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 ... to be improperly 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 ... syntet za de AminoacyltRNASynthetase es Aminoacil ARNt sintetasa fr Aminoacyl ARNt synth tase gl ... 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 ... 2007 08 18 work ref AminoacyltRNA synthetases, class I Class I has two highly conserved sequence motifs ... or protein dimer dimeric one or two subunits, respectively . AminoacyltRNA synthetases, class II ..., respectively . 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 ... accessdate 2007 08 18 work ref that cleave incorrectly paired aminoacyltRNA molecules. The catalytic ... L, Grishin NV, Koonin EV title Evolution of aminoacyltRNA synthetases analysis of unique domain ... and Molecular 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 ... binding it. By mutating aminoacyltRNA synthetases, chemists have expanded the genetic codes of various ... icaars ICAARS B. Pawar, and GPS Raghava 2010 Prediction and classification of aminoacyltRNA synthetases ... 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 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. is a protein domain that catalyse s the attachment of an amino acid to its cognate transfer RNA molecule in a highly specific two step reaction. This protein differs widely in size and oligomeric state, and has a 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 ... Delarue M, Moras D title The aminoacyltRNAsynthetase family modules at work journal Bioessays volume ... 347203a0 ref The 20 aminoacyltRNA synthetases are divided into two classes, I and II. Class I aminoacyltRNA synthetases contain a characteristic Rossman fold catalytic domain and are mostly monomeric ... of Thermus thermophilus methionyl tRNAsynthetase reveals two RNA binding modules journal Structure ... II aminoacyltRNA synthetases share an anti parallel beta sheet fold flanked by alpha helices, ref ... RNA aminoacylation by Escherichia coli glutaminyl tRNAsynthetase journal Biochemistry volume 32 ... cite journal author Schimmel P title Classes of aminoacyltRNA synthetases and the establishment ..., Hartlein M title Sequence, structural and evolutionary relationships between class 2 aminoacyltRNA ... 10.1093 nar 19.13.3489 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 ... name PUB00015156 cite journal author Bairoch A title List of aminoacyltRNA synthetases journal volume ... NARS gene NARS NARS2 References reflist InterPro content IPR004364 DEFAULTSORT AminoacylTrna Synthetases ... 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
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 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
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
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 histidine tRNA ligase EC number 6.1.1.21 CAS number 9068 78 4 IUBMB EC number 6 1 1 21 GO code 0004821 image width caption In enzymology , a histidine tRNA ligase EC number 6.1.1.21 is an enzyme that catalysis catalyzes the chemical reaction ATP L histidine tRNAHis math rightleftharpoons math AMP diphosphate L histidyl tRNAHis The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , L histidine , and tRNA His , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and L histidyl tRNA His . 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 histidine tRNAHis ligase AMP forming . Other names in common use include histidyl tRNAsynthetase , histidyl transfer ribonucleate synthetase , and histidine translase . This enzyme participates in histidine metabolism and aminoacyltrna biosynthesis . 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 1ADJ , PDB link 1ADY , PDB link 1H4V , PDB link 1HTT , PDB link 1KMM , PDB link 1KMN , PDB link 1QE0 , PDB link 1WU7 , and PDB link 1X59 . See also Anti Jo1 References reflist 1 cite journal author von Tigerstrom M, Tener GM date 1967 title Histidyl transfer ribonucleic acid synthetase from bakers yeast journal Can. J. Biochem. volume 45 pages 1067&ndash 74 pmid 6035970 issue 7 ligase stub Ligases CO CS and CN Category EC 6.1.1 Category Enzymes of known structure ... 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
Infobox protein family Symbol polyprenyl synt Name polyprenyl synt image PDB 1rqi EBI.jpg width caption active conformation of farnesyl pyrophosphate synthase bound to isopentyl pyrophosphate and dimethylallyl s thiolodiphosphate Pfam PF00348 Pfam clan InterPro IPR000092 SMART PROSITE PDOC00407 MEROPS SCOP 1fps TCDB OPM family 38 OPM protein 1rqj CAZy CDD Polyprenyl synthetases are a class of enzymes responsible for synthesis of isoprenoid s. Isoprenoid compounds are synthesized by various organisms. For example in eukaryotes the isoprenoid biosynthetic pathway is responsible for the synthesis of a variety of end product chemistry product s including cholesterol , dolichol , ubiquinone or coenzyme Q . In bacteria this pathway leads to the synthesis of isopentenyl tRNA , isoprenoid quinone s, and sugar carrier lipids . Among the enzymes that participate in that pathway, are a number of polyprenyl synthetase enzymes which catalyze a 1 4 condensation between 5 carbon isoprene units. It has been shown ref name pmid2198286 cite journal author Ashby MN, Edwards PA title Elucidation of the deficiency in two yeast coenzyme Q mutants. Characterization of the structural gene encoding hexaprenyl pyrophosphate synthetase journal J. Biol. Chem. volume 265 issue 22 pages 13157 64 year 1990 month August pmid 2198286 doi url ref ref name pmid2089044 cite journal author Fujisaki S, Hara H, Nishimura Y, Horiuchi K, Nishino T title Cloning and nucleotide sequence of the ispA gene responsible for farnesyl diphosphate synthase activity in Escherichia coli journal J. Biochem. volume 108 issue 6 pages 995 1000 year 1990 month December pmid 2089044 doi url ref ref name pmid1826006 cite journal author Carattoli A, Romano N, Ballario P, Morelli G, Macino G title The Neurospora crassa carotenoid biosynthetic gene albino 3 reveals highly conserved regions among prenyltransferases journal J. Biol. Chem. volume 266 issue 9 pages 5854 9 year 1991 month March pmid 1826006 doi url ref ref name pmid ... 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
enzyme Name glutamate tRNA Gln ligase EC number 6.1.1.24 CAS number 9068 76 2 IUBMB EC number 6 1 1 24 GO code 0050561 image width caption In enzymology , a glutamate tRNAGln ligase EC number 6.1.1.24 is an enzyme that catalysis catalyzes the chemical reaction ATP L glutamate tRNAGlx math rightleftharpoons math AMP diphosphate glutamyl tRNAGlx The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , L glutamate , and tRNAGlx , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and glutamyl tRNAGlx . 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 glutamate tRNAGlx ligase AMP forming . This enzyme is also called glutamyl tRNAsynthetase . This enzyme participates in glutamate metabolism . References reflist 1 cite journal author Ibba M, Soll D year 2000 title AminoacyltRNA synthesis journal Annu. Rev. Biochem. volume 69 pages 617&ndash 50 pmid 10966471 doi 10.1146 annurev.biochem.69.1.617 cite journal author Schmitt E, Moulinier L, Fujiwara S, Imanaka T, Thierry JC, Moras D year 1998 title Crystal structure of aspartyl tRNAsynthetase from Pyrococcus kodakaraensis KOD archaeon specificity and catalytic mechanism of adenylate formation journal EMBO J. volume 17 pages 5227&ndash 37 pmid 9724658 doi 10.1093 emboj 17.17.5227 issue 17 pmc 1170850 cite journal author Kim SI, Soll D year 1998 title Major identity element of glutamine tRNAs from Bacillus subtilis and Escherichia coli in the reaction with B. subtilis glutamyl tRNAsynthetase journal Mol. Cells. volume 8 pages 459&ndash 65 pmid 9749534 issue 4 Ligases Category EC 6.1.1 Category Enzymes of unknown structure ligase stub ... 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
enzyme Name proline tRNA ligase EC number 6.1.1.15 CAS number 9055 68 9 IUBMB EC number 6 1 1 15 GO code 0004827 image width caption In enzymology , a proline tRNA ligase EC number 6.1.1.15 is an enzyme that catalysis catalyzes the chemical reaction ATP L proline tRNAPro math rightleftharpoons math AMP diphosphate L prolyl tRNAPro The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , L proline , and tRNA Pro , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and L prolyl tRNA Pro . 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 proline tRNAPro ligase AMP forming . Other names in common use include prolyl tRNAsynthetase , prolyl transferRNA synthetase , prolyl transfer ribonucleate synthetase , proline translase , prolyl transfer ribonucleic acid synthetase , prolyl s RNA synthetase , and prolinyl tRNA ligase . This enzyme participates in arginine and proline 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 1H4Q , PDB link 1H4S , PDB link 1H4T , PDB link 1HC7 , PDB link 1NJ1 , PDB link 1NJ2 , PDB link 1NJ5 , PDB link 1NJ6 , PDB link 1NJ8 , PDB link 2I4L , PDB link 2I4M , PDB link 2I4N , PDB link 2I4O , PDB link 2J3L , and PDB link 2J3M . References reflist 1 cite journal author Norton SJ date 1964 title Purification and properties of the prolyl RNA synthetase of Escherichia coli journal Arch. Biochem. Biophys. volume 106 pages 147&ndash 152 doi 10.1016 0003 9861 64 90167 5 pmid 14217147 cite journal author Peterson PJ and Fowden L date 1965 title Purification, properties and comparative specificities of the enzyme prolyl transfer ribonucleic acid synthetase from Phaseolus aureus and Polygonatum multiflorum ... more details
enzyme Name threonine tRNA ligase EC number 6.1.1.3 CAS number 9023 46 5 IUBMB EC number 6 1 1 3 GO code 0004829 image width caption In enzymology , a threonine tRNA ligase EC number 6.1.1.3 is an enzyme that catalysis catalyzes the chemical reaction ATP L threonine tRNAThr math rightleftharpoons math AMP diphosphate L threonyl tRNAThr The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , L threonine , and tRNA Thr , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and L threonyl tRNA Thr . 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 threonine tRNAThr ligase AMP forming . Other names in common use include threonyl tRNAsynthetase , threonyl transfer ribonucleate synthetase , threonyl transfer RNA synthetase , threonyl transfer ribonucleic acid synthetase , threonyl ribonucleic synthetase , threonine transfer ribonucleate synthetase , threonine translase , threonyl tRNAsynthetase , and TRS . This enzyme participates in glycine, serine and threonine metabolism and aminoacyltrna biosynthesis . Structural studies As of late 2007, 17 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1EVK , PDB link 1EVL , PDB link 1FYF , PDB link 1KOG , PDB link 1NYQ , PDB link 1NYR , PDB link 1QF6 , PDB link 1TJE , PDB link 1TKE , PDB link 1TKG , PDB link 1TKY , PDB link 1WWT , PDB link 1Y2Q , PDB link 2HKZ , PDB link 2HL0 , PDB link 2HL1 , and PDB link 2HL2 . References reflist 1 cite journal author ALLEN EH, GLASSMAN E, SCHWEET RS date 1960 title Incorporation of amino acids into ribonucleic acid. I. The role of activating enzymes journal J. Biol. Chem. volume 235 pages 1061&ndash 7 pmid 13792726 cite journal author HOLLEY RW, BRUNNGRABER EF, SAAD F, WILLIAMS HH date 1961 title Partial purification of the threonine ... more details
enzyme Name leucine tRNA ligase EC number 6.1.1.4 CAS number 9031 15 6 IUBMB EC number 6 1 1 4 GO code 0004823 image width caption In enzymology , a leucine tRNA ligase EC number 6.1.1.4 is an enzyme that catalysis catalyzes the chemical reaction ATP L leucine tRNALeu math rightleftharpoons math AMP diphosphate L leucyl tRNALeu The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , L leucine , and tRNA Leu , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and L leucyl tRNA Leu . 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 leucine tRNALeu ligase AMP forming . Other names in common use include leucyl tRNAsynthetase , leucyl transfer ribonucleate synthetase , leucyl transfer RNA synthetase , leucyl transfer ribonucleic acid synthetase , leucine tRNAsynthetase , and leucine translase . This enzyme participates in valine, leucine and isoleucine biosynthesis and aminoacyltrna biosynthesis . Structural studies As of late 2007, 5 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1WKB , PDB link 1WZ2 , PDB link 2AJG , PDB link 2AJH , and PDB link 2AJI . See also Leucyl tRNAsynthetase References reflist 1 cite journal author ALLEN EH, GLASSMAN E, SCHWEET RS date 1960 title Incorporation of amino acids into ribonucleic acid. I. The role of activating enzymes journal J. Biol. Chem. volume 235 pages 1061&ndash 7 pmid 13792726 cite journal author Berg P, Bergmann FH, Ofengand EJ and Dieckmann M date 1961 title The enzymic synthesis of amino acyl derivatives of ribonucleic acid I. The mechanism of leucyl , valyl , isoleucyl and methionyl ribonucleic acid formation journal J. Biol. Chem. volume 236 pages 1726&ndash 1734 cite journal author Bergmann FH, Berg P and Dieckmann M date 1961 title The enzymic ... more details
tRNA and serine tRNA are aminoacylated by the same synthetase, but may manifest different identities ...enzyme Name serine tRNA ligase EC number 6.1.1.11 CAS number 9023 48 7 IUBMB EC number 6 1 1 11 GO code 0004828 image width caption In enzymology , a serine tRNA ligase EC number 6.1.1.11 is an enzyme that catalysis catalyzes the chemical reaction ATP L serine tRNASer math rightleftharpoons math AMP diphosphate L seryl tRNASer The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , L serine , and tRNA Ser , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and L seryl tRNA Ser . 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 serine tRNASer ligase AMP forming . Other names in common use include seryl tRNAsynthetase , SerRS , seryl transfer ribonucleate synthetase , seryl transfer RNA synthetase , seryl transfer ribonucleic acid synthetase , and serine translase . This enzyme participates in glycine, serine and threonine metabolism and aminoacyltrna biosynthesis . Structural studies As of late 2007, 13 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1SER , PDB link 1SES , PDB link 1SET , PDB link 1SRY , PDB link 1WLE , PDB link 2CIM , PDB link 2CJ9 , PDB link 2CJA , PDB link 2CJB , PDB link 2DQ0 , PDB link 2DQ1 , PDB link 2DQ2 , and PDB link 2DQ3 . References reflist 1 cite journal author Katze JR, Konigsberg W date 1970 title Purification and properties of seryl transfer ribonucleic acid synthetase from Escherichia coli journal J. Biol. Chem. volume 245 pages 923&ndash 30 pmid 4906848 issue 5 cite journal author Makman MH and Cantoni GL date 1965 title Isolation of seryl and phenylalanyl ribonucleic acid synthetases from baker s yeast journal Biochemistry volume 4 pages 1434&ndash 1442 doi ... 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
enzyme Name tryptophan tRNA ligase EC number 6.1.1.2 CAS number 9023 44 3 IUBMB EC number 6 1 1 2 GO code 0004830 image width caption In enzymology , a tryptophan tRNA ligase EC number 6.1.1.2 is an enzyme that catalysis catalyzes the chemical reaction ATP L tryptophan tRNATrp math rightleftharpoons math AMP diphosphate L tryptophyl tRNATrp The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , L tryptophan , and tRNA Trp , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and L tryptophyl tRNATrp . 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 tryptophan tRNATrp ligase AMP forming . Other names in common use include tryptophanyl tRNAsynthetase , L tryptophan tRNATrp ligase AMP forming , tryptophanyl transfer ribonucleate synthetase , tryptophanyl transfer ribonucleic acid synthetase , tryptophanyl transfer RNA synthetase , tryptophanyl ribonucleic synthetase , tryptophanyl transfer ribonucleic synthetase , tryptophanyl tRNA synthase , tryptophan translase , and TrpRS . This enzyme participates in tryptophan metabolism and aminoacyltrna biosynthesis . Structural studies As of late 2007, 21 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1D2R , PDB link 1I6K , PDB link 1I6L , PDB link 1I6M , PDB link 1M83 , PDB link 1MAU , PDB link 1MAW , PDB link 1MB2 , PDB link 1O5T , PDB link 1R6T , PDB link 1R6U , PDB link 1ULH , PDB link 1YIA , PDB link 1YID , PDB link 2A4M , PDB link 2AKE , PDB link 2AZX , PDB link 2DR2 , PDB link 2G36 , PDB link 2IP1 , and PDB link 2OV4 . References reflist 1 cite journal author DAVIE EW, KONINGSBERGER VV, LIPMANN F date 1956 title The isolation of a tryptophan activating ... transfer ribonucleic acid synthetase from bovine pancreas. II. The chemically different subunits ... more details
enzyme Name methionyl tRNA formyltransferase EC number 2.1.2.9 CAS number 9015 76 3 IUBMB EC number 2 1 2 9 GO code 0004479 image width caption In enzymology , a methionyl tRNA formyltransferase EC number 2.1.2.9 is an enzyme that catalysis catalyzes the chemical reaction 10 formyltetrahydrofolate small L small methionyl tRNA sup fMet sup H sub 2 sub O math rightleftharpoons math tetrahydrofolate N formylmethionyl tRNA sup fMet sup The 3 substrate biochemistry substrates of this enzyme are 10 formyltetrahydrofolate , fMet small L small methionyl tRNA sup fMet sup , and water H sub 2 sub O , whereas its two product chemistry products are tetrahydrofolate and fMet N formylmethionyl tRNA sup fMet sup . This enzyme belongs to the family of transferase s that transfer one carbon groups, specifically the hydroxymethyl , formyl and related transferases. The systematic name of this enzyme class is 10 formyltetrahydrofolate L methionyl tRNA N formyltransferase . Other names in common use include N10 formyltetrahydrofolic methionyl transfer ribonucleic , transformylase , formylmethionyl transfer ribonucleic synthetase , methionyl ribonucleic formyltransferase , methionyl tRNA Met formyltransferase , methionyl tRNA transformylase , methionyl transfer RNA transformylase , methionyl transfer ribonucleate methyltransferase , and methionyl transfer ribonucleic transformylase . This enzyme participates in 3 metabolism metabolic pathways methionine metabolism , one carbon pool by folate , and aminoacyltRNA biosynthesis . Structural studies As of late 2007, two tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1FMT and PDB link 2FMT . References reflist 1 cite journal author Dickerman HW, Steers E Jr, Redfield BG, Weissbach H date 1967 title Methionyl soluble ribonucleic acid transformylase. I. Purification and partial ... transferase stub Category EC 2.1.2 Category Enzymes of known structure it Metionil tRNA formiltransferasi ... more details
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