Wiktionary Cofactor may refer to any of the following Cofactor linear algebra , the signed minor of a matrix Minor linear algebra , an alternative name for the determinant of a smaller matrix than that which it describes Cofactor biochemistry , a substance that needs to be present in addition to an enzyme for a certain reaction to be catalysed Shannon expansion or Shannon cofactor, a derived function of another function, a notion useful in computer science and mathematics disambig fr Cofacteur nl Cofactor pt Cofator sr Kofaktor ... more details
Orphan date August 2010 Infobox company name Cofactor Genomics type Private company Private foundation ... homepage www.cofactorgenomics.com footnotes intl yes Cofactor Genomics is a Missouri based firm ... Cofactor Genomics ref Overview Cofactor Genomics was founded in August 2008 ref http cofactorgenomics.com Cofactor Genomics ref after the pioneering efforts of the Human Genome Project made genetic ... an angel investor in California . ref http cofactorgenomics.com Cofactor Genomics ref ref St. Louis Business Journal St. Louis startup Cofactor to sequence Ozzy s genome http stlouis.bizjournals.com stlouis stories 2010 06 28 daily6.html ref Cofactor has since been featured in several nationwide ... stlouis related content.html?topic Cofactor 20Genomics 20LLC St. Louis Business Journal ref ref http www.genomeweb.com sequencing cofactor genomics installs solid 4 sequencing ozzy osbournes genome GenomeWeb Ozzy ref ref http www.genomeweb.com sequencing cofactor genomics novocraft technologies partner southeast asia GenomeWeb Cofactor Novocraft ref ref http www.avclub.com articles ..., Cofactor Genomics is able to construct and analyze fragment , paired end , chip sequencing , micro ... fragment Cofactor Genomics Applications ref Cofactor currently utilizes two Next Gen platforms ... platforms Cofactor Genomics Platforms ref Executive officers Jarret Glasscock, Ph.D. is a co founder as well as the Chief Executive Officer of Cofactor Genomics. ref http www.cofactorgenomics.com contact Cofactor Genomics Contact ref Dr. Glasscock completed his undergraduate degree at the University ... www.cofactorgenomics.com contact Cofactor Genomics Contact ref ref Warren Gish Warren Gish Bio ref ... Institute ref Jon Armstrong, M.S. is the Chief Marketing Officer of Cofactor Genomics. ref http www.cofactorgenomics.com contact Cofactor Genomics Contact ref After acquiring his Master ... s Technology Development Group. ref http www.cofactorgenomics.com contact Cofactor Genomics Contact ... more details
site in a tricyclic molybdenum cofactor . All molybdenum using enzymes so far identified in nature use this cofactor, save for the phylogenetically ancient molybdenum nitrogenase s, which fix nitrogen ... cycle s. ref cite journal title A structural comparison of molybdenum cofactor containing enzymes ... author3 Baas author4 R tey author5 Meckenstock author6 Kroneck ref See also Molybdenum cofactor deficiency ... more details
Cofactor engineering , a subset of metabolic engineering , is defined as the manipulation of the use of cofactor biochemistry cofactors in an organism s metabolic pathways . The field has applications ... Engineering Biotechnology year 2005 volume 100 issue 763 pages 1 17 ref Cofactor biochemistry ... Dequin title Cofactor engineering in Saccharomyces cerevisiae Expression of a H2O forming NADH oxidase ... 314 ref ref name Vadali cite journal last Vadali first Ravishankar coauthors George Bennett title Cofactor ... ref Image NAD phys.svg thumb right 200px Common cofactor NADH , the first discovered. An important group of organic cofactor biochemistry cofactors is the family of molecules referred to as vitamins ... for the concentrations of a single type of cofactor to affect the fluxes of many different pathways ... mineral that acts as a cofactor is iron, which is essential for the proper function of hemoglobin , the oxygen ... 420 http www.jstor.org stable 80032 JSTOR ref A few years after, Hans von Euler Chelpin identified the cofactor ... ATP and coenzyme A, were discovered later in the 1900s. The mechanism of cofactor biochemistry cofactor ... of cofactor concentrations could be used as tools for the improvement of metabolic pathways . ref name ABE Image Cofactor engineering map.gif right 600px Example of how Cofactor Engineering can be used to engineer one pathway to influence another. Significance The significance of cofactor ... of the enzymes involved in the pathway. Cofactor engineering, offers a distinct approach, and some advantages, to altering a metabolic pathway. In cofactor engineering, a metabolic pathway ... of how cofactor engineering can be used, but there are many other unique cases where scientists use cofactors as a way of altering metabolic pathways. A major advantage to cofactor engineering is that scientists ... in multiple pathways, cofactor engineering may be an efficient, cost effective alternative to current ... Sariyar, and Kimathi Blackwood title Metabolic Engineering through Cofactor Manipulation and Its ... more details
sulfur center s, and heme . A cofactor is a non protein chemical compound that is Binding molecular ... termed prosthetic groups . Some sources also limit the use of the term cofactor to inorganic substances ... the cofactor is called an apoenzyme , while the complete enzyme with cofactor is the holoenzyme . ref ... of a protein. On the other hand, prosthetic group emphasizes the nature of the binding of a cofactor ... tolerance , no human enzyme that uses this metal as a cofactor has been identified. ref cite journal ... s rather than as an enzyme cofactor. ref cite journal author Cavalieri RR title Iodine metabolism and thyroid ... molecule, and not usually considered a cofactor of the enzymes it regulates. ref cite journal author ... 15875011 doi 10.1038 435042a ref In many cases, the cofactor includes both an inorganic and organic ... reaction catalyzed by a different enzyme. In the latter case, the cofactor can also be considered ... 263 17 7913 ref Vitamins and derivatives class wikitable Cofactor Vitamin Additional component Chemical ... Cofactor Chemical group s transferred Distribution Adenosine triphosphate ref cite book author ... cofactor in plants journal J. Exp. Bot. volume 53 issue 375 pages 1689 98 year 2002 pmid ... called coenzymes . Each class of group transfer reaction is carried out by a particular cofactor ... as a cofactor. Here, hundreds of separate types of enzymes remove electrons from their substrates and redox reduce NAD sup sup to NADH. This reduced cofactor is then a substrate for any of the reductase ... to bind a different cofactor. ref name Denessiouk cite journal author Denessiouk KA, Rantanen ... . A computational method, IPRO, recently predicted mutations that experimentally switched the cofactor ... cofactor specificity journal Protein Science volume 18 issue 10 pages 2125 38 year 2009 month ... cofactor to be discovered was NAD sup sup , which was identified by Arthur Harden and William Youndin ... 7Ehlyoungs BL4010 cofactors.ppt Cofactors lecture Powerpoint file eMedicineDictionary Cofactor MeshName ... more details
PBB geneid 25920 Cofactor of BRCA1 , also known as COBRA1 , is a human gene ref name entrez cite web title Entrez Gene COBRA1 cofactor of BRCA1 url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 25920 accessdate ref that encodes NELF B. NELF B is a subunit of Negative elongation factor negative elongation factor NELF , which also includes NELF A WHSC2 MIM 606026 , either NELF C or NELF D TH1L MIM 605297 , and NELF E RDBP MIM 154040 . NELF acts with DRB sensitivity inducing factor DSIF , a heterodimer of SPT4 SUPT4H1 MIM 603555 and SPT5 SUPT5H MIM 602102 , to cause transcriptional pausing of RNA polymerase II see MIM 180660 . ref name Narita2003 cite journal author Narita, Takashi coauthors Yamaguchi, Yuki Yano, Keiichi Sugimoto, Seiji Chanarat, Sittinan Wada, Tadashi Kim, Dong ki Hasegawa, Jun Omori, Masashi Inukai, Naoto Endoh, Masaki Yamada, Tomoko Handa, Hiroshi title Human Transcription Elongation Factor NELF Identification of Novel Subunits and Reconstitution of the Functionally Active Complex journal Molecular and Cellular Biology volume 23 pages 1863 1873 year 2003 pmid 12612062 doi 10.1128 MCB.23.6.1863 1873.2003 issue 6 pmc 149481 ref COBRA1 was initially identified in a yeast two hybrid screen using the BRCT1 domain of BRCA1 as bait. ref name Ye2001 cite journal author Ye, Q. coauthors Hu, Y.F. Zhong, H. Nye, A.C. Belmont, A.S. Li, R. year 2001 title BRCA1 induced large scale chromatin unfolding and allele specific effects of cancer predisposing mutations journal The Journal of Cell Biology volume 155 issue 6 pages 911 922 doi 10.1083 jcb.200108049 pmid 11739404 pmc 2150890 ref User Skoch3 turned off automatic update to Summary by PBB ... text Interactions Cofactor of BRCA1 has been shown to Protein protein interaction interact with Estrogen ... al. title Cofactor of BRCA1 a novel transcription factor regulator in upper gastrointestinal adenocarcinomas ... no update protein box yes update summary no update citations yes es Cofactor de BRCA1 ... more details
Infobox Disease Name Molybdenum cofactor deficiency Image Caption DiseasesDB 29905 ICD10 ICD9 ICDO OMIM 252150 MedlinePlus eMedicineSubj ped eMedicineTopic 2172 MeshID Molybdenum cofactor deficiency is a human disease. Absence of molybdenum cofactor leads to accumulation of toxic levels of sulphite and neurological damage usually leading to death within months of birth, due to the lack of active sulfite oxidase . Furthermore a mutational block in molybdenum cofactor biosynthesis causes absence of enyzme activity of xanthine dehydrogenase oxidase and aldehyde oxidase . When caused by a mutation in the MOCS1 gene it is the type A variant. It can also be caused by a mutation in the MOCS2 gene, and in the GEPH gene. ref http www.ncbi.nlm.nih.gov pubmed 12754701 Mutations in the molybdenum cofactor biosynthetic genes MOCS1, MOCS2, and GEPH. ref It should not be confused with molybdenum deficiency . As of 2010, there had been approximately 132 reported cases. ref name pmid17065069 cite journal author Ichida K, Aydin HI, Hosoyamada M, et al. title A Turkish case with molybdenum cofactor deficiency journal Nucleosides Nucleotides Nucleic Acids volume 25 issue 9 11 pages 1087 91 year 2006 pmid 17065069 doi 10.1080 15257770600894022 url ref Diagnosis Early seizures, low blood levels of uric acid , and high levels of sulphite , xanthine and uric acid in urine . Characteristic MRI images of brain. ref http www.imoa.info HSE environmental data biology molybdenum cofactor.html ref Breakthrough In 2009, the first person to be cured of molybdenum cofactor deficiency type A, Baby Z has made world medical and legal history for Monash Children s at Southern Health in Melbourne, Australia. The patient was treated with cyclic pyranopterin monophosphate cPMP , a precursor of the molybdenum cofactor . ref name news.com.au cite news title Doctor cures Baby Z of molybdenum cofactor deficiency ... sulfite oxidase References reflist Category Vitamin, coenzyme, and cofactor metabolism disorders medicine ... more details
enzyme Name phosphoglucomutase glucose cofactor EC number 5.4.2.5 CAS number 37278 22 1 IUBMB EC number 5 4 2 5 GO code 0047468 image width caption In enzymology , a phosphoglucomutase glucose cofactor EC number 5.4.2.5 is an enzyme that catalysis catalyzes the chemical reaction alpha D glucose 1 phosphate math rightleftharpoons math D glucose 6 phosphate Hence, this enzyme has one substrate biochemistry substrate , alpha D glucose 1 phosphate , and one product chemistry product , D glucose 6 phosphate . This enzyme belongs to the family of isomerase s, specifically the phosphotransferases phosphomutases , which transfer phosphate groups within a molecule. The systematic name of this enzyme class is alpha D glucose 1,6 phosphomutase glucose cofactor . Other names in common use include glucose phosphomutase , and glucose 1 phosphate phosphotransferase . This enzyme has at least one effector biology effector , D Glucose . References reflist 1 cite journal author FUJIMOTO A, INGRAM P, SMITH RA date 1965 title D GLUCOSE I PHOSPHATE D GLUCOSE 6 PHOSPHOTRANSFERASE journal Biochim. Biophys. Acta. volume 96 pages 91&ndash 101 pmid 14285271 Boyer, P.D. Ed. , The Enzymes, 3rd ed., vol. 6, 1972, p. 407 477. isomerase stub Category EC 5.4.2 Category Enzymes of unknown structure ... more details
In linear algebra , the cofactor sometimes called adjunct , see A remark about different notations below describes a particular construction that is useful for calculating both the determinant and Invertible matrix inverse of square Matrix mathematics matrices . Specifically the cofactor of the i , j entry of a matrix, also known as the i , j cofactor of that matrix, is the Plus and minus signs sign ed Minor linear algebra minor of that entry. Informal approach to minors and cofactors Finding the minors of a matrix A is a multi step process Choose an entry math a ij math from the matrix. Cross out the entries that lie in the corresponding column math i math and row math j math . Rewrite the matrix without the marked entries. Obtain the determinant math M ij math of this new matrix. math M ij math is termed the minor for entry math a ij math . If i j is an Parity mathematics even number, the cofactor ... i j M ij , math and math C ij math called the cofactor of math a ij math , also referred to as the i , j , i , j or i , j sup th sup cofactor of A . Example Given the matrix math B begin bmatrix b 11 & b 12 & b 13 b 21 & b 22 & b 23 b 31 & b 32 & b 33 end bmatrix math suppose we wish to find the cofactor ... matrix Cofactor expansion main Laplace expansion Given the math n times n math matrix math A begin ... of the cofactors of any row or column of the matrix multiplied by the entries that generated them. Cofactor ... i 1 n a ij C ij math Cofactor expansion along the i th row math det A a i1 C i1 a i2 C i2 a i3 C i3 ... n math matrix A is the matrix whose i , j entry is the cofactor C sub ij sub of A . For instance ... & vdots a n1 & a n2 & cdots & a nn end bmatrix math the cofactor matrix of A is math C begin bmatrix ... n2 & cdots & C nn end bmatrix math where C sub ij sub is the cofactor of a sub ij sub . Adjugate Main ..., 1953, p.491, ref instead of cofactor the term adjunct is used. Moreover, it is denoted as A sub ij sub and defined in the same way as cofactor math mathbf A ij 1 i j mathbf M ij math Using this notation ... more details
PBB geneid 3053 Heparin cofactor II , a protein encoded by the SERPIND1 gene, is a coagulation factor that inhibits IIa, and is a cofactor for heparin and dermatan sulfate minor antithrombin . ref name entrez cite web title Entrez Gene SERPIND1 serpin peptidase inhibitor, clade D heparin cofactor , member 1 url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 3053 accessdate ref The PBB Summary template is automatically maintained by Protein Box Bot. See Template PBB ... with heparin cofactor II deficiency. ref name entrez Heparin Cofactor II deficiency can lead to increased ... cofactor II to alpha1 proteinase inhibitor M358R specifically increases the rate of thrombin ..., anticoagulant activity, and association with heparin cofactor II. journal Blood volume 107 issue 7 ... cite journal author Schillinger M, Exner M, Sabeti S, et al. title High plasma heparin cofactor ... of heparin cofactor II relevance of P17 glutamate residue in serpins, relationship with conformational ... HC, Gentry HR, et al. title Molecular mapping of the thrombin heparin cofactor II complex. journal ... between heparin and heparin cofactor II using surface plasmon resonance. journal Clin. Appl. Thromb ... Noda A, Wada H, Kusiya F, et al. title Plasma levels of heparin cofactor II HCII and thrombin HCII ... heparin cofactor II reveal a multistep allosteric mechanism. journal Proc. Natl. Acad. Sci. U.S.A. ... cite journal author Cunningham MA, Bhakta V, Sheffield WP title Altering heparin cofactor II at VAL439 ... Y, Kurimoto M, et al. title Contribution of basic residues of the A helix of heparin cofactor II ... JW, Church FC title Aspartic acid residues 72 and 75 and tyrosine sulfate 73 of heparin cofactor II ... of human heparin cofactor II from plasma and recombinant Chinese hamster ovary cells and their effects ...?id I04.019 I04.019 MeshName Heparin Cofactor II cite journal author He L, Vicente C, Westrick R, Eitzman D, Tollefsen D title Heparin cofactor II inhibits arterial thrombosis after endothelial injury ... 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 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 is the enzyme responsible for attaching biotin to a specific lysine at the biotin carboxyl carrier protein. Each organism likely has only one BPL protein. Biotin attachment is a two step reaction that results in the formation of an amide linkage between the carboxyl group of biotin and the epsilon amino group of the modified lysine. Biotin attachment is required for biotin biosynthesis and utilization of free biotin. ref name pmid10470036 cite journal author Chapman Smith ... MC, de Mendoza D, Cronan JE. title A novel amidotransferase required for lipoic acid cofactor assembly ... more details
PBB geneid 9351 Sodium hydrogen exchange regulatory cofactor NHE RF2 NHERF 2 also known as tyrosine kinase activator protein 1 TKA 1 or SRY interacting protein 1 SIP 1 is a protein that in humans is encoded by the SLC9A3R2 solute carrier family 9 isoform A3 regulatory factor 2 gene . ref name pmid9054412 cite journal author Poulat F, de Santa Barbara P, Desclozeaux M, Soullier S, Moniot B, Bonneaud N, Boizet B, Berta P title The human testis determining factor SRY binds a nuclear factor containing PDZ protein interaction domains journal J. Biol. Chem. volume 272 issue 11 pages 7167 72 year 1997 month March pmid 9054412 doi 10.1074 jbc.272.11.7167 ref ref name pmid9671706 cite journal author Hall RA, Ostedgaard LS, Premont RT, Blitzer JT, Rahman N, Welsh MJ, Lefkowitz RJ title A C terminal motif found in the beta2 adrenergic receptor, P2Y1 receptor and cystic fibrosis transmembrane conductance regulator determines binding to the Na H exchanger regulatory factor family of PDZ proteins journal Proc. Natl. Acad. Sci. U.S.A. volume 95 issue 15 pages 8496 501 year 1998 month July pmid 9671706 pmc 21104 doi 10.1073 pnas.95.15.8496 ref NHERF 2 is a scaffold protein that connects plasma membrane proteins with members of the Merlin protein ezrin moesin radixin family and thereby helps to link them to the actin cytoskeleton and to regulate their surface expression. It is necessary for cAMP mediated phosphorylation and inhibition of SLC9A3 . In addition, it may also act as scaffold protein in the Cell nucleus nucleus . Function This regulatory protein factor interacts with a sodium hydrogen exchanger NHE3 SLC9A3 in the brush border membrane of the proximal tubule , small intestine , and Colon anatomy colon that plays a major role in transepithelial sodium absorption. SLC9A3R2, as well as SLC9A3R1 and protein kinase A phosphorylation, may play a role in NHE3 regulation. ref cite web ... ref Interactions Sodium hydrogen exchange regulatory cofactor 2 has been shown to Protein protein interaction ... more details
methyl coenzyme M reductase MCR redirects here, but when the MCR article is written, we can change that chembox Watchedfields changed verifiedrevid 431328086 ImageFile Coenzyme F430.svg ImageSize IUPACName OtherNames Section1 Chembox Identifiers CASNo 73145 13 8 PubChem 5460020 SMILES Section2 Chembox Properties Formula chem C 42 H 51 N 6 NiO 13 MolarMass 906.58014 Appearance Density MeltingPt BoilingPt Solubility Section3 Chembox Hazards MainHazards FlashPt Autoignition F sub 430 sub is the prosthetic group of the enzyme methyl coenzyme M reductase . It is found only in methanogen ic Archaea . ref cite journal doi 10.1099 00221287 144 9 2377 author Thauer RK title Biochemistry of Methanogenesis a Tribute to Marjory Stephenson journal Microbiology year 1998 volume 144 issue 9 pages 2377 2406 pmid 9782487 url http mic.sgmjournals.org cgi pmidlookup?view long&pmid 9782487 ref This enzyme catalyzes the release of methane in the final step of methanogenesis chem link coenzyme M CH 3 S CoM coenzyme B HS CoB &rarr chem CH 4 CoB S S CoM Corphin in context Nature uses multiple tetrapyrrole s heme s, chlorophyll , and cobalamin . F sub 430 sub is the most reduced tetrapyrrole in nature with only five double bonds. This particular tetrapyrrole derivative is called a corphin. Because of its relative lack of conjugated unsaturation, it is yellow, not the intense purple red associated with more unsaturated tetrapyrroles. It is also the only tetrapyrrole derivative found in nature to contain nickel . Ni II is too small for the N4 binding site of the corphin, which causes the macrocycle to adopt a ruffled structure. Proposed mechanism of methanogenesis The active form of F sub 430 sub contains Ni I , analogously to the reduced B sub 12 sub cofactors that feature Co I . Whereas Co I is d sup 8 sup and diamagnetic , Ni I is d sup 9 sup and paramagnetic . The mechanism by which Nature cleaves the chem CH 3 S bond in methyl coenzyme M is presently 2006 unclear although it is known tha ... more details
File Moco riboswitch.svg left frame Consensus secondary structure of Moco RNAs. Layout is similar to a previously published figure. ref name Regulski2008 Infobox rfam Name Moco molybdenum cofactor riboswitch image MOCO RNA motif secondary structure.jpg width caption Predicted secondary structure and sequence conservation of MOCO RNA motif Symbol MOCO RNA motif AltSymbols Rfam RF01055 miRBase miRBase family RNA type Cis regulatory element Cis reg riboswitch Tax domain Bacteria GO SO SO 0005836 CAS number EntrezGene HGNCid OMIM PDB RefSeq Chromosome Arm Band LocusSupplementaryData The Moco RNA motif is a conserved RNA structure ref cite journal author Weinberg Z, Barrick JE, Yao Z, et al. title Identification of 22 candidate structured RNAs in bacteria using the CMfinder comparative genomics pipeline journal Nucleic Acids Res. volume 35 issue 14 pages 4809 19 year 2007 pmid 17621584 doi 10.1093 nar gkm487 pmc 1950547 ref that is presumed to be a riboswitch that binds molybdenum cofactor or the related tungsten cofactor . Genetic experiments support the hypothesis that the Moco RNA motif corresponds to a genetic control element that responds to changing concentrations of molybdenum or tungsten cofactor ref name Regulski2008 cite journal author Regulski EE, Moy RH, Weinberg Z, et al. title A widespread riboswitch candidate that controls bacterial genes involved in molybdenum cofactor and tungsten cofactor metabolism journal Mol. Microbiol. volume 68 issue 4 pages 918 year 2008 pmid 18363797 doi 10.1111 j.1365 2958.2008.06208.x pmc 2408646 ref . As these cofactors are not available in purified form, in vitro binding assays cannot be performed. However, the genetic data, complex structure of the RNA and the failure to detect a protein involved in the regulation suggest that the Moco RNA motif corresponds to a class of riboswitches. References references External links Rfam id RF01055 name Moco RNA motif DEFAULTSORT Moco Rna Motif Category Cis regulatory RNA elements Categ ... more details
Cleanup date October 2007 Image Rossmann fold 1g5q.png thumb 300px An example of the Rossmann fold, a structural domain of a decarboxylase protein from the bacterium Staphylococcus epidermidis PDB ID 1G5Q with the bound flavin mononucleotide cofactor shown. The Rossmann fold is a protein structural motif found in proteins that bind nucleotide s, especially the cofactor biochemistry cofactor Nicotinamide adenine dinucleotide NAD . The structure with two repeats is composed of six parallel beta sheet beta strands linked to two pairs of alpha helix alpha helices in the topological order beta alpha beta alpha beta. Because each Rossmann fold can bind one nucleotide, binding domains for dinucleotides such as NAD consist of two paired Rossmann folds that each bind one nucleotide moiety of the cofactor molecule. Single Rossmann folds can bind mononucleotides such as the cofactor flavin mononucleotide FMN . The motif is named for Michael Rossmann , who first pointed out that this is a frequently occurring motif in nucleotide binding proteins, such as dehydrogenases. ref cite journal author Rao S, Rossmann M title Comparison of super secondary structures in proteins journal J Mol Biol volume 76 issue 2 pages 241 56 year 1973 pmid 4737475 doi 10.1016 0022 2836 73 90388 4 ref References references Protein tertiary structure DEFAULTSORT Rossmann Fold Category Protein folds Category Protein structural motifs protein stub de Rossmann Faltung es Plegamiento de Rossmann ... more details
Amine Dehydrogenase EC number 1.4.99.3 , also known as methylamine dehydrogenase MADH , is a tryptophan tryptophylquinone dependent TTQ dependent enzyme that catalysis catalyzes the oxidative deamination of a primary amine to an aldehyde and ammonia . The reaction occurs as follows RCH sub 2 sub NH sub 2 sub H sub 2 sub O Electron acceptor acceptor RCHO ammonia NH sub 3 sub redox reduced acceptor Amine dehydrogenase possesses an sub 2 sub sub 2 sub structure with each smaller subunit possessing a TTQ protein Cofactor biochemistry cofactor . Amine dehydrogenase, studied in Paracoccus denitrificans , at least transiently forms a ternary complex to catalyze methylamine dependent cytochrome c 551i reduction. Within this complex, electrons are transferred from the TTQ cofactor of MADH to the Type 1 copper center of amicyanin, and then to the heme of the cytochrome . References cite journal author Davidson VL title Electron transfer in quinoproteins journal Arch. Biochem. Biophys. volume 428 issue 1 pages 32 40 year 2004 pmid 15234267 doi 10.1016 j.abb.2004.03.022 External links MeshName methylamine dehydrogenase CH NH2 oxidoreductases Category Enzymes organic compound stub enzyme stub it Ammina deidrogenasi ja ... more details
Metmyoglobin is the oxidised form of the oxygen carrying protein myoglobin . Metmyoglobin is the cause of the characteristic brown colouration of meat that occurs as it ages. In living muscle , the concentration of metmyoglobin is vanishingly small, due to the presence of the enzyme metmyoglobin reductase , which, in the presence of the Cofactor biochemistry cofactor NADH and the coenzyme cytochrome b4 converts the Iron Fe sup 3 sup in the heme heme prosthetic group of metmyoglobin back to the Fe sup 2 sup of normal myoglobin. In meat, which is dead muscle , the normal processes of removing metmyoglobin are prevented from effecting this repair, or alternatively the rate of metmyoglobin formation exceeds their capacity, so that there is a net accumulation of metmyoglobin as the meat ages. External links MeshName Metmyoglobin Globins Category Hemoproteins protein stub de Metmyoglobin ja ... more details
Unreferenced date December 2009 Serotonergic or serotoninergic means related to the neurotransmitter serotonin . A synapse is serotonergic if it uses serotonin as its neurotransmitter. A substance is serotonergic if it produces its effects via interactions with the serotonin system. A serotonergic , or serotonergic agent , is any chemical which functions to enhance the effects mediated by serotonin in the central nervous system , and they include the following classes of chemicals Serotonin precursors such as tryptophan and 5 Hydroxytryptophan 5 HTP Cofactor biochemistry Cofactor s required in the body s production of serotonin Serotonergic enzyme s Selective serotonin reuptake inhibitor A common class of serotonergic antidepressants Noradrenergic and specific serotonergic antidepressant Another class of serotonergic antidepressants Serotonergic psychedelic s The serotonergic psychedelic drug s See also Serotonin agonist Serotonin antagonist Cholinergic Dopaminergic Nootropic Serotonergics Category Parasympathetic nervous system Category Neurochemistry Category Neurotransmitters Category Serotonin no Serotonerg sr Serotonergik ... more details
enzyme Name methionine racemase EC number 5.1.1.2 CAS number 9024 07 1 IUBMB EC number 5 1 1 2 GO code 0018111 image width caption In enzymology , a methionine racemase EC number 5.1.1.2 is an enzyme that catalysis catalyzes the chemical reaction L methionine math rightleftharpoons math D methionine Hence, this enzyme has one substrate biochemistry substrate , L methionine , and one product chemistry product , D methionine . This enzyme belongs to the family of isomerase s, specifically those racemase s and epimerase s acting on amino acid s and derivatives. The systematic name of this enzyme class is methionine racemase . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . References reflist 1 McElroy, W.D. and Glass, H.B. Eds. , A Symposium on Amino Acid Metabolism, A Symposium on Amino Acid Metabolism, Baltimore, 1955, p. 616 634. isomerase stub Category EC 5.1.1 Category Pyridoxal phosphate enzymes Category Enzymes of unknown structure ... more details
enzyme Name tetrahydroxypteridine cycloisomerase EC number 5.5.1.3 CAS number 37318 54 0 IUBMB EC number 5 5 1 3 GO code 0050329 image width caption In enzymology , a tetrahydroxypteridine cycloisomerase EC number 5.5.1.3 is an enzyme that catalysis catalyzes the chemical reaction tetrahydroxypteridine math rightleftharpoons math xanthine 8 carboxylate Hence, this enzyme has one substrate biochemistry substrate , tetrahydroxypteridine , and one product chemistry product , xanthine 8 carboxylate . This enzyme belongs to the family of isomerase s, specifically the class of intramolecular lyase s. The systematic name of this enzyme class is tetrahydroxypteridine lyase isomerizing . It employs one cofactor biochemistry cofactor , NAD . References reflist 1 cite journal author McNutt, WS and Damle SP date 1964 title Tetraoxypteridine isomerase journal J. Biol. Chem. volume 239 pages 4272&ndash 4279 pmid 14247682 isomerase stub Category EC 5.5.1 Category NADH dependent enzymes Category Enzymes of unknown structure ... more details
Moco could refer to Language Moco n Slang. The moment when everything becomes clear. The point in time when realisation dawns and previous confusion is replaced with clarity. Derived from the words Mo ment of Co nsciousness . Like a Eureka moment Biology The Rock Cavy rock cavy , a Brazil ian rodent. The enzyme Molybdenum cofactor Geography MoCo , a nickname for Montgomery County, Maryland Mount Moco , the tallest mountain in Angola. Business Mozilla Corporation disambig es Moco desambiguaci n ... more details
Description Ferredoxin NADP Reductase structure from Maize root, atoms in the beta barrel are colored yellow, atoms in the alpha helix beta strand are colored green, and the cofactor FAD is colored red. image PDB Source Based on PDB file 3LVB from http www.pdb.org . Image made in Pymol. GFDL self migration not eligible Copy to Wikimedia Commons bot Fbot priority true ... more details
PBB geneid 4337 Molybdenum cofactor biosynthesis protein 1 is a protein that in humans is encoded by the MOCS1 gene . ref name pmid9731530 cite journal author Reiss J, Cohen N, Dorche C, Mandel H, Mendel RR, Stallmeyer B, Zabot MT, Dierks T title Mutations in a polycistronic nuclear gene associated with molybdenum cofactor deficiency journal Nat Genet volume 20 issue 1 pages 51 3 year 1998 month Oct pmid 9731530 pmc doi 10.1038 1706 ref ref name pmid10053004 cite journal author Reiss J, Dorche C, Stallmeyer B, Mendel RR, Cohen N, Zabot MT title Human molybdopterin synthase gene genomic structure and mutations in molybdenum cofactor deficiency type B journal Am J Hum Genet volume 64 issue 3 pages 706 11 year 1999 month Apr pmid 10053004 pmc 1377787 doi 10.1086 302296 ref ref name entrez cite web title Entrez Gene MOCS1 molybdenum cofactor synthesis 1 url http www.ncbi.nlm.nih.gov sites entrez ... in patients with molybdenum cofactor deficiency , type A. ref name entrez cite web title Entrez Gene MOCS1 molybdenum cofactor synthesis 1 url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch ... Molybdenum cofactor biosynthesis is a conserved pathway leading to the biological activation of molybdenum. The protein encoded by this gene is involved in molybdenum cofactor biosynthesis. This gene ... cofactor biosynthetic genes MOCS1, MOCS2, and GEPH. journal Hum. Mutat. volume 21 issue ... H, Reiss J, et al. title Localization of a gene for molybdenum cofactor deficiency, on the short ... and mutational spectrum of the bicistronic MOCS1 gene defective in molybdenum cofactor deficiency ... cite journal author Reiss J, Christensen E, Dorche C title Molybdenum cofactor deficiency ... Functionality of alternative splice forms of the first enzymes involved in human molybdenum cofactor ... Characterization of MOCS1A, an oxygen sensitive iron sulfur protein involved in human molybdenum cofactor ... cofactor deficiency. journal Nucleosides Nucleotides Nucleic Acids volume 25 issue 9 ... more details
PBB geneid 4338 Molybdenum cofactor synthesis protein 2A and molybdenum cofactor synthesis protein 2B are a pair of protein s that in humans are encoded from the same MOCS2 gene . ref name pmid10053004 cite journal author Reiss J, Dorche C, Stallmeyer B, Mendel RR, Cohen N, Zabot MT title Human molybdopterin synthase gene genomic structure and mutations in molybdenum cofactor deficiency type B journal American Journal of Human Genetics volume 64 issue 3 pages 706 11 year 1999 month March pmid 10053004 pmc 1377787 doi 10.1086 302296 ref ref name pmid9889283 cite journal author Sloan J, Kinghorn JR, Unkles SE title The two subunits of human molybdopterin synthase evidence for a bicistronic messenger RNA with overlapping reading frames journal Nucleic Acids Research volume 27 issue 3 pages 854 8 year 1999 month February pmid 9889283 pmc 148257 doi 10.1093 nar 27.3.854 ref ref name entrez EntrezGene 4338 MOCS2 molybdenum cofactor synthesis 2 ref These two proteins dimerize to form molybdopterin synthase . Function Eukaryotic molybdoenzyme s use a unique molybdenum cofactor MoCo consisting ... cofactor deficiency disease in babies. ref cite journal author Ichida K, Aydin HI, Hosoyamada M, et al. title A Turkish case with molybdenum cofactor deficiency journal Nucleosides, Nucleotides ... cofactor deficiency journal The Journal of Biological Chemistry volume 278 issue 28 pages ... Mutations in the molybdenum cofactor biosynthetic genes MOCS1, MOCS2, and GEPH journal Human Mutation .... title Mutations in a polycistronic nuclear gene associated with molybdenum cofactor deficiency journal ... mutations in a mild case of molybdenum cofactor deficiency journal American Journal of Medical ... for the physiological role of a rhodanese like protein for the biosynthesis of the molybdenum cofactor ... in the molybdenum cofactor genes MOCS1 and MOCS2 and in vitro characterization of a MOCS2 mutation ... O, Kumanda S title Molybdenum cofactor deficiency clinical features in a Turkish patient journal Brain ... more details
PBB geneid 55034 Molybdenum cofactor sulfurase is an enzyme that in humans is encoded by the MOCOS gene . ref name pmid11302742 cite journal author Ichida K, Matsumura T, Sakuma R, Hosoya T, Nishino T title Mutation of human molybdenum cofactor sulfurase gene is responsible for classical xanthinuria type II journal Biochem Biophys Res Commun volume 282 issue 5 pages 1194 200 year 2001 month Apr pmid 11302742 pmc doi 10.1006 bbrc.2001.4719 ref ref name entrez cite web title Entrez Gene MOCOS molybdenum cofactor sulfurase url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 55034 accessdate ref MOCOS sulfurates the molybdenum cofactor of xanthine dehydrogenase xanthine dehydrogenase XDH and aldehyde oxidase Aldehyde oxidase 1 AOX1 , which is required for their enzymatic activities. ref name pmid11302742 References reflist Further reading refbegin 2 PBB Further reading citations cite journal author Maruyama K, Sugano S title Oligo capping a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. journal Gene volume 138 issue 1 2 pages 171 4 year 1994 pmid 8125298 doi 10.1016 0378 1119 94 90802 8 cite journal author Suzuki Y, Yoshitomo Nakagawa K, Maruyama K, et al. title Construction and characterization of a full length enriched and a 5 end enriched cDNA library journal Gene volume 200 issue 1 2 pages 149 56 year 1997 pmid 9373149 doi 10.1016 S0378 1119 97 00411 3 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 Yamamoto T, Moriwaki Y, Takahashi S, et al. title Identification of a new point mutation in the human molybdenum cofactor sulferase ... Arg776Cys in the C terminal domain of the Human Molybdenum Cofactor Sulfurase HMCS associated with type ... more details
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