chembox verifiedrevid 416135882 Reference ref Merck Index , 12th Edition, 8584 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 3 Selanyl small L ... FlashPt Autoignition Selenocysteine Se Cys is an amino acid that is present in several enzyme ... letter symbol Sec and the one letter symbol U for selenocysteine. ref cite journal author IUPAC ... format reprint, with permission ref Structure Selenocysteine has a structure similar to that of cysteine ... group. Proteins that contain one or more selenocysteine residues are called selenoprotein s. Biology Selenocysteine has both a lower pKa and a higher reduction potential than cysteine. These properties ... acids present in biological protein s, Selenocysteine is not coded for directly in the genetic code ... in a truncated, nonfunctional 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 ... 3 UTR of the mRNA, and can direct multiple UGA codons to encode selenocysteine residues. Unlike the other amino acids, no free pool of selenocysteine exists in the cell. Its high reactivity would ... Se . Selenocysteine synthesis occurs on a specialized tRNA , which also functions to incorporate it into nascent polypeptides. The primary and secondary structure of selenocysteine tRNA, tRNA Sec , differ ... conserved base positions. The selenocysteine tRNAs are initially charged with serine by seryl tRNA ... residue is converted to a selenocysteine residue by the pyridoxal phosphate containing enzyme selenocysteine ... and A. Bock title Nucleotide Sequence and Expression of the Selenocysteine Containing Polypeptide ... author F. Zinoni, A. Birkmann, W. Leinfelder and A. Bock title Cotranslational Insertion of Selenocysteine ... of Selenocysteine as the Organoselenium Moiety year 1976 journal PNAS volume 73 issue 8 pages 2659 ... 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 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 ... more details
Rfam box acc RF00031 description Selenocysteine insertion sequence abbreviation SECIS avg length 64.70 avg identity 44.00 type Cis reg se Gautheret D, PMID 12458087 ss Published PMID 12458087 release 10.0 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 non canonical A G base pairs, which are uncommon in nature, but are critically important for correct SECIS element function. Although the eukaryotic, archaeal and bacterial SECIS elements each ... first A coauthors Lescure A, Gautheret D year 2002 title A survey of metazoan selenocysteine ... journal author Mourier T, Pain A, Barrell B, Griffiths Jones S title A selenocysteine tRNA and SECIS ... 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
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 and humans . About 25 different selenocysteine containing selenoproteins have ... more details
Culemann E, Harney JW, Berry MJ title SECIS SBP2 interactions dictate selenocysteine incorporation ..., Yamada K, et al. title cDNA cloning, expression pattern and RNA binding analysis of human selenocysteine ... protein 2 controls its localization and selenocysteine incorporation function. journal Mol. Cell. Biol ... more details
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 certain biological ... are part of the essential amino acid selenocysteine . ref name Wessjohann Preparation Selenols are prepared ... more details
Orphan date February 2009 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 sulfoxide reductase B MsrB family, and it is expressed in a variety of adult and fetal tissues. 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 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. ... 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. 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 http www.ncbi.nlm.nih.gov books bv.fcgi?rid iga.section.1845 1872 Chapter 10 Molecular Biology of Gene Function Genetic code Stop codons ref Protein s are based upon polypeptides, which are unique sequences of amino acid s and 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 &mdash stop codons signal the termination of this process, 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 variations . Mnemonic UGA U Go Away UAA U Are Away UAG U Are Gone The UGA codon has recently been identified as the codon coding for Selenocysteine Sec . This amino acid is found in 25 selenoproteins 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 author Papp LV, Lu J, Holmgren A, Khanna KK title From selenium to selenoproteins synthesis, identity, and their role in human health journal Antioxid. Redox Signal. volume 9 issue 7 pages 775 806 year 2007 month July pmid 17508906 doi 10.1089 ars.2007.1528 url ref The UAG codon can translate into pyrrolysine pyrolysin in a similar way selenocysteine is encoded. Nonsense mutations are changes in DNA sequence that introduce a premature stop codon, causing any resulting protein to be abnormally shortened. This often causes a loss of function in the protein, as critical parts of the amino acid chain are no longer created. Beca ... 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 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 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 pag ... 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
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
Image MRNA structure.svg thumb 400px mRNA structure, approximately to scale for a human mRNA, where the median length of 3 UTR is 700 nucleotides The three prime untranslated region 3 UTR is a particular section of messenger RNA mRNA . It follows the coding region . An mRNA molecule codes for a protein through Translation genetics translation . The mRNA also contains regions that are not translated. In eukaryotes these regions are the 5 cap cap , 5 untranslated region , 3 untranslated region , and Polyadenylation polyA tail see diagram . In prokaryotes mRNA structures have some differences see mRNA as do histone mRNAs. However, both have 3 UTRs. Several regulatory sequence s are found in the 3 UTR A polyadenylation signal, usually AAUAAA , or a slight variant. This marks the site of cleavage of the transcript approximately 30 base pair s past the signal, followed by the addition of several hundred adenine residues poly A tail . Binding sites for proteins, that may affect the mRNA s stability or location in the cell, like SECIS element s which direct the ribosome to translate the codon UGA as selenocysteine s rather than as a stop codon , or AU rich element s AREs , stretches consisting of mainly adenine and uracil nucleotides which can either stabilize or destabilize the mRNA depending on the protein bound to it . Binding sites for miRNA s, a type of RNAi . See also Five prime untranslated region UTRdb UTRome References cite journal author Mazumder B, Seshadri V, Fox PL title Translational control by the 3 UTR the ends specify the means journal Trends Biochem. Sci. volume 28 issue 2 pages 91 8 year 2003 pmid 12575997 doi 10.1016 S0968 0004 03 00002 1 External links http transterm.otago.ac.nz RNAMotif.html Brief introduction to mRNA regulatory elements http www.ba.itb.cnr.it UTR UTResource 3 UTR analysis http www.utrome.org UTRome.org 3 UTRs in nematodes Medical Subject Heading http www.ncbi.nlm.nih.gov entrez query.fcgi?cmd Retrieve&db mesh&list uids 68020413&dopt F ... more details
wiktionarypar sec SEC TOCright SEC or Sec or Se can refer to Government U.S. Securities and Exchange Commission United States 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 Companies Samsung Electronics Corporation Solar Entertainment Corporation Securities Exchange Company, a company run by Charles Ponzi Organisations http web2.ulladulla h.schools.nsw.edu.au moodle mod resource view.php?id 644 Student Environment Council SEC , an Australian group of students inspiring and initiating environmental iniatives. UHS . Mathematics secant Science sec., non standard abbreviation for second Human based genetic algorithm Social evolutionary computation Space Weather Prediction Center Space Environment Center single error correction, in error detection and correction Size exclusion chromatography Sec pathway , in biology, a major route of protein targeting protein translocation across cell membranes Solar Energy Conversion, the conversion of solar energy to electricity Standard three letter abbreviation for selenocysteine Sinusoidal endothelial cell Sports Southeastern Conference SEC , one of the BCS conference major U.S. collegiate sports conferences Religion Scottish Episcopal Church Popular culture Cult of Skaro Dalek Sec , from the television series Doctor Who . Other Sec wine , a French term used to indicate the sweetness level of a wine. A sec is a generic amount of time, not linked with the unit of time measurement seconds . 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
In biology, the PYLIS downstream sequence PYLIS py rro l ysine i nsertion s equence is a stem loop structure which appears on some mRNA sequences. This structural motif causes the UAG amber stop codon to be translated to the amino acid pyrrolysine instead of ending the protein translation. In archaea the PYLIS downstream sequence is positioned straight after the UAG codon which is translated as pyrrolysine. ref name pmid16164991 cite journal author Th obald Dietrich A, Gieg R, Rudinger Thirion J title Evidence for the existence in mRNAs of a hairpin element responsible for ribosome dependent pyrrolysine insertion into proteins journal Biochimie volume 87 issue 9 10 pages 813 7 year 2005 pmid 16164991 doi 10.1016 j.biochi.2005.03.006 url ref ref name pmid15788401 cite journal author Zhang Y, Baranov PV, Atkins JF, Gladyshev VN title Pyrrolysine and selenocysteine use dissimilar decoding strategies journal J. Biol. Chem. volume 280 issue 21 pages 20740 51 year 2005 month May pmid 15788401 doi 10.1074 jbc.M501458200 url ref See also SECIS element Pyrrolysine References reflist Further reading cite journal author Longstaff DG, Blight SK, Zhang L, Green Church KB, Krzycki JA title In vivo contextual requirements for UAG translation as pyrrolysine journal Mol. Microbiol. volume 63 issue 1 pages 229 41 year 2007 month January pmid 17140411 doi 10.1111 j.1365 2958.2006.05500.x url cite journal author Namy O, Zhou Y, Gundllapalli S, et al. title Adding pyrrolysine to the Escherichia coli genetic code journal FEBS Lett. volume 581 issue 27 pages 5282 8 year 2007 month November pmid 17967457 doi 10.1016 j.febslet.2007.10.022 url Category Cis regulatory RNA elements Genetics stub fr l ment PYLIS ... 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
of a cDNA coding for human glutathione peroxidase confirms TGA encodes active site selenocysteine ... 15.13.5484 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 . 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 the archaebacterium Methanococcus voltae journal Eur. J. Biochem. volume 169 pages 571&ndash 7 pm ... more details
Image GlutPeroxidase 1GP1.png thumb Glutathione Peroxidase 1 Peroxidases EC number http www.chem.qmul.ac.uk iubmb enzyme EC1 11 1 1.11.1.x are a large family of enzyme s that typically catalyze a reaction of the form ROOR electron donor 2 e sup sup 2H sup sup ROH R OH For many of these enzymes the optimal Substrate biochemistry substrate is hydrogen peroxide , but others are more active with organic hydroperoxides such as lipid peroxides. Peroxidases can contain a heme cofactor biochemistry cofactor in their active sites, or redox redox active cysteine or selenocysteine residues. The nature of the nucleophile electron donor is very dependent on the structure of the enzyme. For example, horseradish peroxidase can use a variety of organic compounds as electron donors and acceptors. Horseradish peroxidase has an accessible active site , and many compounds can reach the site of the reaction. For an enzyme such as cytochrome c peroxidase , the compounds that donate electrons are very specific, because there is a very closed active site. While the exact mechanisms have yet to be elucidated, peroxidases are known to play a part in increasing a plant s defenses against pathogens. ref Cite journal author Karthikeyan M et al. title Induction of resistance in host against the infection of leaf blight pathogen Alternaria palandui in onion Allium cepa var aggregatum . journal Indian J Biochem Biophys volume 42 issue 6 pages 371 7 year 2005 month December pmid 16955738 format ref Peroxidases are sometimes used as histology histological marker. Cytochrome c peroxidase is used as a soluble, easily purified model for cytochrome c oxidase . The glutathione peroxidase family consists of 8 known human isoforms. Glutathione peroxidases use glutathione as an electron donor and are active with both hydrogen peroxide and organic hydroperoxide substrates. GPX1 Gpx1 , GPX2 gene Gpx2 , Gpx3, and GPX4 Gpx4 have been shown to be selenium containing enzymes, whereas Gpx6 is a selenoprotein in hu ... more details
now also recommends standard abbreviations for the following two amino acids gallery image L selenocysteine 2D skeletal.png Selenocysteine small L small Selenocysteine br Sec U image Pyrrolysine.svg ... 5.60 2.09 9.10 Selenocysteine U Sec 168.053 Valine V Val 117.14784 6.00 2.39 9.74 Tryptophan W Trp ... X weak acidic X 93 Selenocysteine U Sec CH sub 2 sub Selenol SeH X 5.73 X Valine V Val CH CH sub ... Serine S Ser UCU, UCC, UCA, UCG, AGU, AGC 6.8 Threonine T Thr ACU, ACC, ACA, ACG 5.9 Yes Selenocysteine ... is present. br span id selenonote span UGA is normally the opal or umber stop codon, but encodes selenocysteine ... sub 7 sub NO sub 2 sub 101.04768 101.1051 Selenocysteine U Sec C sub 3 sub H sub 5 sub NOSe 150.95364 .... Selenocysteine U Sec Selenium Selenated form of cysteine, which replaces sulfur . Valine V ... more details
year 2008 pmid 18369140 doi 10.1126 science.1152621 ref SECIS element Selenocysteine insertion sequence ... in the selenocysteine insertion element of eukaryotic selenoprotein mRNAs journal RNA volume 2 ... more details
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