ref ImageFileL1 L selenocysteine 2D skeletal.png ImageSizeL1 120px ImageFileR1 Selenocysteine 3D vdW.png ImageSizeR1 120px IUPACName 3 Selanyl 2 aminopropanoic acid OtherNames small L small Selenocysteine ... BoilingPt Solubility Section3 Chembox Hazards MainHazards FlashPt Autoignition Selenocysteine Sec ... symbol U for selenocysteine. ref cite journal author IUPAC IUBMB Joint Commission on Biochemical ... ref Structure Selenocysteine has a structure similar to that of cysteine , but with an atom of selenium ... pH. Proteins that contain one or more selenocysteine residues are called selenoprotein s. Biology Selenocysteine has both a lower pKa 5.47 and a higher reduction potential than cysteine. These properties ... author BJ. Byun and YK. Kang title Conformational preferences and pK a value of selenocysteine ... ref Unlike other amino acids present in biological protein s, selenocysteine is not coded for directly ... factors ref cite journal author J. Donovan and PR. Copeland title The efficiency of selenocysteine ... enzyme. The UGA codon is made to encode selenocysteine by the presence of a SECIS element SElenoCysteine Insertion Sequence in the mRNA . The SECIS element is defined by characteristic nucleotide ... UGA codons to encode selenocysteine residues ref cite journal author MJ. Berry and al. title Functional characterization of the eukaryotic SECIS elements which direct selenocysteine insertion at UGA codons ... pmc articles PMC413599 ref . Unlike the other amino acids, no free pool of selenocysteine exists ... reactive selenide form H sub 2 sub Se . Selenocysteine synthesis occurs on a specialized tRNA , which ... of selenocysteine tRNA, tRNA Sec , differ from those of standard tRNAs in several respects, most ... arm, and substitutions at several well conserved base positions. The selenocysteine tRNAs are initially ... . Rather, the tRNA bound seryl residue is converted to a selenocysteine residue by the pyridoxal phosphate containing enzyme selenocysteine synthase. Finally, the resulting Sec tRNA Sec is specifically ... more details
enzyme Name selenocysteine lyase EC number 4.4.1.16 CAS number 82047 76 5 IUBMB EC number 4 4 1 16 GO code 0009000 image width caption In enzymology , a selenocysteine lyase EC number 4.4.1.16 is an enzyme that catalysis catalyzes the chemical reaction L selenocysteine reduced acceptor math rightleftharpoons math selenide L alanine acceptor Thus, the two substrate biochemistry substrates of this enzyme are L selenocysteine and reduced acceptor , whereas its 3 product chemistry products are selenide , L alanine , and Electron acceptor acceptor . This enzyme belongs to the family of lyase s, specifically the class of carbon sulfur lyases. The systematic name of this enzyme class is L selenocysteine selenide lyase L alanine forming . Other names in common use include selenocysteine reductase , and selenocysteine beta lyase . This enzyme participates in selenoamino acid metabolism . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . 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 1I29 , PDB link 1JF9 , PDB link 1KMJ , and PDB link 1KMK . References reflist 1 cite journal author Esaki N, Nakamura T, Tanaka H, Soda K date 1982 title Selenocysteine lyase, a novel enzyme that specifically acts on selenocysteine. Mammalian distribution and purification and properties of pig liver enzyme journal J. Biol. Chem. volume 257 pages 4386&ndash 91 pmid 6461656 issue 8 enzyme stub Category EC 4.4.1 Category Pyridoxal phosphate enzymes Category Enzymes of known structure ... more details
Orphan date February 2009 Unreferenced date September 2008 A thioselenide is a compound containing a selenium sulfur bond. The mammalian version of the protein thioredoxin reductase contains a selenocysteine residue which forms a thioselenide analogous to a disulfide upon oxidation. The selenium sulfur bond length is about 220 picometers. Category Organosulfur compounds Category Organoselenium compounds ... more details
PBB geneid 7296 Thioredoxin reductase 1, cytoplasmic is an enzyme that in humans is encoded by the TXNRD1 gene . ref name pmid7589432 cite journal author Gasdaska PY, Gasdaska JR, Cochran S, Powis G title Cloning and sequencing of a human thioredoxin reductase journal FEBS Lett volume 373 issue 1 pages 5 9 year 1995 month Nov pmid 7589432 pmc doi 10.1016 0014 5793 95 01003 W 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 This gene encodes a member of the family of pyridine nucleotide oxidoreductases. This protein reduces thioredoxins as well as other substrates, and plays a role in selenium metabolism and protection against oxidative stress. The functional enzyme is thought to be a homodimer which uses FAD as a cofactor. Each subunit contains a selenocysteine Sec residue which is required for catalytic activity. The selenocysteine is encoded by the UGA codon that normally signals translation termination. The 3 UTR of selenocysteine containing genes have a common stem loop structure, the sec insertion sequence SECIS , that is necessary for the recognition of UGA as a Sec codon rather than as a stop signal. Alternative splicing results in several transcript variants encoding the same or different isoforms. ref cite web title Entrez Gene TXNRD1 thioredoxin reductase 1 url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 7296 accessdate ref See also Thioredoxin reductase References reflist refbegin 2 PBB Further reading citations refend PDB Gallery geneid 7296 gene 12 stub NLM content The PBB Controls template provides controls for Protein Box Bot, please see Template PBB Controls for details. PBB Controls update page yes require manual inspection no update protein box yes update summary yes update citations yes Category Selenoproteins ... 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
Infobox rfam Name Selenocysteine insertion sequence 1 image RF00031.jpg width caption Predicted secondary structure and sequence conservation of SECIS 1 Symbol SECIS 1 AltSymbols SECIS Rfam RF00031 miRBase miRBase family RNA type Cis regulatory element Cis reg Tax domain Eukaryota GO GO 0001514 SO SO 1001274 CAS number EntrezGene HGNCid OMIM PDB RefSeq Chromosome Arm Band LocusSupplementaryData In biology , the SECIS element SECIS se leno c ysteine i nsertion s equence is an cis regulatory element RNA element around 60 nucleotides in length that adopts a stem loop structure. ref cite journal last Walczak first R coauthors Westhof E, Carbon P, Krol A year 1996 title A novel RNA structural motif in the selenocysteine insertion element of eukaryotic selenoprotein mRNAs journal RNA volume 2 pages 367&ndash 379 pmid 8634917 issue 4 pmc 1369379 ref This structural motif pattern of nucleotides directs the cell biology cell to translation biology translate UGA codon s as selenocysteine s. UGA is normally a stop codon . SECIS elements are thus a fundamental aspect of messenger RNA s encoding selenoprotein s, proteins that include one or more selenocysteine residues. In bacteria the SECIS element appears soon after the UGA codon it affects. In archaea and eukaryote s, it occurs in the 3 UTR of an mRNA , and can cause multiple UGA codons within the mRNA to code for selenocysteine. One archaeal SECIS element, in Methanococcus , is located in the 5 UTR . The SECIS element appears defined by sequence characteristics, i.e. particular nucleotides tend to be at particular positions in it, and a characteristic secondary structure . The secondary structure is the result of base pairing of complementary RNA nucleotides, and causes a hairpin like structure. The eukaryotic SECIS element includes ... first A coauthors Lescure A, Gautheret D year 2002 title A survey of metazoan selenocysteine insertion ... author Mourier T, Pain A, Barrell B, Griffiths Jones S title A selenocysteine tRNA and SECIS element ... more details
for the airport with that ICAO code Cotopaxi International Airport Orphan date February 2009 PBB geneid 51714 Selenoprotein T , also known as SELT , is a protein that in humans is encoded by the SELT gene . ref name pmid10567350 cite journal author Kryukov GV, Kryukov VM, Gladyshev VN title New mammalian selenocysteine containing proteins identified with an algorithm that searches for selenocysteine insertion sequence elements journal J. Biol. Chem. volume 274 issue 48 pages 33888 97 year 1999 month November pmid 10567350 doi 10.1074 jbc.274.48.33888 url issn ref ref name pmid12775843 cite journal author Kryukov GV, Castellano S, Novoselov SV, Lobanov AV, Zehtab O, Guig R, Gladyshev VN title Characterization of mammalian selenoproteomes journal Science volume 300 issue 5624 pages 1439 43 year 2003 month May pmid 12775843 doi 10.1126 science.1083516 url issn ref ref name entrez cite web title Entrez Gene SELT selenoprotein T url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 51714 accessdate ref Gene The selenocysteine is encoded by the UGA codon that normally signals translation termination. The 3 UTR of selenoprotein genes have a common stem loop structure, the sec insertion sequence SECIS , that is necessary for the recognition of UGA as a Sec codon rather than as a stop signal. ref name entrez Protein structure Selenoprotein T contains a selenocysteine Sec residue at its active site. See also selenoprotein References reflist Further reading refbegin 2 PBB Further reading citations cite journal author Otsuki T, Ota T, Nishikawa T, et al. title Signal sequence and keyword trap in silico for selection of full length human cDNAs encoding secretion or membrane proteins from oligo capped cDNA libraries journal DNA Res. volume 12 issue 2 pages 117 26 year 2007 pmid 16303743 doi 10.1093 dnares 12.2.117 cite journal author Gerhard DS, Wagner L, Feingold EA, et al. title The status, quality, and expansion of the NIH full length cDNA project ... more details
In molecular biology a selenoprotein is any protein that includes a selenocysteine Se Cys amino acid residue. Among functionally characterized selenoproteins are five glutathione peroxidase s GPX and three thioredoxin reductase s, TrxR TXNRD which both contain only one Se Cys. ref name pmid11997494 cite journal author Hatfield DL, Gladyshev VN title How selenium has altered our understanding of the genetic code journal Mol. Cell. Biol. volume 22 issue 11 pages 3565 76 year 2002 month June pmid 11997494 pmc 133838 doi 10.1128 MCB.22.11.3565 3576.2002 url issn ref Selenoprotein P is the most common selenoprotein found in the plasma. It is unusual because in humans it contains 10 Se Cys residues, which are split into two domains, a longer N terminal domain that contains 1 Se Cys, and a shorter C terminal domain that contains 9 Se Cys. The longer N terminal domain is likely an enzymatic domain, and the shorter C terminal domain is likely a means of safely transporting the very reactive Selenium atom throughout the body. ref cite journal author Burk RF, Hill KE title Selenoprotein P an extracellular protein with unique physical characteristics and a role in selenium homeostasis journal Annu Rev Nutr year 2005 volume 25 pages 215 235 pmid 16011466 doi 10.1146 annurev.nutr.24.012003.132120 ref ref cite journal author Burk RF, Hill KE title Selenoprotein P expression, functions, and roles ... in the respective organism. Types Besides the selenocysteine containing selenoproteins ... at least in bacterial cells , unspecific incorporation of selenocysteine in lieu of cysteine seems to be highly toxic. This may be one reason for the existence of a rather complicated pathway of selenocysteine ... amino acid as intermediate. Thus, even if a selenocysteine containing selenoprotein is taken ... a new selenocysteine for incorporation into a selenoprotein. Clinical significance Selenium is a vital nutrient in animal s, including humans . About 25 different selenocysteine containing selenoproteins ... more details
enjoy limited applications in organic synthesis . Image L selenocysteine 2D skeletal.png 180px thumb small L small selenocysteine , a naturally occurring selenol. Biochemical role Selenols are important ... in these proteins are part of the essential amino acid selenocysteine . ref name Wessjohann Preparation ... more details
PBB geneid 51734 Methionine R sulfoxide reductase B1 is an enzyme that in humans is encoded by the SEPX1 gene . ref name pmid10608886 cite journal author Lescure A, Gautheret D, Carbon P, Krol A title Novel selenoproteins identified in silico and in vivo by using a conserved RNA structural motif journal J Biol Chem volume 274 issue 53 pages 38147 54 year 2000 month Feb pmid 10608886 pmc doi 10.1074 jbc.274.53.38147 ref ref name entrez cite web title Entrez Gene SEPX1 selenoprotein X, 1 url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 51734 accessdate 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 This gene encodes a selenoprotein, which contains a selenocysteine Sec residue at its active site. The selenocysteine is encoded by the UGA codon that normally signals translation termination. The 3 UTR of selenoprotein genes have a common stem loop structure, the sec insertion sequence SECIS , that is necessary for the recognition of UGA as a Sec codon rather than as a stop signal. This protein belongs to the Methionine oxidation methionine sulfoxide reductase B MsrB family, and it is expressed in a variety of adult and fetal tissues. ref name entrez See also MSRA gene MSRB2 Methionine oxidation References reflist Further reading refbegin 2 PBB Further reading citations cite journal author Bonaldo MF, Lennon G, Soares MB title Normalization and subtraction two approaches to facilitate gene discovery. journal Genome Res. volume 6 issue 9 pages 791 806 year 1997 pmid 8889548 doi 10.1101 gr.6.9.791 cite journal author Kryukov GV, Kryukov VM, Gladyshev VN title New mammalian selenocysteine containing proteins identified with an algorithm that searches for selenocysteine insertion sequence elements. journal J. Biol. Chem. volume 274 issue 48 pages 33888 97 year 1999 pmid 10567350 doi 10.1074 jbc.274.48.33888 cite journal author Zhang ... more details
hydrogenases the first cysteine of the C terminal motif is a selenocysteine which has experimentally ... MK, Scott RA, Moura JJ, Legall J, Peck Jr HD, Prickril BC, DerVartanian DV title Evidence for selenocysteine ... more details
is able to produce numerous Seleno and Pyrroproteins, which contains the amino acids selenocysteine ... content of proteins containing 21st and 22nd amino acids, selenocysteine and pyrrolysine, in a symbiotic ... more details
dictate selenocysteine incorporation efficiency and selenoprotein hierarchy journal EMBO J. volume ... selenocysteine insertion sequence SECIS binding protein 2 journal Gene volume 291 issue 1 2 pages 279 ... journal author Papp LV title The Redox State of SECIS Binding Protein 2 Controls Its Localization and Selenocysteine ... more details
wiktionarypar sec SEC TOCright SEC , Sec , or Se may refer to Sports Southeastern Conference SEC , one of the BCS Conference major U.S. collegiate sports conferences Government U.S. Securities and Exchange Commission Securities and Exchange Commission Philippines State Examinations Commission , Ireland State Electricity Commission of Victoria Australia State Energy Commission of Western Australia Securities and Exchange Commission of Pakistan Securities and Exchange Commission Nigeria Education St Edmunds College, Ipswich Companies Samsung Electronics Corporation Solar Entertainment Corporation Securities Exchange Company, a company run by Charles Ponzi AuroraSEC Solar Energy Company Mathematics secant Science Human based genetic algorithm Social evolutionary computation Space Weather Prediction Center , also known as the Space Enviornment Center single error correction, in error detection and correction Size exclusion chromatography Sec pathway , in biology, a major route of protein translocation across cell membranes Solar Energy Conversion, the conversion of solar energy to electricity Standard three letter abbreviation for selenocysteine Sinusoidal endothelial cell Religion Scottish Episcopal Church Popular culture Cult of Skaro Dalek Sec , from the television series Doctor Who . Other An abbreviation for second Sec wine , a French term used to indicate the sweetness level of a wine. In music, sec , an abbreviation of Glossary of musical terminology secco . disambig ca SEC de SEC es SEC eo SEC fr Sec ko SEC it SEC nl SEC ja SEC no SEC ru SEC sr Sec sv SEC zh SEC ... more details
Orphan date February 2009 PBB geneid 22929 Selenide, water dikinase 1 is an enzyme that in humans is encoded by the SEPHS1 gene . ref name pmid7665581 cite journal author Low SC, Harney JW, Berry MJ title Cloning and functional characterization of human selenophosphate synthetase, an essential component of selenoprotein synthesis journal J Biol Chem volume 270 issue 37 pages 21659 64 year 1995 month Oct pmid 7665581 pmc doi 10.1074 jbc.270.37.21659 ref ref name entrez cite web title Entrez Gene SEPHS1 selenophosphate synthetase 1 url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 22929 accessdate 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 This protein encodes an enzyme that synthesizes selenophosphate from selenide and ATP. Selenophosphate is the selenium donor used to synthesize selenocysteine, which is co translationally incorporated into selenoproteins at in frame UGA codons. ref name entrez References reflist Further reading refbegin 2 PBB Further reading citations cite journal author Strausberg RL, Feingold EA, Grouse LH, et al. title Generation and initial analysis of more than 15,000 full length human and mouse cDNA sequences. journal Proc. Natl. Acad. Sci. U.S.A. volume 99 issue 26 pages 16899 903 year 2003 pmid 12477932 doi 10.1073 pnas.242603899 pmc 139241 cite journal author Gerhard DS, Wagner L, Feingold EA, et al. title The status, quality, and expansion of the NIH full length cDNA project the Mammalian Gene Collection MGC . journal Genome Res. volume 14 issue 10B pages 2121 7 year 2004 pmid 15489334 doi 10.1101 gr.2596504 pmc 528928 cite journal author Tamura T, Yamamoto S, Takahata M, et al. title Selenophosphate synthetase genes from lung adenocarcinoma cells Sps1 for recycling L selenocysteine and Sps2 for selenite assimilation. journal Proc. Natl. Acad. Sci. U.S.A. volume 101 issue 46 pages 16162 7 year ... more details
PBB geneid 51091 O phosphoseryl tRNA Sec selenium transferase is an enzyme that in humans is encoded by the SEPSECS gene . ref name pmid16230358 cite journal author Xu XM, Mix H, Carlson BA, Grabowski PJ, Gladyshev VN, Berry MJ, Hatfield DL title Evidence for direct roles of two additional factors, SECp43 and soluble liver antigen, in the selenoprotein synthesis machinery journal J Biol Chem volume 280 issue 50 pages 41568 75 year 2005 month Dec pmid 16230358 pmc doi 10.1074 jbc.M506696200 ref ref name pmid10931155 cite journal author Costa M, Rodriguez Sanchez JL, Czaja AJ, Gelpi C title Isolation and characterization of cDNA encoding the antigenic protein of the human tRNP Ser Sec complex recognized by autoantibodies from patients withtype 1 autoimmune hepatitis journal Clin Exp Immunol volume 121 issue 2 pages 364 74 year 2000 month Aug pmid 10931155 pmc 1905695 doi 10.1046 j.1365 2249.2000.01280.x ref ref name pmid17142313 cite journal author Yuan J, Palioura S, Salazar JC, Su D, O Donoghue P, Hohn MJ, Cardoso AM, Whitman WB, Soll D title RNA dependent conversion of phosphoserine forms selenocysteine in eukaryotes and archaea journal Proc Natl Acad Sci U S A volume 103 issue 50 pages 18923 7 year 2006 month Dec pmid 17142313 pmc 1748153 doi 10.1073 pnas.0609703104 ref ref name pmid17194211 cite journal author Xu XM, Carlson BA, Mix H, Zhang Y, Saira K, Glass RS, Berry MJ, Gladyshev VN, Hatfield DL title Biosynthesis of selenocysteine on its tRNA in eukaryotes journal PLoS Biol volume 5 issue 1 pages e4 year 2007 month Apr pmid 17194211 pmc 1717018 doi 10.1371 journal.pbio.0050004 ref ref name entrez cite web title Entrez Gene SLA LP soluble liver antigen liver pancreas antigen url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 51091 accessdate 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 References reflist Further read ... more details
PBB geneid 257202 Glutathione peroxidase 6 GPx 6 is an enzyme that in humans is encoded by the GPX6 gene . ref name entrez cite web title Entrez Gene glutathione peroxidase 6 olfactory url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 257202 accessdate ref ref name pmid12775843 cite journal author Kryukov GV, Castellano S, Novoselov SV, Lobanov AV, Zehtab O, Guig R, Gladyshev VN title Characterization of mammalian selenoproteomes journal Science volume 300 issue 5624 pages 1439 43 year 2003 month May pmid 12775843 doi 10.1126 science.1083516 url issn ref This gene product belongs to the glutathione peroxidase family, which functions in the detoxification of hydrogen peroxide. It contains a selenocysteine Sec residue at its active site. The selenocysteine is encoded by the UGA codon, which normally signals translation termination. The 3 UTR of Sec containing genes have a common stem loop structure, the sec insertion sequence SECIS , which is necessary for the recognition of UGA as a Sec codon rather than as a stop signal. Expression of this gene is restricted to embryos and adult olfactory epithelium. ref name entrez References reflist Further reading refbegin 2 cite journal author Talmud PJ, Drenos F, Shah S, et al. title Gene centric association signals for lipids and apolipoproteins identified via the HumanCVD BeadChip. journal Am. J. Hum. Genet. volume 85 issue 5 pages 628 42 year 2009 pmid 19913121 doi 10.1016 j.ajhg.2009.10.014 pmc 2775832 cite journal author Richard MJ, Guiraud P, Didier C, et al. title Human immunodeficiency virus type 1 Tat protein impairs selenoglutathione peroxidase expression and activity by a mechanism independent of cellular selenium uptake consequences on cellular resistance to UV A radiation. journal Arch. Biochem. Biophys. volume 386 issue 2 pages 213 20 year 2001 pmid 11368344 doi 10.1006 abbi.2000.2197 cite journal author Opalenik SR, Ding Q, Mallery SR, Thompson JA title Glutathione depletion asso ... more details
the rare selenocysteine amino acid and two histidine residues. ref name pmid18815314 ref name pmid9002998 ... ref Selenocysteine is coded by a UGA codon, which generally signifies termination of a peptide through ... PR title Type I iodothyronine deiodinase is a selenocysteine containing enzyme journal Nature volume ... for UGA to be read as a selenocysteine amino acid instead of a stop codon, it is necessary that a downstream stem loop sequence, the selenocysteine insertion sequence SECIS , be present to bind with SECIS ... of selenocysteine is not efficient, ref name pmid9292958 cite journal author St Germain ... more details
In the genetic code , a stop codon or termination codon is a nucleotide triplet within messenger RNA that signals a termination of translation biology translation . ref cite book author Griffiths AJF, Miller JH, Suzuki DT, Lewontin RC, and Gelbart WM title An Introduction to Genetic Analysis year 2000 publisher W.H. Freeman and Company chapterurl http www.ncbi.nlm.nih.gov books bv.fcgi?rid iga.section.1845 1872 chapter Chapter 10 Molecular Biology of Gene Function Genetic code Stop codons ref Protein s are based on polypeptides, which are unique sequences of amino acid s. Most codon s in messenger RNA correspond to the addition of an amino acid to a growing polypeptide chain, which may ultimately become a protein. Stop codons signal the termination of this process by binding release factor s, which cause the ribosomal subunits to disassociate, releasing the amino acid chain. In the standard genetic code, there are several stop codons in RNA UAG amber UAA ochre UGA opal in DNA TAG amber TAA ochre TGA opal or umber See also Genetic code Variations to the standard genetic code l1 variations Mnemonic s UGA U Go Away UAA U Are Away UAG U Are Gone TAG They Are Gone TAA They Are Away TGA They re Going Away The UGA codon has recently been identified as the codon coding for Selenocysteine Sec . This amino acid is found in 25 selenoprotein s where it is located in the active site of the protein. Transcription of this codon is enabled by proximity of the SECIS element SElenoCysteine Incorporation Sequence . ref cite journal pages 775 806 doi 10.1089 ars.2007.1528 title From Selenium to Selenoproteins Synthesis, Identity, and Their Role in Human Health year 2007 last1 Papp first1 Laura Vanda last2 Lu first2 Jun last3 Holmgren first3 Arne last4 Khanna first4 Kum Kum journal Antioxidants & Redox Signaling volume 9 issue 7 pmid 17508906 ref The UAG codon can translate into pyrrolysine in a similar way selenocysteine is encoded. Nonsense mutations are changes in DNA sequence that i ... more details
SECIS element Selenocysteine insertion sequence SECIS directs the cell to translate UGA stop codons as selenocysteine s Metazoa ref cite journal last Walczak first R coauthors Westhof E, Carbon P, Krol A year 1996 title A novel RNA structural motif in the selenocysteine insertion element of eukaryotic ... more details
Orphan date February 2009 PBB geneid 6415 Selenoprotein W is a protein that in humans is encoded by the SEPW1 gene . ref name pmid9256076 cite journal author Gu QP, Beilstein MA, Vendeland SC, Lugade A, Ream W, Whanger PD title Conserved features of selenocysteine insertion sequence SECIS elements in selenoprotein W cDNAs from five species journal Gene volume 193 issue 2 pages 187 96 year 1997 month Sep pmid 9256076 pmc doi 10.1016 S0378 1119 97 00113 3 ref ref name entrez cite web title Entrez Gene SEPW1 selenoprotein W, 1 url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 6415 accessdate 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 This gene encodes a selenoprotein, which contains a selenocysteine Sec residue at its active site. The selenocysteine is encoded by the UGA codon that normally signals translation termination. The 3 UTR of selenoprotein genes have a common stem loop structure, the sec insertion sequence SECIS , that is necessary for the recognition of UGA as a Sec codon rather than as a stop signal. This protein shows highest expression in skeletal muscle and heart, and may be involved in oxidation reduction reactions. A retroprocessed pseudogene, SEPW1P, has been identified and mapped to chromosome 1p35 34. ref name entrez References reflist Further reading refbegin 2 PBB Further reading citations cite journal author Whanger PD title Selenoprotein W a review journal Cell. Mol. Life Sci. volume 57 issue 13 14 pages 1846 52 year 2001 pmid 11215511 doi 10.1007 PL00000666 cite journal author Yeh JY, Beilstein MA, Andrews JS, Whanger PD title Tissue distribution and influence of selenium status on levels of selenoprotein W journal FASEB J. volume 9 issue 5 pages 392 6 year 1995 pmid 7896009 doi cite journal author Smith JS title A transcript map of the chromosome 19q arm glioma tumor suppressor region journal Geno ... more details
of a cDNA coding for human glutathione peroxidase confirms TGA encodes active site selenocysteine ... pmc 305979 cite journal author Mullenbach GT, Tabrizi A, Irvine BD, et al. title Selenocysteine ... more details
enzyme Name coenzyme F420 hydrogenase EC number 1.12.98.1 CAS number 9027 05 8 IUBMB EC number 1 12 98 1 GO code 0050454 image width caption In enzymology , a coenzyme F420 hydrogenase EC number 1.12.98.1 is an enzyme that catalysis catalyzes the chemical reaction H sub 2 sub coenzyme F sub 420 sub math rightleftharpoons math reduced coenzyme F sub 420 sub Thus, the two substrate biochemistry substrates of this enzyme are hydrogen H sub 2 sub and coenzyme F420 , whereas its product chemistry product is reduced coenzyme F420. This enzyme belongs to the family of oxidoreductase s, specifically those acting on hydrogen as donor with other, known, acceptors. The systematic name of this enzyme class is hydrogen coenzyme F420 oxidoreductase . Other names in common use include 8 hydroxy 5 deazaflavin reducing hydrogenase , F420 reducing hydrogenase , and coenzyme F420 dependent hydrogenase . This enzyme participates in folate biosynthesis and is a critical part of energy conservation in some methanogens such as Methanosarcina barkeri . It has 3 cofactor biochemistry cofactors iron , nickel , and deazaflavin . References reflist 1 cite journal author Adams MWW, Mortenson LE and Chen J S date 1981 title Hydrogenase journal Biochim. Biophys. Acta volume 594 pages 105&ndash 176 cite journal author Yamazaki S date 1982 title A selenium containing hydrogenase from Methanococcus vannielii Identification of the selenium moiety as a selenocysteine residue journal J. Biol. Chem. volume 257 pages 7926&ndash 9 pmid 6211447 issue 14 cite journal author Fox JA, Livingston DJ, Orme Johnson WH, Walsh CT date 1987 title 8 Hydroxy 5 deazaflavin reducing hydrogenase from Methanobacterium thermoautotrophicum 1. Purification and characterization journal Biochemistry. volume 26 pages 4219&ndash 27 pmid 3663585 doi 10.1021 bi00388a007 issue 14 cite journal author Muth E, Morschel E, Klein A date 1987 title Purification and characterization of an 8 hydroxy 5 deazaflavin reducing hydrogenase from ... more details
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