunits, respectively . AminoacyltRNA synthetases, class II Class ... . Although phenylalanine tRNAsynthetase is class II, it aminoacylates at the 2 OH. The amino ... of where the aminoacyl is initially attached to the nucleotide, the 2 O aminoacyltRNA will ultimately migrate to the 3 position via transesterification . Structures Both classes of aminoacyltRNA ... accessdate 2007 08 18 work ref that cleave incorrectly paired aminoacyltRNA molecules. The catalytic ..., Grishin NV, Koonin EV title Evolution of aminoacyltRNA synthetases analysis of unique domain architectures ... Biology Reviews, March 2000, p. 202 236, Vol. 64, No. 1 AminoacyltRNA Synthetases, the Genetic Code, and the Evolutionary Process . Expanding the genetic code via mutant aminoacyltRNA synthetases In some of the aminoacyltRNA synthetases, the cavity that holds the amino acid can be mutated ... Raghava 2010 Prediction and classification of aminoacyltRNA synthetases using PROSITE domains. http ... more details
AminoacyltRNA is Transfer RNA tRNA also known as transfer ribonucleic acid to which its cognated amino acid is adhered. Its role is to deliver the amino acid to the ribosome where it will be incorporated into the polypeptide chain that is being produced. ref name Stryer 2006 cite book author Berg J, Tymoczko JL, Stryer L title Biochemistry publisher W. H. Freeman edition 6th ed. location San Francisco year 2006 isbn 0 7167 8724 5 ref A specific amino acid is added to each tRNA, which is crucial since it means that only that particular amino acid will be incorporated when the anticodon of that tRNA fits can form a transient base pair with the next codon of the Messenger RNA mRNA that is being translated into protein. The specific linkage of the correct amino acid to each tRNA is accomplished by aminoacyltRNAsynthetase s. Due to the degeneracy of the genetic code , some of the different tRNAs have the same amino acid attached to them. Synthesis AminoacyltRNA also known as charged tRNA is produced in two steps amino acid activation and transfer. The first step is the adenylation of the amino acid, which forms aminoacyl AMP Amino acid ATP Aminoacyl AMP PP sub i sub Then, the amino acid residue is transferred to the tRNAAminoacyl AMP tRNAAminoacyltRNA AMP The net reaction is Amino acid ATP tRNAAminoacyltRNA AMP PP sub i sub The net reaction is only energetically favourable because the pyrophosphate is hydrolysed that reaction is highly energetically favourable and drives the other reactions. All of these reactions take place inside the aminoacyltRNAsynthetase specific for that tRNA. Drugs that target aminoacyltRNA binding to ribosomal subunit Certain drugs like tetracycline prevent the aminoacyltRNA from binding to the ribosomal subunit in prokaryotes . References ... and how to generate footnotes using the ref & ref tags and the Reflist template Reflist See also AminoacyltRNAsynthetase Category Protein biosynthesis zh tRNA ... more details
enzyme Name aminoacyltRNA hydrolase EC number 3.1.1.29 CAS number 9054 98 2 IUBMB EC number 3 1 1 29 GO code 0004045 image width caption In enzymology , an aminoacyltRNA hydrolase EC number 3.1.1.29 is an enzyme that catalysis catalyzes the chemical reaction N Substituted aminoacyltRNA H sub 2 sub O math rightleftharpoons math N substituted amino acid tRNA Thus, the two substrate biochemistry substrates of this enzyme are N Substituted aminoacyltRNA and water H sub 2 sub O , whereas its two product chemistry products are N substituted amino acid and tRNA . This enzyme belongs to the family of hydrolase s, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is aminoacyltRNA aminoacylhydrolase . Other names in common use include aminoacyl transfer ribonucleate hydrolase , N substituted aminoacyl transfer RNA hydrolase , and peptidyl tRNA hydrolase . Structural studies As of late 2007, 9 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1RYB , PDB link 1WN2 , PDB link 1XTY , PDB link 2D3K , PDB link 2E1B , PDB link 2PTH , PDB link 2Z2I , PDB link 2Z2J , and PDB link 2Z2K . References reflist 1 cite journal author Jost JP, Bock RM date 1969 title Enzymatic hydrolysis of N substituted aminoacyl transfer ribonucleic acid in yeast journal J. Biol. Chem. volume 244 pages 5866&ndash 73 pmid 4981785 issue 21 hydrolase stub Category EC 3.1.1 Category Enzymes of known structure ... more details
mass aminoacyltRNAsynthetase complex. Effects of neutral salts and detergents. journal J. Biol ...PBB geneid 51520 Leucyl tRNAsynthetase, cytoplasmic is an enzyme that in humans is encoded by the LARS gene . ref name pmid6933703 cite journal author Giles RE, Shimizu N, Ruddle FH title Assignment of a human genetic locus to chromosome 5 which corrects the heat sensitive lesion associated with reduced leucyl tRNAsynthetase activity in ts025Cl Chinese hamster cells journal Somatic Cell Genet volume ... entrez cite web title Entrez Gene LARS leucyl tRNAsynthetase url http www.ncbi.nlm.nih.gov sites entrez ... title summary text This gene encodes a cytosolic leucine tRNAsynthetase, a member of the class I aminoacyltRNAsynthetase family. The encoded enzyme catalyzes the ATP dependent ligation of L leucine to tRNA Leu . It is found in the cytoplasm as part of a multisynthetase complex and interacts with the arginine tRNAsynthetase through its C terminal domain. Alternatively spliced transcript variants ... also Leucine tRNA ligase Interactions Leucyl tRNAsynthetase has been shown to Protein protein interaction .... title Interaction network of human aminoacyltRNA synthetases and subunits of elongation factor 1 complex ... of aminoacyltRNA synthetases identification of protein protein interactions and characterization ... of protein protein interactions in multi tRNAsynthetase complex. journal Proc. Natl. Acad. Sci. U.S.A. ... 90 mediates protein protein interactions between human aminoacyltRNA synthetases. journal J. Biol ... of human aminoacyltRNA synthetases and subunits of elongation factor 1 complex. journal Biochem. Biophys ... terminal appended domain of human cytosolic leucyl tRNAsynthetase is indispensable in its interaction with arginyl tRNAsynthetase in the multi tRNAsynthetase complex. journal J. Biol. Chem. volume ... tRNAsynthetase affecting amino acid specificity and tRNA aminoacylation. journal Biochemistry volume ... al. title A novel mutation in the mitochondrial DNA tRNA Leu UUR gene associated with late onset ... more details
tRNAsynthetase, one of the aminoacyltRNA synthetases that charge tRNAs with their cognate amino acids. The encoded enzyme is an alpha 2 dimer which belongs to the class II family of tRNA synthetases ...Merge Glycine tRNA ligase date May 2009 PBB geneid 2617 Glycyl tRNAsynthetase is an enzyme that in humans is encoded by the GARS gene . ref name pmid8595897 cite journal author Nichols RC, Pai SI, Ge Q, Targoff IN, Plotz PH, Liu P title Localization of two human autoantigen genes by PCR screening and in situ hybridization glycyl tRNAsynthetase locates to 7p15 and alanyl tRNAsynthetase locates to 16q22 ... tRNAsynthetase url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch ... or dermatomyositis. ref name entrez Interactions Glycyl tRNAsynthetase has been shown to Protein protein ... month Feb. title Interaction network of human aminoacyltRNA synthetases and subunits of elongation ... glycine tRNAsynthetase. journal Nucleic Acids Res. volume 23 issue 8 pages 1307 10 year 1995 pmid ... Primary structure and functional expression of human Glycyl tRNAsynthetase, an autoantigen in myositis ... author Shiba K, Schimmel P, Motegi H, Noda T title Human glycyl tRNAsynthetase. Wide divergence of primary ... Complex organisation of the 5 end of the human glycine tRNAsynthetase gene. journal Gene volume ... H, et al. title Interaction network of human aminoacyltRNA synthetases and subunits of elongation ... A, Ellsworth RE, Sambuughin N, et al. title Glycyl tRNAsynthetase mutations in Charcot Marie ... X ray analysis of a native human tRNAsynthetase whose allelic variants are associated with Charcot ... glycyl tRNAsynthetase, an enzyme underlying distal spinal muscular atrophy. journal FEBS Lett. volume ... disease causing mutation in human glycyl tRNAsynthetase. journal Proc. Natl. Acad. Sci. U.S.A. ... format accessdate laysummary laysource laydate quote ref See also Glycine tRNA ligase References ... KH, Kim JW, et al. title Interaction between human tRNA synthetases involves repeated sequence elements ... more details
Pfam box Symbol Glu Gln tRNA synth Ic Name Glutamyl glutaminyl tRNAsynthetase, class Ic Pfam PF00749 ... PDB 1irx PDB 1j09 The aminoacyltRNA synthetases EC number 6.1.1. catalyse the attachment of an amino ... issue 6289 pages 203 206 year 1990 pmid 2203971 doi 10.1038 347203a0 ref . The 20 aminoacyltRNA synthetases are divided into two classes, I and II. Class I aminoacyltRNA synthetases contain a characteristic ... S, Lorber B, Giege R title The 2.0 A crystal structure of Thermus thermophilus methionyl tRNAsynthetase reveals two RNA binding modules journal Structure volume 8 issue 2 pages 197 208 year 2000 pmid 10673435 doi 10.1016 S0969 2126 00 00095 2 ref . Class II aminoacyltRNA synthetases share ... coli glutaminyl tRNAsynthetase journal Biochemistry volume 32 issue 34 pages 8758 8771 year 1993 pmid ... conserved regions ref name PUB00000723 cite journal author Delarue M, Moras D title The aminoacyltRNAsynthetase family modules at work journal Bioessays volume 15 issue 10 pages 675 687 year 1993 ... Classes of aminoacyltRNA synthetases and the establishment of the genetic code journal Trends ... and evolutionary relationships between class 2 aminoacyltRNA synthetases journal Nucleic Acids Res ... Bairoch A title List of aminoacyltRNA synthetases journal volume issue pages year 2004 ref . Glutamyl tRNAsynthetase EC number 6.1.1.17 is a class Ic synthetase and shows several similarities with glutaminyl tRNAsynthetase concerning structure and catalytic properties. It is an alpha2 dimer. To date one crystal structure of a glutamyl tRNAsynthetase Thermus thermophilus has been solved. The molecule ... cite journal author Delarue M, Moras D, Poch O, Eriani G, Gangloff J title Partition of tRNA synthetases ... ref . However, tRNA binding involves an alpha helical structure that is conserved between class I and class II synthetases. In reactions catalysed by the class I aminoacyltRNA synthetases, the aminoacyl group is coupled to the 2 hydroxyl of the tRNA, while, in class II reactions, the 3 hydroxyl site ... more details
Pfam box Symbol aa tRNA synt II Name AminoacyltRNAsynthetase, class II D, K and N Pfam PF00152 InterPro IPR004364 PROSITE PDB PDB 1asy PDB 1asz PDB 1b8a PDB 1bbu PDB 1bbw PDB 1c0a PDB 1e1o PDB 1e1t PDB 1e22 PDB 1e24 AminoacyltRNAsynthetase, class II D, K and N EC number 6.1.1. catalyse the attachment of an amino acid to its cognate transfer RNA molecule in a highly specific two step reaction. These proteins differ widely in size and oligomeric state, and have limited sequence homology ref name PUB00007191 cite journal author Delarue M, Moras D, Poch O, Eriani G, Gangloff J title Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs journal Nature volume 347 issue 6289 pages 203 206 year 1990 pmid 2203971 doi 10.1038 347203a0 ref . The 20 aminoacyltRNA synthetases are divided into two classes, I and II. Class I aminoacyltRNA synthetases contain ... The aminoacyltRNAsynthetase family modules at work journal Bioessays volume 15 issue 10 pages 675 ... tRNAsynthetase reveals two RNA binding modules journal Structure volume 8 issue 2 pages 197 208 year 2000 pmid 10673435 doi 10.1016 S0969 2126 00 00095 2 ref . Class II aminoacyltRNA synthetases ... coli glutaminyl tRNAsynthetase journal Biochemistry volume 32 issue 34 pages 8758 8771 year ... P title Classes of aminoacyltRNA synthetases and the establishment of the genetic code journal ..., structural and evolutionary relationships between class 2 aminoacyltRNA synthetases journal Nucleic ... pmc 328370 ref . However, tRNA binding involves an alpha helical structure that is conserved between class I and class II synthetases. In reactions catalysed by the class I aminoacyltRNA synthetases, the aminoacyl group is coupled to the 2 hydroxyl of the tRNA, while, in class II reactions, the 3 hydroxyl ... author Bairoch A title List of aminoacyltRNA synthetases journal volume issue pages year 2004 ... References reflist InterPro content IPR004364 DEFAULTSORT AminoacylTrna Synthetases, Class Ii Category ... more details
protein Name asparagine synthetase caption image width HGNCid 753 Symbol ASNS AltSymbols EntrezGene 440 OMIM 108370 RefSeq NM 001673 UniProt P08243 PDB ECnumber 6.3.5.4 Chromosome 7 Arm q Band 21 LocusSupplementaryData q31 Asparagine synthetase or aspartate ammonia ligase is an enzyme that generates asparagine from aspartate . This amidation reaction is similar to that promoted by glutamine synthetase . External links MeshName Asparagine synthetase ligase stub Ligases Amino acid metabolism enzymes de Asparaginsynthetase ja ... more details
protein Name holocarboxylase synthetase biotin proprionyl Coenzyme A carboxylase ATP hydrolysing ligase caption image width HGNCid 4976 Symbol HLCS AltSymbols EntrezGene 3141 OMIM 609018 RefSeq NM 000411 UniProt P50747 PDB ECnumber 6.3.4.10 Chromosome 21 Arm q Band 22.1 LocusSupplementaryData HLCS holocarboxylase synthetase biotin proprionyl Coenzyme A carboxylase ATP hydrolysing ligase is a human gene that provides instructions for making an enzyme called holocarboxylase synthetase EC number 6.3.4.10 . This enzyme is important for the effective use of biotin , a B vitamin found in foods such as liver , egg yolk s, and milk . In many of the body s tissues, holocarboxylase synthetase activates other specific enzymes called biotin dependent carboxylases by attaching biotin to them. These carboxylases are involved in many critical cellular functions, including the production and breakdown of proteins, fats, and carbohydrates. Holocarboxylase synthetase may also play a role in regulating the activity of genes. In the nucleus, the enzyme likely attaches biotin molecules to histones, which are structural proteins that bind to DNA and give chromosomes their shape. Changing the shape of histones may help determine whether certain genes are turned on or off however, it is not known how adding biotin affects gene regulation. The HLCS gene is located on the long q arm of chromosome 21 human chromosome 21 at position 22.1, from base pair 37,045,059 to base pair 37,284,372. Related conditions Holocarboxylase synthetase deficiency About 30 mutation s in the HLCS gene have been identified in people with holocarboxylase synthetase deficiency. Most of these mutations substitute one amino acid a building block of proteins for another amino acid in the holocarboxylase synthetase enzyme. Many ... synthetase activity may also alter the regulation of certain genes that are important for normal ... synthetase deficiency. See also Biotinylation External links MeshName holocarboxylase synthetases Ligases ... more details
protein Name glutathione synthetase caption image width HGNCid 4624 Symbol GSS AltSymbols EntrezGene 2937 OMIM 601002 RefSeq NM 000178 UniProt P48637 PDB ECnumber 6.3.2.3 Chromosome 20 Arm q Band 11.2 LocusSupplementaryData Infobox protein family Symbol GSH synthase Name Eukaryotic glutathione synthase image PDB 2hgs EBI.jpg width caption human glutathione synthetase Pfam PF03199 Pfam clan CL0483 InterPro IPR004887 SMART PROSITE MEROPS SCOP 2hgs TCDB OPM family OPM protein CAZy CDD Infobox protein family Symbol GSH synth ATP Name Eukaryotic glutathione synthase, ATP binding domain image PDB 2hgs EBI.jpg width caption human glutathione synthetase Pfam PF03917 Pfam clan InterPro IPR005615 SMART PROSITE MEROPS SCOP 1m0t TCDB OPM family OPM protein CAZy CDD Infobox protein family Symbol GSH S N Name Prokaryotic glutathione synthetase, N terminal domain image PDB 1gsh EBI.jpg width caption structure of escherichia coli glutathione synthetase at ph 7.5 Pfam PF02951 Pfam clan InterPro IPR004215 SMART PROSITE MEROPS SCOP 1glv TCDB OPM family OPM protein CAZy CDD Infobox protein family Symbol GSH S ATP Name Prokaryotic glutathione synthetase, ATP grasp domain image PDB 1gsh EBI.jpg width caption structure of escherichia coli glutathione synthetase at ph 7.5 Pfam PF02955 Pfam clan CL0179 InterPro IPR004218 SMART PROSITE MEROPS SCOP 1glv TCDB OPM family OPM protein CAZy CDD Glutathione synthetase GSS EC 6.3.2.3 is the second enzyme in the glutathione biosynthesis pathway. It catalyses the condensation of gamma glutamylcysteine and glycine , to form glutathione. ref cite journal author Nj lsson R, Norgren S title Physiological and pathological aspects of GSH metabolism. journal Acta Paediatr volume 94 issue 2 pages 132 7 year 2005 pmid 15981742 doi 10.1080 08035250410025285 ref In eukaryotes ... Polekhina G, Board PG, Gali RR, Rossjohn J, Parker MW title Molecular basis of glutathione synthetase ... synthetase deficiency References references External links MeshName Glutathione Synthetase ligase ... more details
enzyme Name N 5 amino 5 carboxypentanoyl small L small cysteinyl small D small valine synthase EC number 6.3.2.26 CAS number 57219 73 5 IUBMB EC number 6 3 2 26 GO code 0050564 image width caption ACV synthetase ACVS , small L small aminoadipoyl small L small cysteinyl small D small valine synthetase , N 5 amino 5 carboxypentanoyl small L small cysteinyl small D small valine synthase , EC number 6.3.2.26 is an enzyme that catalysis catalyzes the chemical reaction 3 ATP small L small 2 aminohexanedioate small L small cysteine small L small valine H sub 2 sub O math rightleftharpoons math 3 AMP 3 PP sub i sub N small L small 5 amino 5 carboxypentanoyl small L small cysteinyl small D small valine The five substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , small L small 2 aminohexanedioate, small L small cysteine , small L small valine , and water H sub 2 sub O , whereas its three product chemistry products are adenosine monophosphate AMP , diphosphate , and N small L small 5 amino 5 carboxypentanoyl small L small cysteinyl small D small valine. ACVS is an example of a Nonribosomal peptide nonribosomal peptide synthetase NRPS . It participates in penicillin and cephalosporin biosyntheses. References reflist 1 cite journal author Byford MF, Baldwin JE, Shiau CY, Schofield CJ date 1997 title The Mechanism of ACV Synthetase journal Chem. Rev. volume 97 pages 2631&ndash 2650 pmid 11851475 doi 10.1021 cr960018l issue 7 cite journal author Theilgaard HB, Kristiansen KN, Henriksen CM, Nielsen J date Pt 1 title Purification and characterization of delta L alpha aminoadipyl L cysteinyl D valine synthetase from Penicillium chrysogenum journal Biochem. J. volume 327 pages 185&ndash 91 pmid 9355751 pmc 1218779 ligase stub Category EC 6.3.2 Category Enzymes of unknown structure ... more details
Expert subject Molecular and Cellular Biology date January 2009 Human phosphopantothenoylcysteine synthetase PPC synthetase is a dimer with identical monomers. PPC syththetase converts phosphopantothenate into phosphopantothenoylcysteine by combining with cysteine while using a unit of ATP. References reflist Cite journal doi 10.1016 S0969 2126 03 00146 1 journal Structure year 2003 month Aug volume 11 issue 8 pages 927 936 title Structure of human phosphopantothenoylcysteine synthetase at 2.3 A resolution author Manoj N, Strauss E, Begley TP, Ealick SE pmid 12906824 cite journal journal DNA Repair Amst year 2003 month May volume 13 2 issue 5 pages 441 53 title The enigma of endonuclease VIII author Wallace SS, Bandaru V, Kathe SD, Bond JP url http www.hprd.org alternate?protein 07760&isoform id 07760 1&isoform name Isoform 1 doi 10.1016 S1568 7864 02 00182 9 enzyme stub Category Enzymes ... more details
synthetase from Salmonella typhimurium . Cation binding sites are yellow and orange adenosine ... site of glutamine synthetase illuminates the mechanism of enzymatic inhibition journal Biochemistry ... url issn ref Pfam box Symbol Gln synt N Name Glutamine synthetase, br beta Grasp domain image width 150 caption Crystallographic structure of glutamine synthetase from salmonella typhimurium . ref name ... 2qc8 , PDB2 2ojw Pfam box Symbol Gln synt C Name Glutamine synthetase, br catalytic domain image PDB 2gls EBI.jpg width caption 12 subunit enzyme glutamine synthetase from Salmonella typhimurium . ref ... D title Refined atomic model of glutamine synthetase at 3.5 A resolution journal J. Biol. Chem ... , PDB2 2ojw protein Name glutamate ammonia ligase glutamine synthetase caption image width HGNCid ... ECnumber 6.3.1.2 Chromosome 1 Arm q Band 31 LocusSupplementaryData stack end Glutamine synthetase ... catalysts glutamine synthetase and RuBisCO journal Cold Spring Harb. Symp. Quant. Biol. volume 52 issue ... Image GS reacction.PNG center alt Glutamine Synthetase reaction. Glutamine Synthetase Catalyzed Reaction. Glutamine Synthetase uses ammonia produced by nitrate reduction, amino acid degradation, and photorespiration ... of the ammonium substrate site on glutamine synthetase, a third cation binding site journal Protein ... Feedback inhibition of fully unadenylylated glutamine synthetase from Salmonella typhimurium by glycine ... model for the reaction mechanism of glutamine synthetase, based on five crystal structures ... left alt GS Dodecamer Glutamine Synthetase 12 subunits. ref name pmid11329256 Glutamine Synthetase can ... title Glutamine Synthetase author Goodsell DS date 2002 06 work Molecule of the month publisher RCSB ... properties of the glutamine synthetase from Escherichia coli journal Biochemistry volume 9 issue ... Feedback inhibition of fully unadenylylated glutamine synthetase from Salmonella typhimurium by glycine ... A, Stadtman ER title Metal ion requirement by glutamine synthetase of Escherichia coli in catalysis ... more details
enzyme Name Phosphoribosylaminoimidazole synthetase EC number 2.1.2.2 CAS number 9032 02 4 IUBMB EC number 2 1 2 2 GO code 0004644 image width caption In the field of enzymology , phosphoribosylaminoimidazole synthetase is an enzyme that catalyzes the chemical reaction 10 formyltetrahydrofolate N1 5 phospho D ribosyl glycinamide math rightleftharpoons math tetrahydrofolic acid tetrahydrofolate N2 formyl N1 5 phospho D ribosyl glycinamide This enzyme is required for the de novo biosynthesis of purine s. References refbegin cite journal author Hartman SC, Buchanan JM title Biosynthesis of the purines. XXVI. The identification of the formyl donors of the transformylation reactions journal J. Biol. Chem. volume 234 issue 7 pages 1812 6 year 1959 month July pmid 13672969 doi url issn cite journal author Smith GK, Benkovic PA, Benkovic SJ title L 10 Formyltetrahydrofolate is the cofactor for glycinamide ribonucleotide transformylase from chicken liver journal Biochemistry volume 20 issue 14 pages 4034 6 year 1981 month July pmid 7284307 doi 10.1021 bi00517a013 url issn cite journal author Warren L, Buchanan JM title Biosynthesis of the purines. XIX. 2 Amino N ribosylacetamide 5 phosphate glycinamide ribotide transformylase journal J. Biol. Chem. volume 229 issue 2 pages 613 26 year 1957 month December pmid 13502326 doi url issn refend transferase stub Category EC 2.1.2 ja ... more details
Merge RNase PH date March 2010 enzyme Name tRNA nucleotidyltransferase EC number 2.7.7.56 CAS number 116412 36 3 IUBMB EC number 2 7 7 56 GO code 0009022 image width caption lowercase In enzymology , a tRNA nucleotidyltransferase EC number 2.7.7.56 is an enzyme that catalysis catalyzes the chemical reaction tRNA sub n 1 sub phosphate math rightleftharpoons math tRNA sub n sub a nucleoside diphosphate Thus, the two substrate biochemistry substrates of this enzyme are tRNA n 1 and phosphate , whereas its two product chemistry products are tRNA n and nucleoside diphosphate . This enzyme belongs to the family of transferase s, specifically those transferring phosphorus containing nucleotide groups nucleotidyltransferase s . The systematic name of this enzyme class is tRNA phosphate nucleotidyltransferase . Other names in common use include phosphate dependent exonuclease , RNase PH , and ribonuclease PH . Structural studies As of late 2007, 9 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1OYP , PDB link 1OYR , PDB link 1OYS , PDB link 1R6L , PDB link 1R6M , PDB link 1UDN , PDB link 1UDO , PDB link 1UDQ , and PDB link 1UDS . References reflist 1 cite journal author Cudny H, Deutscher MP date 1988 title 3 processing of tRNA precursors in ribonuclease deficient Escherichia coli. Development and characterization of an in vitro processing system and evidence for a phosphate requirement journal J. Biol. Chem. volume 263 pages 1518&ndash 23 pmid 3275667 issue 3 cite journal author Deutscher MP, Marshall GT, Cudny H date 1988 title RNase PH an Escherichia coli phosphate dependent nuclease distinct from polynucleotide phosphorylase journal Proc. Natl. Acad. Sci. U. S. A. volume 85 pages 4710&ndash 4 pmid 2455297 doi 10.1073 pnas.85.13.4710 issue 13 pmc 280505 enzyme stub Kinases Category EC 2.7.7 Category Enzymes of known structure ... more details
enzyme Name tRNA isopentenyltransferase EC number 2.5.1.8 CAS number 37277 78 4 IUBMB EC number 2 5 1 8 GO code 0004811 image width caption lowercase In enzymology , a tRNA isopentenyltransferase EC number 2.5.1.8 is an enzyme that catalysis catalyzes the chemical reaction isopentenyl diphosphate tRNA math rightleftharpoons math diphosphate tRNA containing 6 isopentenyladenosine Thus, the two substrate biochemistry substrates of this enzyme are isopentenyl diphosphate and tRNA , whereas its two product chemistry products are diphosphate and tRNA containing 6 isopentenyladenosine . This enzyme belongs to the family of transferase s, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is isopentenyl diphosphate tRNA isopentenyltransferase . Other names in common use include transfer ribonucleate isopentenyltransferase , Delta2 isopentenyl pyrophosphate tRNA Delta2 isopentenyl , transferase , Delta2 isopentenyl pyrophosphate transfer ribonucleic acid , and Delta2 isopentenyltransferase . File Isopentenyladenosine.svg thumb 200px none N sup 6 sup Isopentenyladenosine Structural studies As of late 2007, only one tertiary structure structure has been solved for this class of enzymes, with the Protein Data Bank PDB accession code PDB link 2QGN . References reflist 1 Literature cite journal author Kline LK, Fittler F, Hall RH date 1969 title N sup 6 sup sup 2 sup isopentenyl adenosine. Biosynthesis in transfer ribonucleic acid in vitro journal Biochemistry volume 8 issue 11 pages 4361 4371 pmid 4311031 doi 10.1021 bi00839a021 cite journal author Rosenbaum N, Gefter ML date 1972 title sup 2 sup Isopentenylpyrophosphate Transfer Ribonucleic Acid sup 2 sup Isopentenyltransferase from Escherichia coli . Purification and properties of the enzyme journal J. Biol. Chem. volume 247 issue 18 pages 5675 5680 pmid 4341485 transferase stub Category EC 2.5.1 Category Enzymes of known structure ... more details
enzyme Name tRNA sulfurtransferase EC number 2.8.1.4 CAS number 9055 57 6 IUBMB EC number 2 8 1 4 GO code 0016227 image width caption lowercase In enzymology , a tRNA sulfurtransferase EC number 2.8.1.4 is an enzyme that catalysis catalyzes the chemical reaction L cysteine activated tRNA math rightleftharpoons math L serine tRNA containing a thionucleotide Thus, the two substrate biochemistry substrates of this enzyme are L cysteine and activated tRNA , whereas its two product chemistry products are L serine and tRNA containing a thionucleotide . This enzyme belongs to the family of transferase s, specifically the sulfurtransferases, which transfer sulfur containing groups. The systematic name of this enzyme class is L cysteine tRNA sulfurtransferase . Other names in common use include transfer ribonucleate sulfurtransferase , RNA sulfurtransferase , ribonucleate sulfurtransferase , transfer RNA sulfurtransferase , and transfer RNA thiolase . References reflist 1 cite journal author Abrell JW, Kaufman EE, Lipsett MN date 1971 title The biosynthesis of 4 thiouridylate. Separation and purification of two enzymes in the transfer ribonucleic acid sulfurtransferase system journal J. Biol. Chem. volume 246 pages 294&ndash 301 pmid 5541999 issue 2 cite journal author Hayward RS, Weiss SB date 1966 title RNA thiolase the enzymatic transfer of sulfur from cysteine to sRNA in Escherichia coli extracts journal Proc. Natl. Acad. Sci. U. S. A. volume 55 pages 1161&ndash 8 pmid 5334200 doi 10.1073 pnas.55.5.1161 issue 5 pmc 224294 cite journal author Lipsett MN, Peterkofsky A date 1966 title Enzymatic thiolation of E. coli sRNA journal Proc. Natl. Acad. Sci. U. S. A. volume 55 pages 1169&ndash 74 pmid 5334201 doi 10.1073 pnas.55.5.1169 issue 5 pmc 224295 cite journal author Wong TW, Weiss SB, Eliceiri GL, Bryant J date 1970 title Ribonucleic acid sulfurtransferase from Bacillus subtilis W168 Sulfuration with beta mercaptopyruvate and properties of the enzyme system journal Biochemistry ... more details
enzyme Name asparagine tRNA ligase EC number 6.1.1.22 CAS number 37211 76 0 IUBMB EC number 6 1 1 22 GO code 0004816 image width caption In enzymology , an asparagine tRNA ligase EC number 6.1.1.22 is an enzyme that catalysis catalyzes the chemical reaction ATP L asparagine tRNAAsn math rightleftharpoons math AMP diphosphate L asparaginyl tRNAAsn The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , L asparagine , and tRNA Asn , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and L asparaginyl tRNA Asn . This enzyme belongs to the family of ligase s, to be specific those forming carbon oxygen bonds in aminoacyltRNA and related compounds. The systematic name of this enzyme class is L asparagine tRNAAsn ligase AMP forming . Other names in common use include asparaginyl tRNAsynthetase , asparaginyl transfer ribonucleate synthetase , asparaginyl transfer RNA synthetase , asparaginyl transfer ribonucleic acid synthetase , asparagyl transfer RNA synthetase , and asparagine translase . This enzyme participates in alanine and aspartate metabolism and aminoacyltrna biosynthesis . Structural studies As of late 2007, 3 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1X54 , PDB link 1X55 , and PDB link 1X56 . References reflist 1 cite journal author Davies MR, Marshall RD date 1972 title Partial purification of L asparaginyl tRNAsynthetase from rabbit liver journal Biochem. Biophys. Res. Commun. volume 47 pages 1386&ndash 95 pmid 5040239 doi 10.1016 0006 291X 72 90226 4 issue 6 ligase stub Ligases Category EC 6.1.1 Category Enzymes of known structure ... more details
enzyme Name glutamine tRNA ligase EC number 6.1.1.18 CAS number 9075 59 6 IUBMB EC number 6 1 1 18 GO code 0004819 image width caption In enzymology , a glutamine tRNA ligase EC number 6.1.1.18 is an enzyme that catalysis catalyzes the chemical reaction ATP L glutamine tRNAGln math rightleftharpoons math AMP diphosphate L glutaminyl tRNAGln The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , L glutamine , and tRNA Gln , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and L glutaminyl tRNA Gln . This enzyme belongs to the family of ligase s, to be specific those forming carbon oxygen bonds in aminoacyltRNA and related compounds. The systematic name of this enzyme class is L glutamine tRNAGln ligase AMP forming . Other names in common use include glutaminyl tRNAsynthetase , glutaminyl transfer RNA synthetase , glutaminyl transfer ribonucleate synthetase , glutamine tRNAsynthetase , glutamine translase , glutamate tRNA ligase , glutaminyl ribonucleic acid , and GlnRS . This enzyme participates in glutamate metabolism and aminoacyltrna biosynthesis . Structural studies As of late 2007, 15 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1EUQ , PDB link 1EUY , PDB link 1EXD , PDB link 1GSG , PDB link 1GTR , PDB link 1GTS , PDB link 1NYL , PDB link 1O0B , PDB link 1O0C , PDB link 1QRS , PDB link 1QRT , PDB link 1QRU , PDB link 1QTQ , PDB link 1ZJW , and PDB link 2HZ7 . References reflist 1 cite journal author Ravel JM, Wang S, Heinemeyer C and Shive W year 1965 title Glutamyl and glutaminyl ribonucleic acid synthetases of Escherichia coli W. Separation, properties, and stimulation of adenosine triphosphate pyrophosphate exchange by acceptor ribonucleic acid journal J. Biol. Chem. volume 240 pages 432&ndash 438 pmid 14253448 Ligases Category EC 6.1.1 Category Enzymes of known structure ligase stub ... more details
that it is involved in tRNA recognition. ref name pmid9736621 cite journal author Cavarelli J, Delagoutte B, Eriani G, Gangloff J, Moras D title L arginine recognition by yeast arginyl tRNAsynthetase ...enzyme Name arginine tRNA ligase EC number 6.1.1.19 CAS number 37205 35 9 IUBMB EC number 6 1 1 19 GO code 0004814 image width caption Infobox protein family Symbol Arg tRNA synt N Name Arginyl tRNAsynthetase N terminal domain image PDB 1bs2 EBI.jpg width caption yeast arginyl trnasynthetase Pfam PF03485 Pfam clan InterPro IPR005148 SMART PROSITE MEROPS SCOP 1f7u TCDB OPM family OPM protein CAZy CDD In enzymology , an arginine tRNA ligase EC number 6.1.1.19 is an enzyme that catalysis catalyzes the chemical reaction ATP L arginine tRNAArg math rightleftharpoons math AMP diphosphate L arginyl tRNAArg The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , L arginine , and tRNA Arg , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and L arginyl tRNA Arg . This enzyme belongs to the family of ligase s, to be specific those forming carbon oxygen bonds in aminoacyltRNA and related compounds. The systematic name of this enzyme class is L arginine tRNAArg ligase AMP forming . Other names in common use include arginyl tRNAsynthetase , arginyl transfer ribonucleate synthetase , arginyl transfer RNA synthetase , arginyl transfer ribonucleic acid synthetase , arginine tRNAsynthetase , and arginine translase . This enzyme participates in arginine and proline metabolism and aminoacyltrna biosynthesis . It contains a conserved domain at the N terminus called arginyl tRNAsynthetase N terminal domain or additional ... OF ARGINYL RIBONUCLEIC ACID SYNTHETASE FROM RAT LIVER journal J. Biol. Chem. volume 239 pages 1102 ... transfer ribonucleic acid synthetase by transfer ribonucleic acid journal J. Biol. Chem. volume ... title The arginyl transfer ribonucleic acid synthetase of Escherichia coli journal J. Biol. Chem ... more details
enzyme Name glycine tRNA ligase EC number 6.1.1.14 CAS number 9037 62 1 IUBMB EC number 6 1 1 14 GO code 0004820 image width caption Merge Glycyl tRNAsynthetase date May 2009 In enzymology , a glycine tRNA ligase EC number 6.1.1.14 is an enzyme that catalysis catalyzes the chemical reaction ATP glycine tRNAGly math rightleftharpoons math AMP diphosphate glycyl tRNAGly The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , glycine , and tRNA Gly , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and glycyl tRNA Gly . This enzyme belongs to the family of ligase s, to be specific those forming carbon oxygen bonds in aminoacyltRNA and related compounds. The systematic name of this enzyme class is glycine tRNAGly ligase AMP forming . Other names in common use include glycyl tRNAsynthetase , glycyl transfer ribonucleate synthetase , glycyl transfer RNA synthetase , glycyl transfer ribonucleic acid synthetase , and glycyl translase . This enzyme participates in glycine, serine and threonine metabolism and aminoacyltrna biosynthesis . Structural studies As of late 2007, 8 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1ATI , PDB link 1B76 , PDB link 1GGM , PDB link 1J5W , PDB link 2PME , PDB link 2PMF , PDB link 2Q5H , and PDB link 2Q5I . See also Glycyl tRNAsynthetase References reflist 1 cite journal author FRASER MJ date 1963 title Glycyl RNA synthetase of rat liver partial purification and effects of some metal ions on its activity journal Can. J. Biochem. Physiol. volume 41 pages 1123&ndash 33 pmid 13959340 cite journal author Niyomporn B, Dahl JL, Strominger JL date 1968 title Biosynthesis of the peptidoglycan of bacterial cell walls. IX Purification and properties of glycyl transfer ribonucleic acid synthetase from Staphylococcus aureus journal J. Biol. Chem. volume 243 pages 773&ndash 8 pmid 4295604 issue 4 Ligases ... more details
enzyme Name cysteine tRNA ligase EC number 6.1.1.16 CAS number 37318 56 2 IUBMB EC number 6 1 1 16 GO code 0004817 image width caption In enzymology , a cysteine tRNA ligase EC number 6.1.1.16 is an enzyme that catalysis catalyzes the chemical reaction ATP L cysteine tRNACys math rightleftharpoons math AMP diphosphate L cysteinyl tRNACys The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , L cysteine , and tRNA Cys , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and L cysteinyl tRNA Cys . This enzyme belongs to the family of ligase s, to be specific those forming carbon oxygen bonds in aminoacyltRNA and related compounds. The systematic name of this enzyme class is L cysteine tRNACys ligase AMP forming . Other names in common use include cysteinyl tRNAsynthetase , cysteinyl transferRNA synthetase , cysteinyl transfer ribonucleate synthetase , and cysteine translase . This enzyme participates in cysteine metabolism and aminoacyltrna biosynthesis . Structural studies As of late 2007, 3 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1LI5 , PDB link 1LI7 , and PDB link 1U0B . References reflist 1 cite journal author McCorquodale DJ year 1964 title The separation and partial purification of aminoacyl RNA synthetases from Escherichia coli journal Biochim. Biophys. Acta volume 91 pages 541&ndash 548 pmid 14262440 Ligases Category EC 6.1.1 Category Enzymes of known structure ligase stub ... more details
enzyme Name alanine tRNA ligase EC number 6.1.1.7 CAS number 9031 71 4 IUBMB EC number 6 1 1 7 GO code 0004813 image width caption In enzymology , an alanine tRNA ligase EC number 6.1.1.7 is an enzyme that catalysis catalyzes the chemical reaction ATP L alanine tRNAAla math rightleftharpoons math AMP diphosphate L alanyl tRNAAla The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , L alanine , and tRNA Ala , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and L alanyl tRNA Ala . This enzyme belongs to the family of ligase s, to be specific those forming carbon oxygen bonds in aminoacyltRNA and related compounds. The systematic name of this enzyme class is L alanine tRNAAla ligase AMP forming . Other names in common use include alanyl tRNAsynthetase , alanyl transfer ribonucleate synthetase , alanyl transfer RNA synthetase , alanyl transfer ribonucleic acid synthetase , alanine transfer RNA ligase , alanine transfer RNA synthetase , alanine tRNAsynthetase , alanine translase , alanyl transfer ribonucleate synthase , AlaRS , and Ala tRNAsynthetase . This enzyme participates in alanine and aspartate metabolism and aminoacyltrna biosynthesis . See also Sticky mouse mutation in the gene Structural studies As of late 2007, 7 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1RIQ , PDB link 1V4P , PDB link 1YFR , PDB link 1YFS , PDB link 1YFT , PDB link 1YGB , and PDB link 2E1B . References reflist 1 cite journal author HOLLEY RW, GOLDSTEIN J date 1959 title An alanine dependent, ribonuclease inhibited conversion of adenosine 5 phosphate to adenosine triphosphate. II. Reconstruction of the system from purified components journal J. Biol. Chem. volume 234 pages 1765&ndash 8 pmid 13672960 issue 7 cite journal author Webster GC date 1961 title Isolation of an alanine activating enzyme from pig liver journal Biochim. Biophys ... more details
tRNAsynthetase , phenylalanyl transfer ribonucleate synthetase , phenylalanine tRNAsynthetase , phenylalanyl transfer RNA synthetase , phenylalanyl tRNA ligase , phenylalanyl transfer RNA ligase , L phenylalanyl tRNAsynthetase , and phenylalanine translase . This enzyme participates in phenylalanine, tyrosine and tryptophan biosynthesis and aminoacyltrna biosynthesis . Phenylalanine tRNAsynthetase PheRS is known to be among the most complex enzyme s of the aaRS AminoacyltRNAsynthetase ... , and tRNA Phe , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and L phenylalanyl tRNA Phe . This enzyme belongs to the family of ligase s, to be specific those forming carbon oxygen bonds in aminoacyltRNA and related compounds. The systematic name of this enzyme ... L, Reshetnikova L, Goldgur Y, Delarue M, Safro MG title Structure of phenylalanyl tRNAsynthetase ... tRNAsynthetase from thermus thermophilus complexed with cognate tRNAPhe journal Structure ... cite journal author Rodova M, Ankilova V, Safro MG title Human phenylalanyl tRNAsynthetase cloning ... cite journal author Klipcan L, Levin I, Kessler N, Moor N, Finarov I, Safro M title The tRNA induced conformational activation of human mitochondrial phenylalanyl tRNAsynthetase journal Structure ...enzyme Name phenylalanine tRNA ligase EC number 6.1.1.20 CAS number 9055 66 7 IUBMB EC number 6 1 1 20 ... binding domain image PDB 1eiy EBI.jpg width caption the crystal structure of phenylalanyl trnasynthetase from thermus thermophilus complexed with cognate trnaphe Pfam PF03147 Pfam clan InterPro ... tRNA ligase EC number 6.1.1.20 is an enzyme that catalysis catalyzes the chemical reaction ... O, Favre A, Safro M title Prokaryotic and eukaryotic tetrameric phenylalanyl tRNA synthetases display conservation of the binding mode of the tRNA Phe CCA end journal Biochemistry volume 42 issue 36 pages ... MP year 1967 title The isolation and properties of phenylalanyl ribonucleic acid synthetase from ... more details
enzyme Name aspartate tRNA ligase EC number 6.1.1.12 CAS number 9027 32 1 IUBMB EC number 6 1 1 12 GO code 0004815 image width caption In enzymology , an aspartate tRNA ligase EC number 6.1.1.12 is an enzyme that catalysis catalyzes the chemical reaction ATP L aspartate tRNAAsp math rightleftharpoons math AMP diphosphate L aspartyl tRNAAsp The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , L aspartate , and tRNA Asp , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and L aspartyl tRNA Asp . This enzyme belongs to the family of ligase s, to be specific those forming carbon oxygen bonds in aminoacyltRNA and related compounds. The systematic name of this enzyme class is L aspartate tRNAAsp ligase AMP forming . Other names in common use include aspartyl tRNAsynthetase , aspartyl ribonucleic synthetase , aspartyl transfer RNA synthetase , aspartic acid translase , aspartyl transfer ribonucleic acid synthetase , and aspartyl ribonucleate synthetase . This enzyme participates in alanine and aspartate metabolism and aminoacyltrna biosynthesis . Structural studies As of late 2007, 10 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1ASY , PDB link 1ASZ , PDB link 1B8A , PDB link 1C0A , PDB link 1EFW , PDB link 1EOV , PDB link 1EQR , PDB link 1G51 , PDB link 1IL2 , and PDB link 1L0W . See also DARS gene References reflist 1 cite journal author Gangloff J, Dirheimer G date 1973 title Studies on aspartyl tRNAsynthetase from Baker s yeast. I Purification and properties of the enzyme journal Biochim. Biophys. Acta. volume 294 pages 263&ndash 72 pmid 4575961 issue 1 cite journal author NORTON SJ, RAVEL JM, LEE C, SHIVE W date 1963 title Purification and properties of the aspartyl ribonucleic acid synthetase of Lactobacillus arabinosus journal J. Biol. Chem. volume 238 pages 269&ndash 74 pmid 13939000 Ligases Category EC 6.1.1 ... more details
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