Infobox protein family Symbol ACPS Name ACPS image PDB 1qr0 EBI.jpg width caption crystal structure of the 4 phosphopantetheinyl transferase sfp coenzyme a complex Pfam PF01648 Pfam clan InterPro IPR008278 SMART PROSITE MEROPS SCOP 1qr0 TCDB OPM family OPM protein CAZy CDD In molecular biology, the 4 phosphopantetheinyl transferase superfamily of protein s ACPS transfer the 4 phosphopantetheine 4 PP moiety from coenzyme A CoA to the invariant serine of pp binding. This post translational modification renders holo ACP capable of acyl group activation via thioesterification of the cysteamine thiol of 4 PP. ref name pmid7559576 cite journal author Lambalot RH, Walsh CT title Cloning, overproduction, and characterization of the Escherichia coli holo acyl carrier protein synthase journal J. Biol. Chem. volume 270 issue 42 pages 24658 61 year 1995 month October pmid 7559576 doi 10.1074 jbc.270.42.24658 url ref This superfamily consists of two subtypes The ACPS type such as E. coli ACPS and the Sfp type such as B. subtilis SFP. The secondary structure structure of the Sfp type is known, ref name pmid10581256 cite journal author Reuter K, Mofid MR, Marahiel MA, Ficner R title Crystal structure of the surfactin synthetase activating enzyme sfp a prototype of the 4 phosphopantetheinyl transferase superfamily journal EMBO J. volume 18 issue 23 pages 6823 31 year 1999 month December pmid 10581256 pmc 1171745 doi 10.1093 emboj 18.23.6823 url ref which shows the active site accommodates a magnesium ion . The most highly conservation genetics conserved regions of the protein are involved in Binding molecular binding the magnesium ion . References reflist InterPro content IPR008278 Category Protein families ... more details
File Bacterial GST.jpg thumb 400px right Beta class glutathione transferase structure from Proteus mirabilis PDB 1PMT . ref Rossjohn J, Polekhina G, Feil SC, Allocati N, Masulli M, Di Ilio C, Parker MW 1998 A mixed disulfide bond in bacterial glutathione transferase functional and evolutionary implications. Structure 6 721 734. ref Bacterial glutathione transferases GSTs EC 2.5.1.18 are part of a superfamily molecular biology superfamily of enzyme s that play a crucial role in cellular detoxification . ref cite journal author Hayes JD, Flanagan JU, Jowsey IR title Glutathione transferases journal Annual Review of Pharmacology and Toxicology volume 45 issue pages 51 88 year 2005 pmid 15822171 doi 10.1146 annurev.pharmtox.45.120403.095857 ref ref cite journal author Sheehan D, Meade G, Foley VM, Dowd CA title Structure, function and evolution of glutathione transferases implications for classification of non mammalian members of an ancient enzyme superfamily journal The Biochemical Journal volume 360 issue 1 pages 1 16 year 2001 month November pmid 11695986 pmc 1222196 doi 10.1042 0264 6021 3600001 ref ref cite journal author Oakley AJ title Glutathione transferases new functions journal Current Opinion in Structural Biology volume 15 issue 6 pages 716 23 year 2005 month December pmid 16263269 doi 10.1016 j.sbi.2005.10.005 ref The common feature of the GSTs is to catalyse the nucleophilic ... of the glutathione S transferase supergene family journal Journal of Bacteriology volume 172 issue ... of the glutathione S transferase superfamily journal FEBS Letters volume 323 issue 1 2 pages 135 40 ... S transferase in Ochrobactrum anthropi function of xenobiotic substrates and other forms of stress ... P, Xun L, Hargis M title Characterization of a Flavobacterium glutathione S transferase gene ... 2709490 doi 10.1016 j.abb.2007.04.035 ref See also Glutathione Glutathione S transferase Fosfomycin ... Bacteria Category Enzymes Category Prokaryotes transferase stub cell biology stub ... more details
PBB geneid 4257 Microsomal glutathione S transferase 1 is an enzyme that in humans is encoded by the MGST1 gene . ref name entrez cite web title Entrez Gene MGST1 microsomal glutathione S transferase 1 url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 4257 accessdate ref Function The MAPEG family Membrane Associated Proteins in Eicosanoid and Glutathione metabolism consists of six human proteins, two of which are involved in the production of leukotriene s and prostaglandin E , important mediators of inflammation . Other family members, demonstrating glutathione S transferase and peroxidase activities, are involved in cellular defense against toxic, carcinogenic, and pharmacologically active electrophilic compounds. This gene encodes a protein that catalyzes the conjugation of glutathione to electrophiles and the reduction of lipid hydroperoxides. This protein is localized to the endoplasmic reticulum and outer mitochondrial membrane where it is thought to protect these membranes from oxidative stress . Four transcript variants of this gene encode one ... for the microsomal glutathione S transferase is on human chromosome 12. journal Genomics volume ... NE, Montoya MA title Structural organization of the human microsomal glutathione S transferase ... glutathione transferase 1 in mammalian tissues. A predominant alternate first exon in human ... S transferase gene MGST1 on chromosome 12p13.1 13.2. Identification of the correct promoter ... C synthase and microsomal glutathione S transferase elucidated by indirect immunofluorescence analysis ... polymorphisms SNPs in the microsomal glutathione S transferase 1 MGST1 gene journal J. Hum. Genet ... S transferase polymorphisms in relation to laryngeal carcinoma risk journal Cancer Lett. volume ... microsomal glutathione transferase 1 and prostaglandin E synthase genes is mediated by Sp1 and Sp3 ... of an intact noncovalent homotrimer of detergent solubilized rat microsomal glutathione transferase ... more details
enzyme Name xyloglucan xyloglucosyl transferase EC number 2.4.1.207 CAS number IUBMB EC number 2 4 1 207 GO code 0016762 image width caption In enzymology , a xyloglucan xyloglucosyl transferase EC number 2.4.1.207 is an enzyme that catalysis catalyzes the chemical reaction in which a beta 14 bond in the backbone of a xyloglucan in broken the xyloglucanyl segment is then transferred to the oxygen O sub 4 sub of the non reducing terminal glucose residue of either xyloglucan or an oligosaccharide thereof. ref name Thompson cite journal last Thompson first James E. coauthors Fry, Stephen C. year 2001 journal The Plant Journal volume 26 issue 1 pages 23 34 url http www.icmb.ed.ac.uk research institutes plant PDF 2001 Thompson 2001 23.pdf doi 10.1046 j.1365 313x.2001.01005.x pmid 11359607 title Restructuring of wall bound xyloglucan by transglycosylation in living plant cells. ref This enzyme belongs to the family of glycosyltransferase s, specifically the hexosyltransferases. The systematic name of this enzyme class is xyloglucan xyloglucan xyloglucanotransferase . Other names in common use include endo xyloglucan transferase , and xyloglucan endotransglycosylase . 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 1UMZ and PDB link 1UN1 . References reflist 1 cite journal author Fry SC, Smith RC, Renwick KF, Martin DJ, Hodge SK, Matthews KJ date Pt 3 title Xyloglucan endotransglycosylase, a new wall loosening enzyme activity from plants journal Biochem. J. volume 282 pages 821&ndash 8 pmid 1554366 pmc 1130861 issue Pt 3 cite journal author Nishitani K, Tominaga R year 1992 title Endo xyloglucan transferase, a novel class of glycosyltransferase that catalyzes transfer of a segment of xyloglucan molecule to another xyloglucan molecule journal J. Biol. Chem. volume 267 pages 21058&ndash 64 pmid 1400418 issue 29 cite journal author Foucher AL, McIntosh A, Douce ... more details
PBB geneid 1791 Terminal deoxynucleotidyl transferase TdT , also known as DNA nucleotidylexotransferase DNTT or terminal transferase , is a specialized DNA polymerase expressed in immature, pre B, pre T lymphoid cells, and acute lymphoblastic leukemia lymphoma cells. TdT adds N nucleotide s to the V D J recombination V,D, and J exon s during antibody gene recombination enabling the phenomenon of junctional diversity . In humans, terminal transferase is encoded by the DNTT gene . ref name pmid3862101 cite journal author Isobe M, Huebner K, Erikson J, Peterson RC, Bollum FJ, Chang LM, Croce CM title Chromosome localization of the gene for human terminal deoxynucleotidyltransferase to region 10q23 q25 journal Proc. Natl. Acad. Sci. U.S.A. volume 82 issue 17 pages 5836 40 year 1985 month September ... in vitro . Uses Terminal transferase has applications in molecular biology . It can be used in Rapid ... isotope s, for example in the TUNEL assay T erminal deoxynucleotidyl transferase d U TP N ick E ... title Terminal deoxynucleotidyl transferase negative acute lymphoblastic leukemia journal Arch. Pathol ... Malley DP, Orazi A title Terminal deoxynucleotidyl transferase positive cells in spleen, appendix and branchial ... 2443.2001.00449.x cite journal author Chang LM, Bollum FJ title Molecular biology of terminal transferase ... G, et al. title Four color flow cytometric investigation of terminal deoxynucleotidyl transferase positive ... L, Lovell MA, et al. title Nonpositive terminal deoxynucleotidyl transferase in pediatric precursor ... analysis of residues in the nucleotide binding domain of human terminal deoxynucleotidyl transferase ... transferase and discovery of novel DNA polymerase mu journal Seikagaku volume 74 issue ... of human Pso4 in mammalian DNA repair and association with terminal deoxynucleotidyl transferase. journal ... al. title Association of terminal deoxynucleotidyl transferase with Ku. journal Proc. Natl. Acad ... refend External links MeshName Terminal Deoxyribonucleotidyltransferase transferase stub Kinases ... more details
Infobox protein family Symbol Carboxyl trans Name Carboxyl trans image PDB 1pix EBI.jpg width caption crystal structure of the carboxyltransferase subunit of the bacterial ion pump glutaconyl coenzyme a decarboxylase Pfam PF01039 Pfam clan CL0127 InterPro IPR000022 SMART PROSITE MEROPS SCOP 1od2 TCDB 3.B.1 OPM family OPM protein CAZy CDD In molecular biology, proteins containing the carboxyl transferase domain include biotin dependent carboxylase carboxylases . ref name pmid8102604 cite journal author Toh H, Kondo H, Tanabe T title Molecular evolution of biotin dependent carboxylases journal Eur. J. Biochem. volume 215 issue 3 pages 687 96 year 1993 month August pmid 8102604 doi 10.1111 j.1432 1033.1993.tb18080.x url ref ref name pmid8366018 cite journal author Thornton CG, Kumar GK, Haase FC, Phillips NF, Woo SB, Park VM, Magner WJ, Shenoy BC, Wood HG, Samols D title Primary structure of the monomer of the 12S subunit of transcarboxylase as deduced from DNA and characterization of the product expressed in Escherichia coli journal J. Bacteriol. volume 175 issue 17 pages 5301 8 year 1993 month September pmid 8366018 pmc 206582 doi url ref This protein domain domain carries out the following reaction transcarboxylation from biotin to an acceptor molecule. There are two recognised types of carboxyl transferase. One of them uses acyl CoA and the other uses 2 oxo acid as the acceptor molecule of carbon dioxide . All of the members in this family utilise acyl CoA as the acceptor molecule. References reflist InterPro content IPR000022 Category Protein families ... more details
Infobox protein family Symbol BPL Name Cofactor transferase domain image PDB 1bia EBI.jpg width 250 caption The three dimensional structure of BirA, the repressor of the Escherichia coli biotin biosynthetic operon. ref name pmid1409631 cite journal author Wilson KP, Shewchuk LM, Brennan RG, Otsuka AJ, Matthews BW title Escherichia coli biotin holoenzyme synthetase bio repressor crystal structure delineates the biotin and DNA binding domains journal Proc. Natl. Acad. Sci. U.S.A. volume 89 issue 19 pages 9257 61 year 1992 month October pmid 1409631 pmc 50105 doi 10.1073 pnas.89.19.9257 url ref Pfam PF03099 InterPro IPR004143 SMART PROSITE SCOP 1bia TCDB OPM family OPM protein PDB Infobox protein family Symbol Lip prot lig C Name Bacterial lipoate protein ligase C terminus image PDB 1vqz EBI.jpg width caption crystal structure of putative lipoate protein ligase np 345629.1 from streptococcus pneumoniae tigr4 at 1.99 a resolution Pfam PF10437 Pfam clan InterPro IPR019491 SMART PROSITE MEROPS SCOP TCDB OPM family OPM protein CAZy CDD Infobox protein family Symbol BPL C Name Biotin protein ligase C terminal domain image width caption Pfam PF02237 Pfam clan CL0206 InterPro IPR003142 SMART PROSITE MEROPS SCOP 1bia TCDB OPM family OPM protein CAZy CDD In molecular biology, the Cofactor transferase family is a family of protein domain s that includes biotin protein ligase s, lipoate protein ligases A, octanoyl acyl carrier protein protein N octanoyltransferases, and lipoyl protein protein N lipoyltransferases. ref name pmid11106165 cite journal author Reche PA title Lipoylating and biotinylating enzymes contain a homologous catalytic module journal Protein Sci. volume 9 issue 10 pages 1922 9 year 2000 month October pmid 11106165 pmc 2144473 doi 10.1110 ps.9.10.1922 url ref The metabolism of the cofactors Biotin and lipoic acid share this family. They also share the target modification domain Pfam PF00364 , and the sulfur insertion enzyme Pfam PF04055 . Biotin protein ligase BPL ... more details
F, Derom C, Vlietinck R, Mengelers R, Delespaul P, van Os J title The catechol O methyl transferase ... M. Wichers title The Catechol O Methyl Transferase Val158Met Polymorphism and Experience of Reward in the Flow ... MJ, O Donovan MC title The catechol O methyl transferase COMT gene as a candidate for psychiatric ... O Methyl Transferase Category EC 2.1.1 de Catechol O Methyltransferase it Catecolo O metiltransferasi ... more details
Infobox disease Name Succinyl CoA 3 oxoacid CoA transferase deficiency Image Caption DiseasesDB ICD10 ICD9 ICDO OMIM 245050 MedlinePlus eMedicineSubj eMedicineTopic MeshID Succinyl CoA 3 oxoacid CoA transferase deficiency is an inborn error of ketone body utilization. Succinyl CoA 3 oxoacid CoA transferase catalyzes the transfer of Coenzyme A from Succinyl Coenzyme A to acetoacetate . It can be caused by mutation in the OXCT1 gene. Disease stub Category Inborn errors of metabolism ... more details
enzyme Name L seryl tRNASec selenium transferase EC number 2.9.1.1 CAS number IUBMB EC number 2 9 1 1 GO code 0004125 image width caption In enzymology , a L seryl tRNASec selenium transferase EC number 2.9.1.1 is an enzyme that catalysis catalyzes the chemical reaction L seryl tRNASec selenophosphate math rightleftharpoons math L selenocysteinyl tRNASec phosphate Thus, the two substrate biochemistry substrates of this enzyme are L seryl tRNASec and selenophosphate , whereas its two product chemistry products are L selenocysteinyl tRNASec and phosphate . This enzyme belongs to the family of transferase s, specifically those transferring selenium containing groups selenotransferases. The systematic name of this enzyme class is selenophosphate L seryl tRNASec selenium transferase . Other names in common use include L selenocysteinyl tRNASel synthase , L selenocysteinyl tRNASec synthase selenocysteine synthase , cysteinyl tRNASec selenium transferase , and cysteinyl tRNASec selenium transferase . This enzyme participates in selenoamino acid metabolism . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . References reflist 1 cite journal author Forchhammer K, Bock A date 1991 title Selenocysteine synthase from Escherichia coli. Analysis of the reaction sequence journal J. Biol. Chem. volume 266 pages 6324&ndash 8 pmid 2007585 issue 10 transferase stub Category EC 2.9.1 Category Pyridoxal phosphate enzymes Category Enzymes of unknown structure ... more details
enzyme Name cinnamoyl CoA phenyllactate CoA transferase EC number 2.8.3.17 CAS number IUBMB EC number 2 8 3 17 GO code 0043785 image width caption In enzymology , a cinnamoyl CoA phenyllactate CoA transferase EC number 2.8.3.17 is an enzyme that catalysis catalyzes the chemical reaction E cinnamoyl CoA R phenyllactate math rightleftharpoons math E cinnamate R phenyllactyl CoA Thus, the two substrate biochemistry substrates of this enzyme are E cinnamoyl CoA and R phenyllactate , whereas its two product chemistry products are E cinnamate and R phenyllactyl CoA . This enzyme belongs to the family of transferase s, to be specific, the CoA transferases. The systematic name of this enzyme class is E cinnamoyl CoA R phenyllactate CoA transferase . This enzyme is also called FldA . References reflist 1 cite journal author Dickert S, Pierik AJ, Linder D, Buckel W date 2000 title The involvement of coenzyme A esters in the dehydration of R phenyllactate to E cinnamate by Clostridium sporogenes journal Eur. J. Biochem. volume 267 pages 3874&ndash 84 pmid 10849007 doi 10.1046 j.1432 1327.2000.01427.x issue 12 transferase stub Category EC 2.8.3 Category Enzymes of unknown structure ... more details
enzyme Name Succinyl CoA R benzylsuccinate CoA transferase EC number 2.8.3.15 CAS number IUBMB EC number 2 8 3 15 GO code image width caption In enzymology , a succinyl CoA R benzylsuccinate CoA transferase EC number 2.8.3.15 is an enzyme that catalysis catalyzes the chemical reaction succinyl CoA R 2 benzylsuccinate math rightleftharpoons math succinate R 2 benzylsuccinyl CoA Thus, the two substrate biochemistry substrates of this enzyme are succinyl CoA and R 2 benzylsuccinate , whereas its two product chemistry products are succinate and R 2 benzylsuccinyl CoA . This enzyme belongs to the family of transferase s, specifically the CoA transferases. The systematic name of this enzyme class is succinyl CoA R 2 benzylsuccinate CoA transferase . This enzyme is also called benzylsuccinate CoA transferase . This enzyme participates in benzoate degradation via coa ligation . References reflist 1 cite journal author Leutwein C, Heider J date 2001 title Succinyl CoA R benzylsuccinate CoA transferase an enzyme of the anaerobic toluene catabolic pathway in denitrifying bacteria journal J. Bacteriol. volume 183 pages 4288&ndash 95 pmid 11418570 doi 10.1128 JB.183.14.4288 4295.2001 issue 14 pmc 95319 cite journal author Leutwein C, Heider J date Pt 11 title Anaerobic toluene catabolic pathway in denitrifying Thauera aromatica activation and beta oxidation of the first intermediate, R benzylsuccinate journal Microbiology. volume 145 pages 3265&ndash 71 pmid 10589736 cite journal author Leuthner B, Heider J date 2000 title Anaerobic toluene catabolism of Thauera aromatica the bbs operon codes for enzymes of beta oxidation of the intermediate benzylsuccinate journal J. Bacteriol. volume 182 pages 272&ndash 7 pmid 10629170 doi 10.1128 JB.182.2.272 277.2000 issue 2 pmc 94273 cite journal author Heider J date 2001 title A new family of CoA transferases journal FEBS. Lett. volume 509 pages 345&ndash 9 pmid 11749953 doi 10.1016 S0014 5793 01 03178 7 issue 3 transferase stub Category EC ... more details
mergeto UDP N acetylglucosamine 1 carboxyvinyltransferase date February 2011 UDP N acetylglucosamine enolpyruvyl transferase or MurA is an enzyme ref name urlEnolpyruvate transferase, EPT family Cite web url http supfam.mrc lmb.cam.ac.uk SUPERFAMILY cgi bin scop.cgi?sunid 55209 title Enolpyruvate transferase, EPT family format work accessdate 2008 11 23 ref that catalyzes the first committed step in peptidoglycan biosynthesis, namely the ligation of phosphoenolpyruvate PEP to the 3 hydroxyl group of Uridine diphosphate N acetylglucosamine UDP N acetylglucosamine . This pyruvate moiety provides the linker that bridges the glycan and peptide portion of peptidoglycan. ref name Brown Cite journal author Brown ED, Vivas EI, Walsh CT, Kolter R title MurA MurZ , the enzyme that catalyzes the first committed step in peptidoglycan biosynthesis, is essential in Escherichia coli journal J. Bacteriol. volume 177 issue 14 pages 4194 7 year 1995 month July pmid 7608103 pmc 177162 ref The enzyme is inhibited by the antibiotic fosfomycin , which covalently modifies an active site cysteine residue. ref name isbn0 07 144578 1 Cite book author King, Michael B. title Lange Q & A publisher McGraw Hill, Medical Pub. Division location New York year 2005 pages 298 isbn 0 07 144578 1 oclc doi accessdate ref References Reflist Category EC 2.5.1 Category Enzymes of known structure transferase stub ... more details
enzyme Name phospho N acetylmuramoyl pentapeptide transferase EC number 2.7.8.13 CAS number 9068 50 2 IUBMB EC number 2 7 8 13 GO code 0008963 image width caption In enzymology , a phospho N acetylmuramoyl pentapeptide transferase EC number 2.7.8.13 is an enzyme that catalysis catalyzes the chemical reaction UDP Mur sub 2 sub Ac oyl L Ala gamma D Glu L Lys D Ala D Ala undecaprenyl phosphate math rightleftharpoons math UMP Mur sub 2 sub Ac oyl L Ala gamma D Glu L Lys D Ala D Ala diphosphoundecaprenol Thus, the two substrate biochemistry substrates of this enzyme are UDP Mur2Ac oyl L Ala gamma D Glu L Lys D Ala D Ala and undecaprenyl phosphate , whereas its 3 product chemistry products are uridine monophosphate UMP , Mur2Ac oyl L Ala gamma D Glu L Lys D Ala D Ala , and diphosphoundecaprenol . This enzyme belongs to the family of transferase s, specifically those transferring non standard substituted phosphate groups. The systematic name of this enzyme class is UDP MurAc oyl L Ala gamma D Glu L Lys D Ala D Ala undecaprenyl phos phate phospho N acetylmuramoyl pentapeptide transferase . Other names in common use include MraY transferase , UDP MurNAc L Ala D gamma Glu L Lys D Ala D Ala C55 isoprenoid , alcohol transferase , UDP MurNAc Ala gammaDGlu Lys DAla DAla undecaprenylphosphate , transferase , phospho N acetylmuramoyl pentapeptide translocase , phospho MurNAc pentapeptide transferase , phospho NAc muramoyl pentapeptide translocase UMP , phosphoacetylmuramoylpentapeptide translocase , and phosphoacetylmuramoylpentapeptidetransferase . This enzyme participates in peptidoglycan biosynthesis . References reflist 1 cite journal author Heydanek MG Jr, Neuhaus FC date 1969 title The initial stage in peptidoglycan synthesis. IV. Solubilization of phospho N acetylmuramyl pentapeptide translocase journal Biochemistry. volume 8 pages 1474&ndash 81 pmid 5805290 doi 10.1021 bi00832a024 issue 4 cite journal author Higashi Y, Strominger JL, Sweeley CC date 1967 title Structure of a lipid ... more details
Technical date October 2009 enzyme Name glycerophospholipid arachidonoyl transferase CoA independent EC number 2.3.1.147 CAS number 102347 79 5 IUBMB EC number 2 3 1 147 GO code 0047177 image width caption In the field of enzymology , a glycerophospholipid arachidonoyl transferase CoA independent EC number 2.3.1.147 is an enzyme that catalysis catalyzes the chemical reaction 1 organyl 2 arachidonoyl sn glycero 3 phosphocholine 1 organyl 2 lyso sn glycero 3 phosphoethanolamine math rightleftharpoons math 1 organyl 2 arachidonoyl sn glycero 3 phosphoethanolamine 1 organyl 2 lyso sn glycero 3 phosphocholine This enzyme catalyzes the transfer of arachidonic acid and other polyenoic fatty acids from intact choline or ethanolamine containing glycerophospholipid s to the sn 2 position of a lyso glycerophospholipid. The organyl group on sn 1 of the donor or acceptor molecule can be alkyl, acyl or alk 1 enyl. This enzyme belongs to the family of transferase s, specifically those acyltransferase s transferring groups other than aminoacyl groups. Nomenclature The systematic name of this enzyme class is 1 organyl 2 arachidonoyl sn glycero 3 phosphocholine 1 organyl 2 lys o sn glycero 3 phosphoethanolamine arachidonoyltransferase CoA independent . References Reflist 1 Cite journal author Robinson M, Blank ML, Snyder F date 1985 title Acylation of lysophospholipids by rabbit alveolar macrophages Specificities of CoA dependent and CoA independent reactions journal J. Biol. Chem. volume 260 pages 7889&ndash 95 pmid 4008481 issue 13 Cite journal author Snyder F, Lee TC, Blank ML date 1992 title The role of transacylases in the metabolism of arachidonate and platelet activating factor journal Prog. Lipid. Res. volume 31 pages 65&ndash 86 pmid 1641397 doi 10.1016 0163 7827 92 90016 C issue 1 DEFAULTSORT Glycerophospholipid Arachidonoyl Transferase Coa Independent Category EC 2.3.1 Category Enzymes of unknown structure Transferase stub it Glicerofosfolipide arachidonoil transferasi CoA ... more details
Pfam box Symbol GST C Name Glutathione S transferase, C terminal domain image PDB 1z9h EBI.jpg width caption Pfam PF00043 InterPro IPR004046 SMART Prosite SCOP 2gst TCDB OPM family 139 OPM protein 1z9h CDD cd00299 PDB PDB3 1gnw A 111 206 PDB3 1bx9 A 111 206 PDB3 1aw9 107 202 PDB3 1bye B 110 201 PDB3 1axd A 110 201 PDB3 1pn9 B 104 190 PDB3 1jlv B 111 185 PDB3 1r5a A 126 192 PDB3 1n2a A 100 189 PDB3 1a0f B 100 189 PDB3 2pmt B 100 189 PDB3 1pmt 100 189 PDB3 1f2e D 100 189 PDB3 1nhy A 107 199 PDB3 2cz3 A 105 197 PDB3 2cz2 A 105 197 PDB3 1fw1 A 153 197 PDB3 1e6b A 111 203 PDB3 1oe7 A 102 196 PDB3 1oe8 A 102 196 PDB3 1u3i A 102 196 PDB3 1k0d C 223 345 PDB3 1hqo A 223 345 PDB3 1k0b C 223 345 PDB3 1k0c A 223 345 PDB3 1g6y B 223 345 PDB3 1k0a A 223 345 PDB3 1g6w C 223 345 PDB3 1jzr D 223 345 PDB3 2ljr A 128 201 PDB3 1ljr B 128 201 PDB3 2c3n D 111 200 PDB3 2c3t D 111 200 PDB3 2c3q D 111 200 PDB3 1v2a C 103 188 PDB3 1z9h B 276 370 PDB3 1eem A 114 210 PDB3 1oyj C 106 205 PDB3 1gwc B 122 203 PDB3 1gum E 100 192 PDB3 1xwg A 99 192 PDB3 1pl2 B 99 192 PDB3 1pkw B 99 192 PDB3 1pkz B 99 192 PDB3 1usb A 99 192 PDB3 1guh A 99 192 PDB3 1pl1 B 99 192 PDB3 1gsd A 99 192 PDB3 1gsf A 99 192 PDB3 1k3l B 99 192 PDB3 1gse A 99 192 PDB3 1k3o B 99 192 PDB3 1ydk A 99 192 PDB3 1k3y B 99 192 PDB3 1tdi A 99 192 PDB3 1ml6 A 99 192 PDB3 1f3b A 99 192 PDB3 1f3a B 99 192 PDB3 1ev9 A 99 192 PDB3 1ev4 A 99 192 PDB3 1vf3 ... PDB3 1tu7 B 94 186 PDB3 1m0u A 141 235 PDB3 2gsq 95 189 PDB3 1gsq 95 189 Glutathione S transferase, C terminal domain is a structural domain of glutathione S transferase GST . GST conjugates reduced glutathione ... cite journal author Board P, Chelvanayagam G, Dulhunty A, Gage P, Curtis S title The glutathione transferase ... transferase zeta reveals the molecular basis for its remarkable catalytic promiscuity journal Biochemistry ... Further reading Three dimensional structure of Escherichia coli glutathione S transferase complexed ... S Transferase, C Terminal Domain Category Protein domains Category Single pass transmembrane proteins ... more details
enzyme Name N acetyllactosaminide beta 1,6 N acetylglucosaminyltransferase EC number 2.4.1.150 CAS number 85638 40 0 IUBMB EC number 2 4 1 150 GO code 0008109 image width caption In enzymology , a N acetyllactosaminide beta 1,6 N acetylglucosaminyl transferase EC number 2.4.1.150 is an enzyme that catalysis catalyzes the chemical reaction UDP N acetyl D glucosamine beta D galactosyl 1,4 N acetyl D glucosaminyl R math rightleftharpoons math UDP N acetyl beta D glucosaminyl 1,6 beta D galactosyl 1,4 N acetyl D glucosaminyl R Thus, the two substrate biochemistry substrates of this enzyme are UDP N acetyl D glucosamine and beta D galactosyl 1,4 N acetyl D glucosaminyl R , whereas its 3 product chemistry products are uridine diphosphate UDP , N acetyl beta D glucosaminyl 1,6 beta D galactosyl 1,4 N acetyl D , and glucosaminyl R . This enzyme belongs to the family of glycosyltransferase s, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP N acetyl D glucosamine beta D galactosyl 1,4 N acetyl D glucosam inide beta 1,6 N acetyl D glucosaminyltransferase . Other names in common use include N acetylglucosaminyltransferase , uridine diphosphoacetylglucosamine acetyllactosaminide , beta1 6 acetylglucosaminyltransferase , Galbeta1 4GlcNAc R beta1 6 N acetylglucosaminyltransferase , and UDP GlcNAc Gal R, beta D 6 N acetylglucosaminyltransferase . This enzyme participates in glycosphingolipid biosynthesis neo lactoseries and glycan structures biosynthesis 2 . References reflist 1 cite journal author van den Eijnden DH, Winterwerp H, Smeeman P, Schiphorst WE date 1983 title Novikoff ascites tumor cells contain N acetyllactosaminide beta 1 leads to 3 and beta 1 leads to 6 N acetylglucosaminyltransferase activity journal J. Biol. Chem. volume 258 pages 3435&ndash 7 pmid 6219989 issue 6 enzyme stub Category EC 2.4.1 Category Enzymes of unknown structure ... more details
enzyme Name poly ribitol phosphate N acetylglucosaminyltransferase EC number 2.4.1.70 CAS number 37277 71 7 IUBMB EC number 2 4 1 70 GO code 0047269 image width caption In enzymology , a poly ribitol phosphate N acetylglucosaminyl transferase EC number 2.4.1.70 is an enzyme that catalysis catalyzes the chemical reaction UDP N acetyl D glucosamine poly ribitol phosphate math rightleftharpoons math UDP N acetyl D glucosaminyl poly ribitol phosphate Thus, the two substrate biochemistry substrates of this enzyme are UDP N acetyl D glucosamine and poly ribitol phosphate , whereas its two product chemistry products are uridine diphosphate UDP and N acetyl D glucosaminyl poly ribitol phosphate . This enzyme belongs to the family of glycosyltransferase s, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP N acetyl D glucosamine poly ribitol phosphate N acetyl D glucosaminyltransferase . Other names in common use include UDP acetylglucosamine poly ribitol phosphate , acetylglucosaminyltransferase , uridine diphosphoacetylglucosamine poly ribitol phosphate , and acetylglucosaminyltransferase . References reflist 1 cite journal author Nathenson SG, Ishimoto N and Strominger JL date 1966 title UDP N acetylglucosamine polyribitol phosphate N acetylglucosaminyltransferases from Staphylococcus aureus journal Methods Enzymol. volume 8 pages 426&ndash 429 doi 10.1016 0076 6879 66 08079 0 series Methods in Enzymology isbn 9780121818081 enzyme stub Category EC 2.4.1 Category Enzymes of unknown structure it Poli ribitolo fosfato N acetilglucosaminil transferasi ... more details
wiktionary transpeptidase transpeptidation Transpeptidase may refer to DD transpeptidase , a bacterial enzyme that cross links the peptidoglycan chains to form rigid cell walls Peptidyl transferase , which acts as an enzyme in ribosomes Gamma glutamyl transpeptidase , a liver enzyme D glutamyl transpeptidase disambiguation ... more details
Image Chloramphenicol 2D skeletal.svg thumb Chloramphenicol Image Thiamphenicol.svg thumb Thiamphenicol Amphenicols are a class of antibiotics with a phenylpropanoid structure. They function by blocking the enzyme peptidyl transferase on the 50S ribosome subunit of bacteria . ref http www.apvma.gov.au archive gazette0307p13.shtml APVMA Florfenicol ref Examples of amphenicols include chloramphenicol , thiamphenicol , azidamfenicol and florfenicol . The first in class compound was chloramphenicol, introduced in 1949. Chloramphenicol was initially discovered as a natural product, but all amphenicols are now made by chemical synthesis. References references Amphenicols Category Amphenicols antibiotic stub es Fenicol fr Ph nicol ro Amfenicol wuu ... more details
Image Act acp.png thumbnail Streptomyces coeli color actinorhodin polyketide synthase acyl carrier protein PDB 2AF8 The acyl carrier protein ACP is an important component in both fatty acid and polyketide biosynthesis with the growing chain bound during synthesis as a thiol ester at the distal thiol of a 4 phosphopantethiene moiety. The protein is expressed in the inactive apo form and the 4 phosphopantetheine moiety must be post translationally attached to a conserved serine residue on the ACP by the action of holo acyl carrier protein synthase ACPS , a phosphopantetheinyl transferase. 4 Phosphopantetheine is an essential prosthetic group of several acyl carrier proteins involved in pathways of primary and secondary metabolism including the acyl carrier proteins ACP of fatty acid synthase s, ACPs of polyketide synthase s, and peptidyl carrier proteins PCP and aryl carrier proteins ArCP of nonribosomal peptide synthetases NRPS . Phosphopantetheine fulfills two demands in these biosynthetic pathways. First, the intermediates remain covalently linked to the synthases or synthetases in an energy rich linkage. Second, the flexibility and length of the phosphopantetheine chain approximately 2 nm allows the covalently tethered intermediates to have access to spatially distinct enzyme active sites. This increases the effective molarity of the intermediate and allows an assembly line like process. The ACPs are small negatively charged helical bundle proteins with a high degree of structural and amino acid similarity. The structures of a number of acyl carrier proteins have been solved using various Protein NMR NMR and crystallography techniques. The ACPs are related in structure and mechanism to the peptidyl carrier proteins PCP from nonribosomal peptide synthases. External links MeshName Acyl Carrier Protein Carrier proteins Category Proteins id ACP pl ACP bia ko zh ... more details
chembox Verifiedfields changed verifiedrevid 376113993 ImageFile1 Pleuromutilin skeletal.svg IUPACName 4 R ,5 S ,6 S ,8 R ,9a R ,10 R 6 Ethenyl 5 hydroxy 4,6,9,10 tetramethyl 1 oxodecahydro 3a,9 propanocyclopenta 8 annulen 8 yl hydroxyacetate OtherNames Section1 Chembox Identifiers CASNo Ref cascite correct ?? CASNo 125 65 5 PubChem 31326 ChEMBL Ref ebicite changed EBI ChEMBL 497295 SMILES CC12C C CCC3 CCC O C23 C C C O C C C C CC1OC O CO Section2 Chembox Properties Formula C sub 22 sub H sub 34 sub O sub 5 sub MolarMass 378.502 g mol Appearance Density MeltingPt BoilingPt Solubility Section3 Chembox Hazards MainHazards FlashPt Autoignition Pleuromutilin and its derivatives are antibacterial drugs that inhibit protein synthesis in bacteria by binding to the peptidyl transferase component of the 50S subunit of ribosome s. ref cite journal last Long first Katherine S title Interaction of Pleuromutilin Derivatives with the Ribosomal Peptidyl Transferase Center journal Antimicrobial Agents and Chemotherapy date April 2006 volume 50 issue 4 pages 1458 1462 url http aac.asm.org cgi reprint 50 4 1458.pdf doi 10.1128 AAC.50.4.1458 1462.2006 pmid 16569865 first2 LH first3 L first4 B pmc 1426994 ref ref cite doi 10.1021 jm800261u ref This class of antibiotics includes retapamulin licenced for topical use in humans , valnemulin and tiamulin approved for use in animals and the investigational drug s File Azamulin skeletal.svg azamulin and BC 3781 . History Pleuromutilin was first discovered as an antibiotic in 1950. ref Cite journal last Novak first R authorlink coauthors Shlaes DM title The pleuromutilin antibiotics a new class for human use journal Current Opinion in Investigational Drugs volume 11 issue 2 pages 182 91 publisher location date 2010 Feb url jstor issn doi id mr zbl jfm accessdate 2011 08 02 pmid 20112168 ref It is derived from the fungus Clitopilus passeckerianus formerly Pleurotus passeckerianus , and has also been found in Drosophila subatrata , Clitopilus sc ... more details
domains, within which domain V is most important in its peptidyltransferase activity. Each domain ... peptidyl transfer reaction , prevents premature polypeptide hydrolysis, provides a binding site for the G ... elongation , and termination , and helps protein folding after synthesis. Promotes peptidyl transfer reaction and prevents peptidyl hydrolysis An induced fit mechanism has been revealed for how 50S catalyze peptidyl transfer reaction and prevent peptidyl hydrolysis. The amino group of aminoacyl tRNA binds to A site attacks the carbon of carbonyl group of peptidyl tRNA binds to P site and finally ... . An induced fit mechanism to promote peptide bond formation and exclude hydrolysis of peptidyl ... more details
Orphan date July 2011 Infobox protein family Symbol CPT Name Chloramphenicol phosphotransferase like protein image PDB 1zp6 EBI.jpg width caption crystal structure of atu3015, a putative cytidylate kinase from agrobacterium tumefaciens, northeast structural genomics target atr62 Pfam PF07931 Pfam clan CL0023 InterPro IPR012853 SMART PROSITE MEROPS SCOP 1grq TCDB OPM family OPM protein CAZy CDD In molecular biology, the chloramphenicol phosphotransferase like protein family includes the chloramphenicol 3 O phosphotransferase CPT expressed by Streptomyces venezuelae . Chloramphenicol Cm is a metabolite produced by this bacterium that can inhibit ribosomal peptidyl transferase activity and therefore protein production. By transferring a phosphate group to the C 3 hydroxyl group of Cm, CPT inactivates this potentially lethal metabolite. ref name pmid11468347 cite journal author Izard T title Structural basis for chloramphenicol tolerance in Streptomyces venezuelae by chloramphenicol phosphotransferase activity journal Protein Sci. volume 10 issue 8 pages 1508 13 year 2001 month August pmid 11468347 pmc 2374082 doi 10.1002 pro.101508 url ref ref name pmid10835366 cite journal author Izard T, Ellis J title The crystal structures of chloramphenicol phosphotransferase reveal a novel inactivation mechanism journal EMBO J. volume 19 issue 11 pages 2690 700 year 2000 month June pmid 10835366 pmc 212772 doi 10.1093 emboj 19.11.2690 url ref References reflist InterPro content IPR012853 DEFAULTSORT Chloramphenicol Phosphotransferase Like Protein Family Category Protein domains ... more details
Chembox verifiedrevid 444051451 ImageFile Phosphopantetheine.svg ImageSize IUPACName OtherNames Section1 Chembox Identifiers ChemSpiderID Ref chemspidercite correct chemspider ChemSpiderID 103123 InChI 1 C11H23N2O7PS c1 11 2,7 20 21 17,18 19 9 15 10 16 13 4 3 8 14 12 5 6 22 h9,15,22H,3 7H2,1 2H3, H,12,14 H,13,16 H2,17,18,19 t9 m0 s1 InChIKey JDMUPRLRUUMCTL VIFPVBQEBX StdInChI Ref stdinchicite correct chemspider StdInChI 1S C11H23N2O7PS c1 11 2,7 20 21 17,18 19 9 15 10 16 13 4 3 8 14 12 5 6 22 h9,15,22H,3 7H2,1 2H3, H,12,14 H,13,16 H2,17,18,19 t9 m0 s1 StdInChIKey Ref stdinchicite correct chemspider StdInChIKey JDMUPRLRUUMCTL VIFPVBQESA N CASNo 2226 71 3 PubChem 115254 DrugBank Ref drugbankcite correct drugbank DrugBank DB03912 ChEBI Ref ebicite correct EBI ChEBI 4222 SMILES O C NCCS CCNC O C H O C C C COP O O O MeSHName phosphopantetheine Section2 Chembox Properties Formula C sub 11 sub H sub 23 sub N sub 2 sub O sub 7 sub PS MolarMass 358.349 g mol Appearance Density MeltingPt BoilingPt Section3 Chembox Hazards Solubility MainHazards FlashPt Autoignition 4 Phosphopantetheine is an essential prosthetic group of acyl carrier protein ACP and peptidyl carrier protein s PCP and aryl carrier protein s ArCP derived from Coenzyme A . ref cite journal author Elovson J, Vagelos PR title Acyl carrier protein. X. Acyl carrier protein synthetase journal J. Biol. Chem. volume 243 issue 13 pages 3603 11 year 1968 month July pmid 4872726 ref It is also present in formyltetrahydrofolate dehydrogenase . ref cite journal author Strickland KC, Hoeferlin LA, Oleinik NV, Krupenko NI, Krupenko SA title Acyl carrier protein specific 4 phosphopantetheinyl transferase activates 10 formyltetrahydrofolate dehydrogenase journal J. Biol. Chem. volume 285 issue 3 pages 1627 33 year 2010 month January pmid 19933275 doi 10.1074 jbc.M109.080556 url pmc 2804320 ref Functions Phosphopantetheine fulfills two demands. First, the intermediates remain covalently linked to the synthases or synthetases in ... more details
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