The Peptidyltransferase is an Aminoacyltransferases aminoacyltransferase EC number 2.3.2.12 as well as the primary enzymatic function of the ribosome , which forms peptide links between adjacent amino acids using tRNA s during the Translation genetics translation process of protein biosynthesis . Peptidyltransferase activity is carried out by the ribosome. Peptidyltransferase activity is not mediated by any ribosomal proteins but by ribosomal RNA rRNA , a ribozyme. This RNA relic is the most significant piece of evidence supporting the RNA World hypothesis. In Bacteria , the 50S 23S component ribosome subunit contains the peptidyltransferase component and acts as a ribozyme. In eukaryotic cells , the 60S 28S component ribosome subunit contains the peptidyltransferase component and acts as the ribozyme. Peptidyl transferases are not limited to translation, but there are relatively few enzymes with this function. Antibiotic target The following protein synthesis inhibitor s target peptidyltransferase Chloramphenicol binds ref name pmid7515506 cite journal author Gu Z, Harrod R, Rogers EJ, Lovett PS title Anti peptidyltransferase leader peptides of attenuation regulated chloramphenicol resistance genes journal Proc. Natl. Acad. Sci. U.S.A. volume 91 issue 12 pages 5612 6 year 1994 month June pmid 7515506 pmc 44046 doi 10.1073 pnas.91.12.5612 url ref to A2451 and A2452 residues ... to peptidyltransferase. ref cite journal last Long first Katherine S title Interaction of Pleuromutilin Derivatives with the Ribosomal PeptidylTransferase Center journal Antimicrobial Agents and Chemotherapy ... Hansen last3 Jakobsen last4 Vester ref Macrolide antibiotics are thought to inhibit peptidyltransferase ... ref See also Transferase Translation genetics Translation Enzyme References reflist External links MeshName Peptidyl transferases Acyltransferases GeneticTranslation Category Transferases Enzyme stub ca Peptidil transferasa de Peptidyltransferase es Peptidil transferasa fr Peptidyl transf rase ... more details
enzyme Name peptidyl glutaminase EC number 3.5.1.43 CAS number 37228 70 9 IUBMB EC number 3 5 1 43 GO code 0050170 image width caption In enzymology , a peptidyl glutaminase EC number 3.5.1.43 is an enzyme that catalysis catalyzes the chemical reaction alpha N peptidyl L glutamine H sub 2 sub O math rightleftharpoons math alpha N peptidyl L glutamate NH sub 3 sub Thus, the two substrate biochemistry substrates of this enzyme are alpha N peptidyl L glutamine and water H sub 2 sub O , whereas its two product chemistry products are alpha N peptidyl L glutamate and ammonia NH sub 3 sub . This enzyme belongs to the family of hydrolase s, those acting on carbon nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is peptidyl L glutamine amidohydrolase . Other names in common use include peptidoglutaminase I , peptideglutaminase , and peptidoglutaminase . References reflist 1 cite journal author Kikuchi M, Hayashida H, Nakano E, Sakaguchi K date 1971 title Peptidoglutaminase. Enzymes for selective deamidation of gamma amide of peptide bound glutamine journal Biochemistry. volume 10 pages 1222&ndash 9 pmid 4928623 doi 10.1021 bi00783a019 issue 7 hydrolase stub Category EC 3.5.1 Category Enzymes of unknown structure ... more details
In biochemistry , a transferase is an enzyme that catalyzes the transfer of a functional group e.g., a methyl or phosphate group from one molecule called the donor to another called the acceptor . For example, an enzyme that catalyzed this reaction would be a transferase A&ndash X B &rarr A B&ndash X In this example, A would be the donor, and B would be the acceptor. The donor is often a coenzyme . Nomenclature Proper names of transferases are formed as donor acceptor grouptransferase. However, other names are much more common. The common names of transferases are often formed as acceptor grouptransferase or donor grouptransferase. For example, a DNA methyltransferase is a transferase that catalyzes the transfer of a methyl group to a DNA acceptor. Classification Transferases are classified as EC 2 in the Enzyme Commission number EC number classification. Transferases can be further classified into nine subclasses Category EC 2.1 EC 2.1 includes enzymes that transfer one carbon groups methyltransferase Category EC 2.2 EC 2.2 includes enzymes that transfer aldehyde or ketone groups Category EC 2.3 EC 2.3 includes acyltransferase s Category EC 2.4 EC 2.4 includes glycosyltransferase s Category EC 2.5 EC 2.5 includes enzymes that transfer alkyl or aryl groups, other than methyl groups Category EC 2.6 EC 2.6 includes enzymes that transfer nitrogenous groups transaminase Category EC 2.7 EC 2.7 includes enzymes that transfer phosphorus containing groups phosphotransferase , including polymerase and kinase Category EC 2.8 EC 2.8 includes enzymes that transfer sulfur containing groups sulfurtransferase and sulfotransferase Category EC 2.9 EC 2.9 includes enzymes that transfer selenium ... Transferases ar bg ca Transferasa cs Transfer za da Transferase de Transferase es Transferasa fr Transf rase gl Transferase it Transferasi he lt Transferaz s nl Transferase ja pl Transferazy pt Transferase ro Transferaz ru sr Transferaza sv Transferaser ... more details
Expert subject Molecular and Cellular Biology date November 2008 enzyme Name Glutathione S transferase ... width caption Crystallographic structure of glutathione S transferase from Taxonomy of Anopheles ... and structure of a new Delta class glutathione transferase isoenzyme journal Biochem. J ... url ref Enzymes of the glutathione S transferase GST family are composed of many cytosolic , mitochondrial ... AJ title Identification, characterization and structure of a new Delta class glutathione transferase ... lipids, ref name Leaver 1998 Cite journal title A piscine glutathione S transferase ... IM, Jakoby WB title The Identity of Glutathione S Transferase B with Ligandin, a Major Binding ... name Beckett 1987 Cite journal title Glutathione S transferase measurements and liver disease in man ... GJ, Hayes JD doi 10.3164 jcbn.2.1 ref GST Family members Across species, the glutathione S transferase ... Homo sapiens GST Class Members 22 Max All Species Alpha Glutathione S transferase A1 GSTA1 , GSTA2 ... style padding left 2em GSTK2 Mu Glutathione S transferase Mu 1 GSTM1 , GSTM1L RNAi , GSTM2 , GSTM3 ... style padding left 2em MGST3 Structure Infobox protein family Symbol GST C Name Glutathione S transferase ... binding site of rat glutathione S transferase mu 1 bound to the GSH adduct of phenanthrene 9,10 ... binding site of a glutathione S transferase as revealed by X ray crystallographic analysis of product .... GST tags and the GST pull down assay Genetic engineers have used glutathione S transferase to create ... the GST protein in solution. Role in disease Genetic polymorphisms in glutathione S transferase and its ... 10.1007 s11670 010 0087 7 ref See also Maltose binding protein Glutathione S transferase, C terminal domain Bacterial glutathione transferase Affinity chromatography References Reflist External links ... 199 MAPEG Eicosanoid and Glutathione metabolism proteins family MeshName Glutathione S Transferase ... of GST Fusion Proteins Alkyl and aryl transferases Category Transferases de Glutathion S Transferase ... more details
Guanylyl transferases are enzyme s that transfer a guanosine monophosphate GMP also known as guanylic acid group, usually from Guanosine triphosphate GTP to another molecule, releasing pyrophosphate . Many eukaryote eukaryotic guanylyl transferases are capping enzyme s that catalyze the formation of the 5 cap in the co transcriptional modification of messenger RNA . Because the 5 end of the RNA molecule ends in a phosphate group, the bond formed between the RNA and the GTP molecule is an unusual 5 5 triphosphate linkage, instead of the 3 5 linkages between the other nucleotides that form an RNA strand. In capping enzymes, a highly conserved lysine residue serves as the catalytic residue that forms a covalent enzyme GMP complex. ref name Fresco Fresco LD, Buratowski S. 1994 . Active site of the mRNA capping enzyme guanylyltransferase from Saccharomyces cerevisiae similarity to the nucleotidyl attachment motif of DNA and RNA ligases. Proc Natl Acad Sci USA 91 14 6624 6628. ref The transfer RNA tRNA for histidine is unique among eukaryotic tRNAs in requiring the addition of a guanine nucleotide before being aminoacylation aminoacylated by the histidine aminoacyl tRNA synthetase tRNA synthetase . The yeast guanylyl transferase specific to tRNA sup His sup is unique in being the only known non tRNA synthetase enzyme that specifically recognizes the tRNA anticodon . ref name Jackman Jackman JE, Phizicky EM. 2006 . tRNAHis guanylyltransferase adds G 1 to the 5 end of tRNAHis by recognition of the anticodon, one of several features unexpectedly shared with tRNA synthetases. RNA 12 1007 1014. ref Guanylyl transferases also exist for transferring guanosine nucleotides to sugar molecules, such as mannose and fucose . See also mRNA guanylyltransferase External links http www.expasy.org enzyme 2.7.7. EC number 2.7.7. nucleotidyltransferases References reflist transferase stub Kinases Category EC 2.7.7 ... more details
Peptidyl glutamyl peptide hydrolyzing PGPH enzyme activity is a means of proteolysis that cleaves peptide bond s in protein s immediately after acid ic or branched chain amino acid s. One of the three catalysis catalytic Protein subunit subunit s of the proteasome has PGPH activity and is strongly inhibited by the proteasome inhibitor epoxomicin . ref name Meng Meng L, Mohan R, Kwok BHB, Elofsson M, Sin N, Crews CM. 1999 . Epoxomicin, a potent and selective proteasome inhibitor, exhibits in vivo antiinflammatory activity. Proc Natl Acad Sci USA 96 18 10403 10408. ref References references External links http db.yeastgenome.org cgi bin GO go.pl?goid 45024 Gene Ontology entry hydrolase stub Category Posttranslational modification Category Metabolism Category EC 3.4 ... more details
enzyme Name propionate CoA transferase EC number 2.8.3.1 CAS number 9026 15 7 IUBMB EC number 2 8 3 1 GO code 0018729 image width caption In enzymology , a propionate CoA transferase EC number 2.8.3.1 is an enzyme that catalysis catalyzes the chemical reaction acetyl CoA propanoate math rightleftharpoons math acetate propanoyl CoA Thus, the two substrate biochemistry substrates of this enzyme are acetyl CoA and propanoate , whereas its two product chemistry products are acetate and propanoyl CoA . This enzyme belongs to the family of transferase s, specifically the CoA transferases. The systematic name of this enzyme class is acetyl CoA propanoate CoA transferase . Other names in common use include propionate coenzyme A transferase , propionate CoA lactoyl CoA transferase , propionyl CoA acetate CoA transferase , and propionyl CoA transferase . This enzyme participates in 3 metabolism metabolic pathways pyruvate metabolism , propanoate metabolism , and styrene degradation . References reflist 1 cite journal author Stadtman ER date 1952 title Acyl coenzyme A synthesis by phosphotransacetylase and coenzyme A transphorase journal Fed. Proc. volume 11 pages 291 transferase stub Category EC 2.8.3 Category Enzymes of unknown structure ... more details
enzyme Name succinate citramalate CoA transferase EC number 2.8.3.7 CAS number 9033 60 7 IUBMB EC number 2 8 3 7 GO code 0047370 image width caption In enzymology , a succinate citramalate CoA transferase EC number 2.8.3.7 is an enzyme that catalysis catalyzes the chemical reaction succinyl CoA citramalate math rightleftharpoons math succinate citramalyl CoA Thus, the two substrate biochemistry substrates of this enzyme are succinyl CoA and citramalate , whereas its two product chemistry products are succinate and citramalyl CoA . This enzyme belongs to the family of transferase s, specifically the CoA transferases. The systematic name of this enzyme class is succinyl CoA citramalate CoA transferase . Other names in common use include itaconate CoA transferase , citramalate CoA transferase , citramalate coenzyme A transferase , and succinyl coenzyme A citramalyl coenzyme A transferase . This enzyme participates in c5 branched dibasic acid metabolism . References reflist 1 cite journal author Cooper RA, Kornberg HL date 1964 title The utilization of itaconate by Pseudomonas sp journal Biochem. J. volume 91 pages 82&ndash 91 pmid 4284209 issue 1 pmc 1202819 transferase stub Category EC 2.8.3 Category Enzymes of unknown structure ... more details
enzyme Name glutaconate CoA transferase EC number 2.8.3.12 CAS number 79078 99 2 IUBMB EC number 2 8 3 12 GO code 0018730 image width caption In enzymology , a glutaconate CoA transferase EC number 2.8.3.12 is an enzyme that catalysis catalyzes the chemical reaction acetyl CoA E glutaconate math rightleftharpoons math acetate glutaconyl 1 CoA Thus, the two substrate biochemistry substrates of this enzyme are acetyl CoA and E glutaconate , whereas its two product chemistry products are acetate and glutaconyl 1 CoA . This enzyme belongs to the family of transferase s, specifically the CoA transferases. The systematic name of this enzyme class is acetyl CoA E glutaconate CoA transferase . This enzyme participates in styrene degradation and butanoate metabolism . References reflist 1 cite journal doi 10.1111 j.1432 1033.1981.tb06404.x author Buckel W, Dorn U, Semmler R date 1981 title Glutaconate CoA transferase from Acidaminococcus fermentans journal Eur. J. Biochem. volume 118 pages 315&ndash 21 pmid 6945182 issue 2 transferase stub Category EC 2.8.3 Category Enzymes of unknown structure ... more details
Orphan date November 2010 enzyme Name 5 hydroxypentanoate CoA transferase EC number 2.8.3.14 CAS number 111684 68 5 IUBMB EC number 2 8 3 14 GO code 0047591 image width caption In enzymology , a 5 hydroxypentanoate CoA transferase EC number 2.8.3.14 is an enzyme that catalysis catalyzes the chemical reaction acetyl CoA 5 hydroxypentanoate math rightleftharpoons math acetate 5 hydroxypentanoyl CoA Thus, the two substrate biochemistry substrates of this enzyme are acetyl CoA and 5 hydroxypentanoate , whereas its two product chemistry products are acetate and 5 hydroxypentanoyl CoA . This enzyme belongs to the family of transferase s, specifically the CoA transferases. The systematic name of this enzyme class is acetyl CoA 5 hydroxypentanoate CoA transferase . Other names in common use include 5 hydroxyvalerate CoA transferase , and 5 hydroxyvalerate coenzyme A transferase . References reflist 1 cite journal doi 10.1515 bchm3.1990.371.2.1077 author Eikmanns U, Buckel W year 1990 title Properties of 5 hydroxyvalerate CoA transferase from Clostridium aminovalericum journal Biol. Chem. Hoppe Seyler volume 371 pages 1077&ndash 82 pmid 2085413 issue 11 Category EC 2.8.3 Category Enzymes of unknown structure transferase stub ... more details
enzyme Name butyrate acetoacetate CoA transferase EC number 2.8.3.9 CAS number 66231 37 6 IUBMB EC number 2 8 3 9 GO code 0047371 image width caption In enzymology , a butyrate acetoacetate CoA transferase EC number 2.8.3.9 is an enzyme that catalysis catalyzes the chemical reaction butanoyl CoA acetoacetate math rightleftharpoons math butanoate acetoacetyl CoA Thus, the two substrate biochemistry substrates of this enzyme are butanoyl CoA and acetoacetate , whereas its two product chemistry products are butanoate and acetoacetyl CoA . This enzyme belongs to the family of transferase s, specifically the CoA transferases. The systematic name of this enzyme class is butanoyl CoA acetoacetate CoA transferase . Other names in common use include butyryl coenzyme A acetoacetate coenzyme A transferase , and butyryl CoA acetoacetate CoA transferase . References reflist 1 cite journal author Barker HA, Jeng IM, Neff N, Robertson JM, Tam FK, Hosaka S date 1978 title Butyryl CoA acetoacetate CoA transferase from a lysine fermenting Clostridium journal J. Biol. Chem. volume 253 pages 1219&ndash 25 pmid 624727 issue 4 transferase stub Category EC 2.8.3 Category Enzymes of unknown structure ... more details
enzyme Name succinate hydroxymethylglutarate CoA transferase EC number 2.8.3.13 CAS number 80237 90 7 IUBMB EC number 2 8 3 13 GO code 0047369 image width caption In enzymology , a succinate hydroxymethylglutarate CoA transferase EC number 2.8.3.13 is an enzyme that catalysis catalyzes the chemical reaction succinyl CoA 3 hydroxy 3 methylglutarate math rightleftharpoons math succinate S 3 hydroxy 3 methylglutaryl CoA Thus, the two substrate biochemistry substrates of this enzyme are succinyl CoA and 3 hydroxy 3 methylglutarate , whereas its two product chemistry products are succinate and S 3 hydroxy 3 methylglutaryl CoA . This enzyme belongs to the family of transferase s, specifically the CoA transferases. The systematic name of this enzyme class is succinyl CoA 3 hydroxy 3 methylglutarate CoA transferase . Other names in common use include hydroxymethylglutarate coenzyme A transferase , and dicarboxyl CoA dicarboxylic acid coenzyme A transferase . References reflist 1 cite journal author Deana R, Rigoni F, Deana AD, Galzigna L date 1981 title Submitochondrial localization and partial purification of the succinylCoA 3 hydroxy 3 methylglutarate coenzyme A transferase from rat liver journal Biochim. Biophys. Acta. volume 662 pages 119&ndash 24 pmid 6946836 issue 1 transferase stub Category EC 2.8.3 Category Enzymes of unknown structure ... more details
enzyme Name 3 oxoadipate CoA transferase EC number 2.8.3.6 CAS number 9026 16 8 IUBMB EC number 2 8 3 6 GO code 0047569 image width caption In enzymology , a 3 oxoadipate CoA transferase EC number 2.8.3.6 is an enzyme that catalysis catalyzes the chemical reaction succinyl CoA 3 oxoadipate math rightleftharpoons math succinate 3 oxoadipyl CoA Thus, the two substrate biochemistry substrates of this enzyme are succinyl CoA and 3 oxoadipate , whereas its two product chemistry products are succinate and 3 oxoadipyl CoA . This enzyme belongs to the family of transferase s, specifically the CoA transferases. The systematic name of this enzyme class is succinyl CoA 3 oxoadipate CoA transferase . Other names in common use include 3 oxoadipate coenzyme A transferase , and 3 oxoadipate succinyl CoA transferase . This enzyme participates in benzoate degradation via hydroxylation . References reflist 1 cite journal author KATAGIRI M, HAYAISHI O date 1957 title Enzymatic degradation of beta ketoadipic acid journal J. Biol. Chem. volume 226 pages 439&ndash 48 pmid 13428776 issue 1 transferase stub Category EC 2.8.3 Category Enzymes of unknown structure ... more details
enzyme Name citrate CoA transferase EC number 2.8.3.10 CAS number 65187 14 6 IUBMB EC number 2 8 3 10 GO code 0008814 image width caption In enzymology , a citrate CoA transferase EC number 2.8.3.10 is an enzyme that catalysis catalyzes the chemical reaction acetyl CoA citrate math rightleftharpoons math acetate 3S citryl CoA Thus, the two substrate biochemistry substrates of this enzyme are acetyl CoA and citrate , whereas its two product chemistry products are acetate and 3S citryl CoA . This enzyme belongs to the family of transferase s, specifically the CoA transferases. The systematic name of this enzyme class is acetyl CoA citrate CoA transferase . This enzyme participates in citrate cycle tca cycle . References reflist 1 cite journal author Dimroth P, Loyal R, Eggerer H date 1977 title Characterization of the isolated transferase subunit of citrate lyase as a CoA Transferase. Evidence against a covalent enzyme substrate intermediate journal Eur. J. Biochem. volume 80 pages 479&ndash 88 pmid 336371 doi 10.1111 j.1432 1033.1977.tb11903.x issue 2 transferase stub Category EC 2.8.3 Category Enzymes of unknown structure ... more details
enzyme Name oxalate CoA transferase EC number 2.8.3.2 CAS number 9026 17 9 IUBMB EC number 2 8 3 2 GO code 0050161 image width caption In enzymology , an oxalate CoA transferase EC number 2.8.3.2 is an enzyme that catalysis catalyzes the chemical reaction succinyl CoA oxalate math rightleftharpoons math succinate oxalyl CoA Thus, the two substrate biochemistry substrates of this enzyme are succinyl CoA and oxalate , whereas its two product chemistry products are succinate and oxalyl CoA . This enzyme belongs to the family of transferase s, specifically the CoA transferases. The systematic name of this enzyme class is succinyl CoA oxalate CoA transferase . Other names in common use include succinyl beta ketoacyl CoA transferase , and oxalate coenzyme A transferase . This enzyme participates in glyoxylate and dicarboxylate metabolism . References reflist 1 cite journal author Quayle JR, Keech DB, Taylor GA date 1961 title Carbon assimilation by Pseudomonas oxalaticus OXI . 4. Metabolism of oxalate in cell free extracts of the organism grown on oxalate journal Biochem. J. volume 78 pages 225&ndash 36 pmid 16748872 issue 2 pmc 1205258 transferase stub Category EC 2.8.3 Category Enzymes of unknown structure ... more details
enzyme Name 3 oxoacid CoA transferase EC number 2.8.3.5 CAS number 9027 43 4 IUBMB EC number 2 8 3 5 GO code 0008260 image width caption In enzymology , a 3 oxoacid CoA transferase EC number 2.8.3.5 is an enzyme that catalysis catalyzes the chemical reaction succinyl CoA a 3 oxo acid math rightleftharpoons math succinate a 3 oxoacyl CoA Thus, the two substrate biochemistry substrates of this enzyme are succinyl CoA and 3 oxo acid , whereas its two product chemistry products are succinate and 3 oxoacyl CoA . This enzyme belongs to the family of transferase s, specifically the CoA transferases. The systematic name of this enzyme class is succinyl CoA 3 oxo acid CoA transferase . Other names in common use include 3 oxoacid coenzyme A transferase , 3 ketoacid CoA transferase , 3 ketoacid coenzyme A transferase , 3 oxo CoA transferase , 3 oxoacid CoA dehydrogenase , acetoacetate succinyl CoA transferase , acetoacetyl coenzyme A succinic thiophorase , succinyl coenzyme A acetoacetyl coenzyme A transferase , and succinyl CoA transferase . This enzyme participates in 3 metabolism metabolic pathways synthesis and degradation of ketone bodies , valine, leucine and isoleucine degradation , and butanoate metabolism . This protein may use the morpheein model of allosteric regulation . ref name pmid22182754 cite journal author T. Selwood and E. K. Jaffe. title Dynamic dissociating homo oligomers and the control of protein function. journal Arch. Biochem. Biophys. volume 519 issue 2 pages 131 43 year 2011 pmid 22182754 url http www.ncbi.nlm.nih.gov entrez query.fcgi?cmd Retrieve&db PubMed&dopt Citation&list uids 22182754 doi 10.1016 j.abb.2011.11.020 ref Structural studies As of late 2007 ... year 1967 title Coenzyme A transferase. Kinetics and exchange reactions journal J. Biol. Chem. volume ... A transferase journal J. Biol. Chem. volume 221 issue 1 pages 15&ndash 31 pmid 13345795 Category EC 2.8.3 Category Enzymes of known structure transferase stub de 3 Ketos ure CoA Transferase ... more details
enzyme Name Formyl CoA transferase EC number 2.8.3.16 CAS number 128826 27 7 IUBMB EC number 2 8 3 16 GO code image width caption In enzymology , a formyl CoA transferase EC number 2.8.3.16 is an enzyme that catalysis catalyzes the chemical reaction formyl CoA oxalate math rightleftharpoons math formate oxalyl CoA Thus, the two substrate biochemistry substrates of this enzyme are formyl CoA and oxalate , whereas its two product chemistry products are formate and oxalyl CoA . This enzyme belongs to the family of transferase s, specifically the CoA transferases. The systematic name of this enzyme class is formyl CoA oxalate CoA transferase . Other names in common use include formyl coenzyme A transferase , and formyl CoA oxalate CoA transferase . Structural studies As of late 2007, 4 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1T3Z , PDB link 1T4C , PDB link 1VGQ , and PDB link 1VGR . References reflist 1 cite journal author Baetz AL, Allison MJ date 1990 title Purification and characterization of formyl coenzyme A transferase from Oxalobacter formigenes journal J. Bacteriol. volume 172 pages 3537&ndash 40 pmid 2361939 issue 7 pmc 213325 cite journal author Sidhu H, Ogden SD, Lung HY, Luttge BG, Baetz AL, Peck AB date 1997 title DNA sequencing and expression of the formyl coenzyme A transferase gene, frc, from Oxalobacter formigenes journal J. Bacteriol. volume 179 pages 3378&ndash 81 pmid 9150242 issue 10 pmc 179125 transferase stub Category EC 2.8.3 Category Enzymes of known structure ... more details
enzyme Name malonate CoA transferase EC number 2.8.3.3 CAS number 9026 18 0 IUBMB EC number 2 8 3 3 GO code 0050078 image width caption In enzymology , a malonate CoA transferase EC number 2.8.3.3 is an enzyme that catalysis catalyzes the chemical reaction acetyl CoA malonate math rightleftharpoons math acetate malonyl CoA Thus, the two substrate biochemistry substrates of this enzyme are acetyl CoA and malonate , whereas its two product chemistry products are acetate and malonyl CoA . This enzyme belongs to the family of transferase s, specifically the CoA transferases. The systematic name of this enzyme class is acetyl CoA malonate CoA transferase . This enzyme is also called malonate coenzyme A transferase . This enzyme participates in beta alanine metabolism and propanoate metabolism . References reflist 1 cite journal author HAYAISHI O date 1955 title Enzymatic decarboxylation of malonic acid journal J. Biol. Chem. volume 215 pages 125&ndash 36 pmid 14392148 issue 1 cite journal author Takamura Y and Kitayama Y date 1981 title Purification and some properties of malonate decarboxylase from Pseudomonas ovalis an oligomeric enzyme with bifunctional properties journal Biochem. Int. volume 3 pages 483&ndash 491 transferase stub Category EC 2.8.3 Category Enzymes of unknown structure ... more details
enzyme Name acetate CoA transferase EC number 2.8.3.8 CAS number 37278 35 6 IUBMB EC number 2 8 3 8 GO code 0008775 image width caption In enzymology , an acetate CoA transferase EC number 2.8.3.8 is an enzyme that catalysis catalyzes the chemical reaction acyl CoA acetate math rightleftharpoons math a fatty acid anion acetyl CoA Thus, the two substrate biochemistry substrates of this enzyme are acyl CoA and acetate , whereas its two product chemistry products are fatty acid anion and acetyl CoA . This enzyme belongs to the family of transferase s, specifically the CoA transferases. The systematic name of this enzyme class is acyl CoA acetate CoA transferase . Other names in common use include acetate coenzyme A transferase , butyryl CoA acetate CoA transferase , butyryl coenzyme A transferase , and succinyl CoA acetate CoA transferase . This enzyme participates in 4 metabolism metabolic pathways benzoate degradation via coa ligation , propanoate metabolism , butanoate metabolism , and two component system general . 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 1K6D . References reflist 1 cite journal author Vanderwinkel E, Furmanski P, Reeves HC, Ajl SJ date 1968 title Growth of Escherichia coli on fatty acids requirement for coenzyme A transferase activity journal Biochem. Biophys. Res. Commun. volume 33 pages 902&ndash 8 pmid 4884054 doi 10.1016 0006 291X 68 90397 5 issue 6 cite journal author Kaschabek SR, Kuhn B, Muller D, Schmidt E, Reineke W date 2002 title Degradation of aromatics and chloroaromatics by Pseudomonas sp strain B13 purification and characterization of 3 oxoadipate succinyl coenzyme A CoA transferase and 3 oxoadipyl CoA thiolase ..., and analysis of sequences encoding 3 oxoadipate succinyl coenzyme A CoA transferase and 3 oxoadipyl ... 223.2002 issue 1 pmc 134769 transferase stub Category EC 2.8.3 Category Enzymes of known structure ... more details
enzyme Name citramalate CoA transferase EC number 2.8.3.11 CAS number 9033 60 7 IUBMB EC number 2 8 3 11 GO code 0047775 image width caption In enzymology , a citramalate CoA transferase EC number 2.8.3.11 is an enzyme that catalysis catalyzes the chemical reaction acetyl CoA citramalate math rightleftharpoons math acetate 3S citramalyl CoA Thus, the two substrate biochemistry substrates of this enzyme are acetyl CoA and citramalate , whereas its two product chemistry products are acetate and 3S citramalyl CoA . This enzyme belongs to the family of transferase s, specifically the CoA transferases. The systematic name of this enzyme class is acetyl CoA citramalate CoA transferase . This enzyme participates in c5 branched dibasic acid metabolism . References reflist 1 cite journal author Dimroth P, Buckel W, Loyal R, Eggerer H date 1977 title Isolation and function of the subunits of citramalate lyase and formation of hybrids with the subunits of citrate lyase journal Eur. J. Biochem. volume 80 pages 469&ndash 77 pmid 923590 doi 10.1111 j.1432 1033.1977.tb11902.x issue 2 transferase stub Category EC 2.8.3 Category Enzymes of unknown structure ... more details
PBB geneid 2944 Glutathione S transferase Mu 1 gene name GSTM1 is a human glutathione S transferase . The PBB Summary template is automatically maintained by Protein Box Bot. See Template PBB Controls to Stop updates. PBB Summary section title summary text Cytosolic and membrane bound forms of glutathione S transferase are encoded by two distinct supergene families. At present, eight distinct classes of the soluble cytoplasmic mammalian glutathione S transferases have been identified alpha, kappa, mu, omega, pi, sigma, theta and zeta. This gene encodes a cytoplasmic glutathione S transferase that belongs to the mu class. The mu class of enzymes functions in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. The genes encoding the mu class of enzymes are organized in a gene cluster on chromosome 1p13.3 and are known to be highly polymorphic. These genetic variations can change an individual s susceptibility to carcinogens and toxins as well as affect the toxicity and efficacy of certain drugs. Null mutations of this class mu gene have been linked with an increase in a number of cancers , likely due to an increased susceptibility to environmental toxins and carcinogens. Multiple protein isoforms are encoded by transcript variants of this gene. ref cite web title Entrez Gene GSTM1 glutathione S transferase M1 url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 2944 accessdate ref References reflist Further reading refbegin PBB Further reading citations cite journal author Engel LS, Taioli E, Pfeiffer R, et al. title Pooled analysis and meta analysis of glutathione S transferase M1 and bladder cancer a HuGE review. journal Am. J. Epidemiol. volume 156 issue 2 pages 95 109 year 2002 pmid 12117698 doi 10.1093 aje kwf018 ... JD, Lampe JW title Modulation of human serum glutathione S transferase A1 2 concentration by cruciferous ... more details
enzyme Name dihydrolipoyllysine residue 2 methylpropanoyl transferase EC number 2.3.1.168 CAS number IUBMB EC number 2 3 1 168 GO code 0043754 image width caption Cleanup date November 2008 In enzymology , a dihydrolipoyllysine residue 2 methylpropanoyl transferase EC number 2.3.1.168 is an enzyme that catalysis catalyzes the chemical reaction 2 methylpropanoyl CoA enzyme N sub 6 sub dihydrolipoyl lysine math rightleftharpoons math CoA enzyme N sub 6 sub S 2 methylpropanoyl dihydrolipoyl lysine Thus, the two substrate biochemistry substrates of this enzyme are 2 methylpropanoyl CoA and enzyme N6 dihydrolipoyl lysine , whereas its two product chemistry products are coenzyme A CoA and enzyme N6 S 2 methylpropanoyl dihydrolipoyl lysine . This enzyme belongs to the family of transferase s, specifically those acyltransferase s transferring groups other than aminoacyl groups. The systematic name of this enzyme class is 2 methylpropanoyl CoA enzyme N6 dihydrolipoyl lysine S 2 methylpropanoyl transferase . Other names in common use include dihydrolipoyl transacylase , enzyme dihydrolipoyllysine 2 methylpropanoyl CoA , S 2 methylpropanoyl transferase , 2 methylpropanoyl CoA enzyme 6 N dihydrolipoyl lysine , and S 2 methylpropanoyl transferase . This enzyme participates in valine, leucine and isoleucine degradation . Structural studies As of late 2007, 6 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1ZWV , PDB link 2COO , PDB link 2IHW , PDB link 2II3 , PDB link 2II4 , and PDB link 2II5 . References reflist 1 cite journal author Massey LK, Sokatch JR, Conrad RS date 1976 title Branched chain amino acid catabolism in bacteria journal Bacteriol. Rev. volume 40 pages 42&ndash 54 pmid 773366 issue 1 pmc 413937 cite journal author Chuang DT, Hu CC, Ku LS, Niu WL, Myers DE, Cox RP date 1984 title Catalytic ... Category EC 2.3.1 Category Enzymes of known structure transferase stub it Residuo di ... more details
enzyme Name Lipoyl octanoyl transferase EC number 2.3.1.181 CAS number IUBMB EC number 2 3 1 181 GO code image width caption Orphan date February 2009 In enzymology , a lipoyl octanoyl transferase EC number 2.3.1.181 is an enzyme that catalysis catalyzes the chemical reaction octanoyl acyl carrier protein protein math rightleftharpoons math protein N sub 6 sub octanoyl lysine acyl carrier protein Thus, the two substrate biochemistry substrates of this enzyme are octanoyl acyl carrier protein and protein , whereas its two product chemistry products are protein N6 octanoyl lysine and acyl carrier protein . This enzyme belongs to the family of transferase s, specifically those acyltransferase s transferring groups other than aminoacyl groups. The systematic name of this enzyme class is octanoyl acyl carrier protein protein N octanoyltransferase . Other names in common use include LipB , lipoyl octanoyl acyl carrier protein protein , N lipoyltransferase , lipoyl octanoyl acyl carrier protein protein transferase , lipoate octanoate transferase , lipoyltransferase , octanoyl acyl carrier protein protein N octanoyltransferase , and lipoyl octanoyl transferase . This enzyme participates in lipoic acid metabolism. References reflist 1 cite journal author Broadwater JA, Haas JA, Fox BG, Booker SJ date 2005 title Expression, purification, and physical characterization of Escherichia coli lipoyl octanoyl transferase journal Protein. Expr. Purif. volume 39 pages 269&ndash 82 pmid 15642479 issue 2 doi 10.1016 j.pep.2004.10.021 cite journal author Vanden Boom TJ, Reed KE, Cronan JE Jr date 1991 title Lipoic acid metabolism in Escherichia coli isolation of null mutants defective in lipoic acid biosynthesis, molecular cloning and characterization of the E. coli lip locus, and identification of the lipoylated protein of the glycine cleavage system journal J. Bacteriol. volume 173 pages ... transferase stub Category EC 2.3.1 Category Enzymes of unknown structure ... more details
PBB geneid 2938 Glutathione S transferase A1 is an enzyme that in humans is encoded by the GSTA1 gene . ref name pmid9503014 cite journal author Mucher G, Becker J, Knapp M, Buttner R, Moser M, Rudnik Schoneborn S, Somlo S, Germino G, Onuchic L, Avner E, Guay Woodford L, Zerres K title Fine mapping of the autosomal recessive polycystic kidney disease locus PKHD1 and the genes MUT, RDS, CSNK2 beta, and GSTA1 at 6p21.1 p12 journal Genomics volume 48 issue 1 pages 40 5 year 1998 month Apr pmid 9503014 pmc doi 10.1006 geno.1997.5145 ref The PBB Summary template is automatically maintained by Protein Box Bot. See Template PBB Controls to Stop updates. PBB Summary section title summary text Cytosolic and membrane bound forms of glutathione S transferase are encoded by two distinct supergene families ... Gene GSTA1 glutathione S transferase A1 url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch ... B title Heterologous expression of recombinant human glutathione transferase A1 1 from a hepatoma ... and characterization of eight glutathione S transferase isoenzymes of hamster. Comparison ... F, Nguyen T, Pickett CB title Isolation and characterization of a human glutathione S transferase Ha1 ... of the C terminal sequence to the catalytic activity of GST2, a human alpha class glutathione transferase ... of human glutathione S transferase 2 genes to chromosome band 6p12. journal Proc. Natl. Acad ... Nucleotide sequence of the human liver glutathione S transferase subunit 1 cDNA. journal Biochem ... of the 5 flanking sequences of the human alpha class glutathione S transferase genes. journal Biochem ... and organization of the human alpha class glutathione S transferase genes and related pseudogenes ... of human alpha class glutathione transferase A1 1, and a comparison with the Mu and Pi ... transferase A1 1 in the apo form and in complexes with ethacrynic acid and its glutathione conjugate ... S transferase Alpha 1 1 plasma concentrations in controls and in patients with gastrointestinal ... more details
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