Cryptochrome References references External links eMedicineDictionary Flavoprotein The menu science .... Flavoproteins Category Proteins protein stub cs Flavoprotein de Flavoproteine es Flavoprote na it Flavoproteina ... more details
Protein Name Electron transferring flavoprotein dehydrogenase image caption Ribbon diagram of electron transferring flavoprotein dehydrogenase in complex with coenzyme Q10 ubiquinone bottom . Symbol ETFD AltSymbols ETF QO HGNCid 3483 Chromosome 4 Arm q Band LocusSupplementaryData 4q32.1 ECnumber 1.5.5.1 OMIM 231675 EntrezGene 2110 RefSeq NM 004453 UniProt Q16134 PDB 2GMH Electron transferring flavoprotein dehydrogenase ETF dehydrogenase or electron transfer flavoprotein ubiquinone oxidoreductase , EC 1.5.5.1 is an enzyme that transfers electrons from electron transferring flavoprotein in the mitochondrial matrix , to the coenzyme Q ubiquinone pool in the inner mitochondrial membrane . ref cite journal author Ramsay RR, Steenkamp DJ, Husain M title Reactions of electron transfer flavoprotein and electron transfer flavoprotein ubiquinone oxidoreductase journal Biochem. J. volume 241 issue 3 pages 883 92 year 1987 pmid 3593226 doi pmc 1147643 ref It is part of the electron transport chain . The enzyme is found in both prokaryotes and eukaryotes and contains a Flavin group flavin and iron sulfur protein FE S cluster . ref cite journal author Zhang J, Frerman FE, Kim JJ title Structure of electron transfer flavoprotein ubiquinone oxidoreductase and electron transfer to the mitochondrial ubiquinone pool journal Proc. Natl. Acad. Sci. U.S.A. volume 103 issue 44 pages 16212 7 year 2006 pmid 17050691 doi 10.1073 pnas.0604567103 pmc 1637562 ref Deficiency in EFT dehydrogenase causes the human genetic disease multiple acyl CoA dehydrogenase deficiency . ref cite journal author Vianey Liaud C, Divry P, Gregersen N, Mathieu M title The inborn errors of mitochondrial fatty acid oxidation journal J. Inherit. Metab. Dis. volume 10 Suppl 1 issue pages 159 200 year 1987 pmid 3119938 doi 10.1007 BF01812855 ref Reduced electron transferring flavoprotein ubiquinone electron transferring flavoprotein ubiquinol See also Oxidative phosphorylation Electron transport chain Microbial metabolism ... more details
An electron transfer flavoprotein ETF is a flavoprotein and functions as a specific electron acceptors for primary dehydrogenase s, transferring the electrons to terminal respiratory systems such as electron transferring flavoprotein dehydrogenase . They can be functionally classified into constitutive, housekeeping ETFs, mainly involved in the oxidation of fatty acids Group I , and ETFs produced by some prokaryotes under specific growth conditions, receiving electrons only from the oxidation of specific substrates Group II . ref name pmid8599534 cite journal author Weidenhaupt M, Rossi P, Beck C, Fischer HM, Hennecke H title Bradyrhizobium japonicum possesses two discrete sets of electron transfer flavoprotein genes fixA, fixB and etfS, etfL journal Arch. Microbiol. volume 165 issue 3 pages 169 78 year 1996 pmid 8599534 doi ref ETFs are heterodimeric proteins composed of an alpha and beta subunit, and contain an FAD cofactor and Adenosine monophosphate AMP . ref name pmid8525056 cite journal author Tsai MH, Saier MH title Phylogenetic characterization of the ubiquitous electron transfer flavoprotein families ETF alpha and ETF beta journal Res. Microbiol. volume 146 issue 5 pages 397 404 year 1995 pmid 8525056 doi ref ref name pmid8962055 cite journal author Roberts DL, Frerman FE, Kim JJ title Three dimensional structure of human electron transfer flavoprotein to 2.1 A resolution journal Proc. Natl. Acad. Sci. U.S.A. volume 93 issue 25 pages 14355 60 year 1996 pmid 8962055 doi 10.1073 pnas.93.25.14355 pmc 26136 ref ETF consists of three domains domains I and II are formed by the N and C terminal portions of the alpha subunit, respectively, while domain III is formed by the beta subunit. Domains I and III share an almost identical alpha beta alpha sandwich fold, while domain II forms an alpha beta alpha sandwich similar to that of bacterial flavodoxin s. FAD is bound in a cleft ... External links Pfam database Electron transferring flavoprotein. http pfam.sanger.ac.uk family?entry ... more details
TD title An unusual yet strongly conserved flavoprotein reductase in bacteria and mammals journal ... NM, Barber MJ title Characterization of the flavoprotein moieties of NADPH sulfite reductase from Salmonella ... ML title Structural prototypes for an extended family of flavoprotein reductases comparison of phthalate ... 2 issue 12 pages 2112 2133 year 1993 pmid 8298460 ref , and various other flavoprotein s. Human proteins ... more details
Flavus is the Latin word for yellow and has given the name to many, more or less yellow, objects Anatomy Ligamentum flavum Biochemistry Flavin group Flavin Flavonoid s Flavoprotein SpeciesAbbreviation flavus See also Flavius disambig Category Latin adjectives in current use bg ... more details
transferring flavoprotein journal J. Biol. Chem. volume 277 pages 8457&ndash 65 pmid 11756429 doi ... Scrutton NS, Sutcliffe MJ year 2000 title Trimethylamine dehydrogenase and electron transferring flavoprotein ... more details
enzyme Name dimethylamine dehydrogenase EC number 1.5.8.1 CAS number IUBMB EC number 1 5 8 1 GO code 0047133 image width caption In enzymology , a dimethylamine dehydrogenase EC number 1.5.8.1 is an enzyme that catalysis catalyzes the chemical reaction dimethylamine H sub 2 sub O electron transferring flavoprotein math rightleftharpoons math methylamine formaldehyde reduced electron transferring flavoprotein The 3 substrate biochemistry substrates of this enzyme are dimethylamine , water H sub 2 sub O , and electron transferring flavoprotein , whereas its 3 product chemistry products are methylamine , formaldehyde , and reduced electron transferring flavoprotein . This enzyme belongs to the family of oxidoreductase s, specifically those acting on the CH NH group of donors with a flavin as acceptor. The systematic name of this enzyme class is dimethylamine electron transferring flavoprotein oxidoreductase . This enzyme participates in methane metabolism . It employs one cofactor biochemistry cofactor , FMN . References reflist 1 cite journal author Yang CC, Packman LC, Scrutton NS date 1995 title The primary structure of Hyphomicrobium X dimethylamine dehydrogenase. Relationship to trimethylamine dehydrogenase and implications for substrate recognition journal Eur. J. Biochem. volume 232 pages 264&ndash 71 pmid 7556160 doi 10.1111 j.1432 1033.1995.tb20808.x issue 1 1.5 enzyme stub Category EC 1.5.8 Category Flavin enzymes Category Enzymes of unknown structure it Dimetilammina deidrogenasi ja ... more details
E. coli nitroreductase is a flavoprotein found in the bacteria Escherichia coli . It catalyses the reduction of Nitro compound nitro groups in a wide range of substrates, to produce the corresponding hydroxylamine . Although its role in vivo is unclear, it has been identified as useful in the metabolism of a number of prodrug s in anti cancer gene therapy . ref Denny, W.A. Nitroreductase based GDEPT Current Pharmaceutical Design , 2002, 8 15 , 1349 1361. ref See also Reduction of nitro compounds References references protein stub Category Bacterial enzymes ... more details
PBB geneid 2108 Electron transfer flavoprotein, alpha polypeptide glutaric aciduria II , also known as ETFA , is a protein which in humans is encoded by the ETFA gene . ref name entrez cite web title Entrez Gene ETFA electron transfer flavoprotein, alpha polypeptide glutaric aciduria II url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 2108 accessdate ref ETFA participates in catalyzing the initial step of the mitochondrion mitochondrial fatty acid beta oxidation . It shuttles electrons between primary electron transferring flavoprotein dehydrogenase flavoprotein dehydrogenases and the membrane bound electron transfer flavoprotein ubiquinone oxidoreductase. Defects in electron transfer flavoprotein have been implicated in glutaric acidemia type 2 type II glutaricaciduria in which multiple acyl CoA dehydrogenase deficiencies result in large excretion of glutaric, lactic, ethylmalonic, butyric, isobutyric, 2 methyl butyric, and isovaleric acids. ref name entrez cite web title Entrez Gene ETFA electron transfer flavoprotein, alpha polypeptide glutaric aciduria ... author Frerman FE title Acyl CoA dehydrogenases, electron transfer flavoprotein and electron transfer flavoprotein dehydrogenase. journal Biochem. Soc. Trans. volume 16 issue 3 pages 416 8 year 1988 ... in the alpha subunit of electron transfer flavoprotein in eight patients. journal J. Clin. Invest ... subunit of electron transfer flavoprotein in three patients with glutaric acidemia type II and identification ... flavoprotein. journal J. Biol. Chem. volume 263 issue 30 pages 15773 80 year 1988 pmid 3170610 doi ... of human electron transfer flavoprotein to 2.1 A resolution. journal Proc. Natl. Acad. Sci. U.S.A. volume ... transfer flavoprotein alpha chain alpha T171 displays decreased thermal stability and is overrepresented ... change in complexes of trimethylamine dehydrogenase and electron transferring flavoprotein ... pmc 1356129 cite journal author Schiff M, Froissart R, Olsen RK, et al. title Electron transfer flavoprotein ... more details
PBB geneid 2110 Electron transfer flavoprotein ubiquinone oxidoreductase, mitochondrial is an enzyme that in humans is encoded by the ETFDH gene . ref name entrez cite web title Entrez Gene ETFDH electron transferring flavoprotein dehydrogenase url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 2110 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 Electron transferring flavoprotein dehydrogenase in the inner mitochondrial membrane accepts electrons from electron transfer flavoprotein which is located in the mitochondrial matrix and reduces ubiquinone in the mitochondrial membrane. The protein is synthesized as a 67 kDa precursor which is targeted to mitochondria and processed in a single step to a 64 kDa mature form located in the mitochondrial membrane. Deficiency in electron transferring flavoprotein dehydrogenase have been demonstrated in some patients with type II glutaricacidemia. ref name entrez cite web title Entrez Gene ETFDH electron transferring flavoprotein dehydrogenase url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 2110 accessdate ref References reflist Further reading refbegin 2 PBB Further reading citations cite journal author Olsen RK, Olpin SE, Andresen BS, et al. title ETFDH mutations as a major cause of riboflavin responsive multiple acyl CoA dehydrogenation deficiency. journal Brain volume 130 issue Pt 8 pages 2045 54 year 2007 pmid 17584774 doi 10.1093 brain awm135 cite ... is caused by mutations in the electron transferring flavoprotein dehydrogenase ETFDH gene. journal ... structure and mutations of the electron transfer flavoprotein ubiquinone oxidoreductase ETF QO gene ... of human electron transfer flavoprotein ubiquinone oxidoreductase from a baculovirus vector kinetic ... electron transfer flavoprotein ubiquinone oxidoreductase journal Eur. J. Biochem. volume 219 issue ... more details
PBB geneid 2109 Electron transfer flavoprotein subunit beta is a protein that in humans is encoded by the ETFB gene . ref name entrez cite web title Entrez Gene ETFB electron transfer flavoprotein, beta polypeptide url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 2109 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 electron transfer flavoprotein, beta polypeptide, which shuttles electrons between primary flavoprotein dehydrogenases involved in mitochondrial fatty acid and amino acid catabolism and the membrane bound electron transfer flavoprotein ubiquinone oxidoreductase. The gene deficiencies have been implicated in type II glutaricaciduria. Alternatively spliced transcript variants have been found for this gene. ref name entrez cite web title Entrez Gene ETFB electron transfer flavoprotein, beta polypeptide url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 2109 accessdate ref References reflist Further reading refbegin 2 PBB Further reading citations cite journal author Royal V, Alberts MJ, Pericak Vance MA, et al. title RsaI RFLP for electron transport flavoprotein beta ETFB ... and polymorphisms of the gene encoding the beta subunit of the electron transfer flavoprotein in three ... N, et al. title Assignment of the gene encoding the beta subunit of the electron transfer flavoprotein ... flavoprotein. journal Eur. J. Biochem. volume 213 issue 3 pages 1003 8 year 1993 pmid 8504797 doi ... title Three dimensional structure of human electron transfer flavoprotein to 2.1 A resolution. journal ... variant in the human electron transfer flavoprotein alpha chain alpha T171 displays decreased ... transferring flavoprotein. journal J. Biol. Chem. volume 280 issue 34 pages 30361 6 year 2005 .... title Electron transfer flavoprotein deficiency functional and molecular aspects. journal Mol. Genet ... more details
ETF may refer to Exchange traded fund , an investment vehicle European Training Foundation , a vocational training organization International Transport Workers Federation European Transport Workers Federation Emergency Task Force TPS Emergency Task Force , a tactical unit of the Toronto Police ETF Enriched text format Escape the Fate , a post hardcore band Electron transferring flavoprotein , a metabolic macromolecule Early termination fee, a type of contractual termination fee Enemy Territory Fortress , a software modification of Wolfenstein Enemy Territory Modifications Wolfenstein Enemy Territory disambig cs ETF de ETF fr ETF ko ETF it ETF nl ETF pl ETF ... more details
protein Name acyl Coenzyme A dehydrogenase, C 2 to C 3 short chain caption image width HGNCid 90 Symbol ACADS AltSymbols EntrezGene 35 OMIM 606885 RefSeq NM 000017 UniProt P16219 PDB ECnumber 1.3.99.2 Chromosome 12 Arm q Band 24.31 LocusSupplementaryData Butyryl CoA dehydrogenase is a flavoprotein . It acts upon butyryl coenzyme A . See also Butyric acid Butyrate fermentation Causes of hypoglycemia Metabolic Defects External links MeshName Butyryl CoA Dehydrogenase oxidoreductase stub CH CH oxidoreductases Flavoproteins ... more details
enzyme Name methionine synthase reductase EC number 1.16.1.8 CAS number 207004 87 3 IUBMB EC number 1 16 1 8 GO code 0030586 image width caption In enzymology , a methionine synthase reductase EC number 1.16.1.8 is an enzyme that catalysis catalyzes the chemical reaction 2 methionine synthase methylcob I alamin 2 S adenosylhomocysteine NADP sup sup math rightleftharpoons math 2 methionine synthase cob I alamin NADPH H sup sup 2 S adenosyl L methionine The 3 substrate biochemistry substrates of this enzyme are methionine synthase methylcob I alamin , S adenosylhomocysteine , and nicotinamide adenine dinucleotide phosphate NADP sup sup , whereas its 4 product chemistry products are methionine synthase cob I alamin , nicotinamide adenine dinucleotide phosphate NADPH , hydrogen ion H sup sup , and S adenosyl L methionine . This enzyme belongs to the family of oxidoreductase s, specifically those oxidizing metal ion with NAD or NADP as acceptor. The systematic name of this enzyme class is methionine synthase methylcob I alamin,S adenosylhomocysteine NADP oxidoreductase . Other names in common use include methionine synthase cob II alamin reductase methylating , methionine synthase reductase , methionine synthase cobalamin methyltransferase cob II alamin , and reducing . It employs one cofactor biochemistry cofactor , flavoprotein . References reflist 1 cite journal author Rommens JM, Scherer SW, Rosenblatt DS, Gravel RA date 1998 title Cloning and mapping of a cDNA for methionine synthase reductase, a flavoprotein defective in patients with homocystinuria journal Proc. Natl. Acad. Sci. U. S. A. volume 95 pages 3059&ndash 64 pmid 9501215 doi 10.1073 pnas.95.6.3059 issue 6 pmc 19694 cite journal author Olteanu H, Banerjee R date 2001 title Human methionine synthase reductase, a soluble P 450 reductase like dual flavoprotein, is sufficient for NADPH dependent methionine synthase activation journal J. Biol. Chem. volume 276 pages 35558&ndash 63 pmid 11466310 doi 10.1074 jbc. ... more details
About molecular photoreceptors other types of photoreceptors Photoreceptor disambiguation Unreferenced date March 2007 Photoreceptors are light sensitive protein s involved in the sensing and response to light in a variety of organisms. Some examples are rhodopsin in the photoreceptor cell s of the vertebrate retina , phytochrome in plants, and bacteriorhodopsin and bacteriophytochromes in some bacterium bacteria . They mediate light responses as varied as visual perception , phototropism and phototaxis , as well as responses to light dark cycles such as circadian rhythm and other photoperiodism s including control of flowering times in plants and mating seasons in animals. Structure Photoreceptor proteins typically consist of a protein moiety and a non protein photopigment that reacts to light via photoisomerization or photoreduction , thus initiating a change of the receptor protein which triggers a signal transduction cascade. Pigments found in photoreceptors include retinal retinylidene protein s, for example rhodopsin in animals , Flavin group flavin flavoprotein s, for example cryptochrome in plants and animals and Bilin biochemistry bilin biliprotein s, for example phytochrome in plants . Photoreceptors in animals Also see Photoreceptor cell Melanopsin in vertebrate retina, mediates pupillary reflex, involved in regulation of circadian rhythms Photopsin in vertebrate retina, reception of various colors of light Rhodopsin in vertebrate retina, green blue light reception Photoreceptors in plants Cryptochrome in plants, blue light reception Phototropin in plants, mediates phototropism Phytochrome in plants, red and far red light reception Photoreceptors in phototactic flagellates Also see Eyespot apparatus Channelrhodopsin in unicellular algae, mediates phototaxis Chlamyopsin and volvoxopsin Flavoprotein s Photoreceptors in archaea and bacteria Bacteriophytochrome sensory Bacteriorhodopsin Halorhodopsin Proteorhodopsin Photoreception and signal transduction Phot ... more details
enzyme Name 5 pyridoxate dioxygenase EC number 1.14.12.5 CAS number 37256 70 5 IUBMB EC number 1 14 12 5 GO code 0047592 image width caption In enzymology , a 5 pyridoxate dioxygenase EC number 1.14.12.5 is an enzyme that catalysis catalyzes the chemical reaction 3 hydroxy 4 hydroxymethyl 2 methylpyridine 5 carboxylate NADPH H sup sup O sub 2 sub math rightleftharpoons math 2 acetamidomethylene 3 hydroxymethyl succinate NADP sup sup The 4 substrate biochemistry substrates of this enzyme are 3 hydroxy 4 hydroxymethyl 2 methylpyridine 5 carboxylate , nicotinamide adenine dinucleotide phosphate NADPH , hydrogen ion H sup sup , and oxygen O sub 2 sub , whereas its two product chemistry products are 2 acetamidomethylene 3 hydroxymethyl succinate and nicotinamide adenine dinucleotide phosphate NADP sup sup . This enzyme belongs to the family of oxidoreductase s, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of two atoms o oxygen into the other donor. The systematic name of this enzyme class is 5 pyridoxate,NADPH oxygen oxidoreductase decyclizing . This enzyme is also called 5 pyridoxate oxidase . This enzyme participates in vitamin B6 vitamin B sub 6 sub metabolism . It has 2 cofactor biochemistry cofactors FAD , and Flavoprotein . References reflist 1 cite journal author Sparrow LG, Ho PP, Sundaram TK, Zach D, Nyns EJ, Snell EE date 1969 title The bacterial oxidation of vitamin B6. VII. Purification, properties, and mechanism of action of an oxygenase which cleaves the 3 hydroxypyridine ring journal J. Biol. Chem. volume 244 pages 2590&ndash 600 pmid 4306031 issue 10 1.14 enzyme stub Category EC 1.14.12 Category NADPH dependent enzymes Category Flavin enzymes Category Flavoprotein enzymes Category Enzymes of unknown structure it 5 piridossato diossigenasi ja 5 ... more details
enzyme Name taxifolin 8 monooxygenase EC number 1.14.13.19 CAS number 39307 19 2 IUBMB EC number 1 14 13 19 GO code 0050326 image width caption In enzymology , a taxifolin 8 monooxygenase EC number 1.14.13.19 is an enzyme that catalysis catalyzes the chemical reaction taxifolin NAD P H H sup sup O sub 2 sub math rightleftharpoons math 2,3 dihydrogossypetin NAD P H sub 2 sub O The 5 substrate biochemistry substrates of this enzyme are taxifolin , nicotinamide adenine dinucleotide NADH , nicotinamide adenine dinucleotide phosphate NADPH , hydrogen ion H sup sup , and oxygen O sub 2 sub , whereas its 4 product chemistry products are 2,3 dihydrogossypetin , nicotinamide adenine dinucleotide NAD sup sup , nicotinamide adenine dinucleotide phosphate NADP sup sup , and water H sub 2 sub O . This enzyme belongs to the family of oxidoreductase s, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is taxifolin,NAD P H oxygen oxidoreductase 8 hydroxylating . This enzyme is also called taxifolin hydroxylase . It has 2 cofactor biochemistry cofactors FAD , and Flavoprotein . References reflist 1 cite journal author Jeffrey AM, Knight M, Evans WC date 1972 title The bacterial degradation of flavonoids. Hydroxylation of the A ring of taxifolin by a soil pseudomonad journal Biochem. J. volume 130 pages 373&ndash 81 pmid 4146277 issue 2 pmc 1174416 1.14.13 enzyme stub Category EC 1.14.13 Category NADPH dependent enzymes Category NADH dependent enzymes Category Flavin enzymes Category Flavoprotein enzymes Category Enzymes of unknown structure it Taxifolina 8 monoossigenasi ja 8 ... more details
enzyme Name dehydrogluconate dehydrogenase EC number 1.1.99.4 CAS number 9028 82 4 IUBMB EC number 1 1 99 4 GO code 0047843 image width caption In enzymology , a dehydrogluconate dehydrogenase EC number 1.1.99.4 is an enzyme that catalysis catalyzes the chemical reaction 2 dehydro D gluconate acceptor math rightleftharpoons math 2,5 didehydro D gluconate reduced acceptor Thus, the two substrate biochemistry substrates of this enzyme are 2 dehydro D gluconate and Electron acceptor acceptor , whereas its two product chemistry products are 2,5 didehydro D gluconate and reduced acceptor . This enzyme belongs to the family of oxidoreductase s, specifically those acting on the CH OH group of donor with other acceptors. The systematic name of this enzyme class is 2 dehydro D gluconate acceptor 2 oxidoreductase . Other names in common use include ketogluconate dehydrogenase , alpha ketogluconate dehydrogenase , 2 keto D gluconate dehydrogenase , and 2 oxogluconate dehydrogenase . It has 2 cofactor biochemistry cofactors FAD , and Flavoprotein . References reflist 1 cite journal author DATTA AG, KATZNELSON H date 1956 title The oxidation of 2 ketogluconate by a partially purified enzyme from Acetobactor melanogenum journal Arch. Biochem. Biophys. volume 65 pages 576&ndash 8 pmid 13395514 doi 10.1016 0003 9861 56 90218 1 issue 2 cite journal author Shinagawa E and Ameyama M date 1982 title 2 Keto D gluconate dehydrogenase from Gluconobacter melanogenus, membrane bound journal Methods Enzymol. volume 89 pages 194&ndash 198 doi 10.1016 S0076 6879 82 89034 4 1.1 enzyme stub Category EC 1.1.99 Category Flavin enzymes Category Flavoprotein enzymes Category Enzymes of unknown structure it Deidrogluconato deidrogenasi ja ... more details
enzyme Name NADPH dehydrogenase quinone EC number 1.6.99.6 CAS number 37256 37 4 IUBMB EC number 1 6 99 6 GO code 0008753 image width caption In enzymology , a NADPH dehydrogenase quinone EC number 1.6.99.6 is an enzyme that catalysis catalyzes the chemical reaction NADPH H sup sup acceptor math rightleftharpoons math NADP sup sup reduced acceptor The 3 substrate biochemistry substrates of this enzyme are nicotinamide adenine dinucleotide phosphate NADPH , hydrogen ion H sup sup , and Electron acceptor acceptor , whereas its two product chemistry products are nicotinamide adenine dinucleotide phosphate NADP sup sup and reduced acceptor . This enzyme belongs to the family of oxidoreductase s, specifically those acting on NADH or NADPH with other acceptors. The systematic name of this enzyme class is NADPH quinone acceptor oxidoreductase . Other names in common use include reduced nicotinamide adenine dinucleotide phosphate quinone , dehydrogenase , NADPH oxidase , and NADPH2 dehydrogenase quinone . It has 2 cofactor biochemistry cofactors FAD , and Flavoprotein . Several compounds are known to enzyme inhibitor inhibit this enzyme , including Folate , and Dicumarol . Structural studies As of late 2007, only one tertiary structure structure has been solved for this class of enzymes, with the Protein Data Bank PDB accession code PDB link 1F5V . References reflist 1 cite journal author Koli AK, Yearby C, Scott W, Donaldson KO date 1969 title Purification and properties of three separate menadione reductases from hog liver journal J. Biol. Chem. volume 244 pages 621&ndash 9 pmid 4388793 issue 4 1.6 enzyme stub Category EC 1.6.99 Category NADPH dependent enzymes Category Flavin enzymes Category Flavoprotein enzymes Category Enzymes of known structure it NADPH deidrogenasi chinone ja NADPH ... more details
SCMO may refer to SCMO company Supply Chain Management Outsource, a global consulting firm in logistics, transport, and supply chain management Subsidiary Communications Multiplex Operation , a subcarrier on a broadcasting station Scottish Catholic Media Office Southern California Marlin Online , a fishing magazine Soci t Canadienne de M t orologie et d Oc anographie Summary Court Martial Order , a military justice procedure Special Court Martial Order , a military justice procedure Summary Court Martial Officer Senior Clinical Medical Officer Senior Chief Medical Officer Superconducting Cavity Maser Oscillator , a liquid helium cooled oscillator Self Consistent Molecular Orbital method, a method that is used to calculate the energies of the ground Supplemental Case Management Order Sr2CoMoO6 , a magnetoelectric perovskite Single Common Market Organisation , a European Union organization Supply Chain MOnitoring , the monitoring of stocks throughout the entire chain Supply Chain Management Officer Select Committee Media Officer Surface Coal Mining Operation Steel Coal Mining Operations SCMO 1 , an Eastern Cape Provincial Supplier Database application form SterigmatoCystin biosynthesis MOnooxygenase from Aspergillus nidulans, a BVMO of the flavoprotein monooxygenase superfamily in biochemistry disambig ... more details
Unreferenced date April 2009 A conjugated protein is a protein that functions in interaction with other chemical groups attached by covalent bond s or by weak interactions. Many proteins contain only amino acid s and no other chemical groups, and they are called simple proteins. However, other kind of proteins yield, on hydrolysis, some other chemical component in addition to amino acids and they are called conjugated proteins. The nonamino part of a conjugated protein is usually called its prosthetic group . Most prosthetic groups are formed from vitamins. Conjugated proteins are classified on the basis of the chemical nature of their prosthetic groups. Some examples of conjugated proteins are lipoprotein s, glycoprotein s, phosphoprotein s, hemoprotein s, flavoprotein s, metalloprotein s, phytochrome s, cytochrome s and opsin s. Haemoglobin contains the prosthetic group containing iron, which is the haem. It is with in the haem group that carries the oxygen molecule through the binding of the oxygen molecule to the iron ion Fe2 found in the haem group. Glycoproteins are generally the largest and most abundant group of conjugated proteins. They range from glycoproteins in cell surface membranes that constitute the glycocalyx , to important antibodies produced by leukocytes . Category Proteins protein stub es Prote na conjugada fr H t roprot ine ja pt Prote na conjugada ru uk zh ... more details
Mixed function oxidase is the name of a family of oxidase enzymes that catalyze a reaction in which each of the two atoms of oxygen in O sub 2 sub is used for a different function in the reaction. ref MeshName Mixed Function Oxygenases ref Oxidase is a general name for enzymes that catalyze oxidations in which molecular oxygen is the electron acceptor but oxygen atoms do not appear in the oxidized product. Often, oxygen is reduced to either water cytochrome oxidase of the mitochondrial electron transfer chain or hydrogen peroxide dehydrogenation of fatty acyl CoA in peroxisome s . Most of the oxidases are flavoprotein s. The name mixed function oxidase indicates that the enzyme oxidizes two different substrate simultaneously. Desaturation of fatty acyl CoA in vertebrates is an example of the mixed function oxidase reaction. In the process, saturated fatty acyl CoA and NADPH are oxidized by molecular oxygen O sub 2 sub to produce monounsaturated fatty acyl CoA, NADP sup sup and 2 molecules of water. Reaction The mixed function oxidase reaction proceeds as follows 3 AH BH sub 2 sub O sub 2 sub AOH B H sub 2 sub O References reflist Category Oxidoreductases biochem stub pl Monooksygenaza zh ... more details
Infobox Disease Name Glutaric acidemia type 2 Image Glutaric acid.png Caption Glutaric acid DiseasesDB 29816 ICD10 ICD10 E 72 3 e 70 ICD9 ICD9 277.85 ICDO OMIM 231680 MedlinePlus eMedicineSubj eMedicineTopic MeshID D054069 Glutaric acidemia type 2 is an autosomal recessive metabolic disorder that is characterised by defects in the ability of the body to use protein s and fat s for energy. Incompletely processed proteins and fats can build up, leading to a dangerous chemical imbalance called acidosis . Diagnosis Glutaric acidemia type 2 often appears in infancy as a sudden metabolic crisis, in which acidosis and low blood sugar hypoglycemia cause weakness, behavior changes, and vomiting. There may also be enlargement of the liver , heart failure , and a characteristic odor resembling that of sweaty feet. Some infants with glutaric acidemia type 2 have birth defects, including multiple fluid filled growths in the kidneys polycystic kidneys . Glutaric acidemia type 2 is a very rare disorder. Its precise incidence is unknown. It has been reported in several different ethnic groups. Genetics Image autorecessive.svg thumb right Glutaric acidemia type 2 has an autosomal recessive pattern of inheritance. Mutations in the ETFA , ETFB , and ETFDH gene s cause glutaric acidemia type II. Glutaric acidemia type 2 is caused by a deficiency in either of two enzymes, called electron transfer flavoprotein and electron transfer flavoprotein dehydrogenase. These enzymes are normally active in the mitochondria , which are the energy producing centers of cells. When one of these enzymes is defective or missing, partially broken down nutrients accumulate in the cells and damage them, causing the signs and symptoms of glutaric acidemia type II. This condition is inherited in an autosomal recessive pattern, which means the defective gene is located on an autosome , and two copies of the gene one from each parent are needed to inherit the disorder. The parents of an individual with an autos ... more details
Encyclopedia
top
