Infobox protein family Symbol Flavoprotein Name Flavoprotein image PDB 1e20 EBI.jpg width caption the fmn binding protein athal3 Pfam PF02441 Pfam clan InterPro IPR003382 SMART PROSITE MEROPS SCOP 1e20 TCDB OPM family OPM protein CAZy CDD Flavoproteins are proteins that contain a nucleic acid derivative of riboflavin the flavin adenine dinucleotide FAD or flavin mononucleotide FMN . Flavoproteins are involved in a wide array of biological processes, including, but by no means limited to, bioluminescence , removal of Radical chemistry radicals contributing to oxidative stress, photosynthesis , DNA repair , and apoptosis . The spectroscopic properties of the Flavin group flavin cofactor make it a natural reporter for changes occurring within the active site this makes flavoproteins one of the most studied enzyme families. Discovery The first mention of a flavoprotein in the scientific literature dates back to 1879, when the work on the composition of cow s milk resulted in the isolation of a bright yellow pigment , that we now know as Flavin group flavin , but termed lactochrome at the time. By the early 1930s, this same pigment had been isolated from a range of sources, and recognised as a component of the vitamin B complex . Its structure was determined almost simultaneously by two groups in 1934, and given the name riboflavin , derived from the ribityl side chain and yellow colour of the conjugated ring system. ref name Massey Massey, V. 2000 The chemical and biological versatility ... The flavoprotein family contains a diverse range of enzymes, including Epidermin biosynthesis protein, EpiD, which has been shown to be a flavoprotein that Competitive inhibition bind s FMN. This enzyme ... of EpiD, a flavoprotein involved in the biosynthesis of the lantibiotic epidermin journal J ... External links eMedicineDictionary Flavoprotein The menu science of the program http 3d alignment.eu ... InterPro content IPR003382 Category Protein families Category Proteins ca Flavoprote na cs Flavoprotein ... more details
Infobox protein family Symbol ETF Name Electron transfer flavoprotein domain image PDB 1efp EBI.jpg width caption electron transfer flavoprotein etf from paracoccus denitrificans Pfam PF01012 Pfam clan CL0039 InterPro IPR014730 SMART PROSITE PDOC00583 MEROPS SCOP 1efv TCDB OPM family OPM protein CAZy CDD Infobox protein family Symbol ETF alpha Name Electron transfer flavoprotein FAD binding domain image PDB 1o96 EBI.jpg width caption structure of electron transferring flavoprotein for methylophilus methylotrophus. Pfam PF00766 Pfam clan CL0085 InterPro IPR014731 SMART PROSITE PDOC00583 MEROPS SCOP 1efv TCDB OPM family OPM protein CAZy CDD 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 ... of the ubiquitous electron transfer flavoprotein families ETF alpha and ETF beta journal ... structure of human electron transfer flavoprotein to 2.1 A resolution journal Proc. Natl. Acad ... family?acc PF01012 tabview tab0 Pfam entry for Electron transfer flavoprotein domain http pfam.sanger.ac.uk family?acc PF00766 tabview tab0 Pfam entry for Electron transfer flavoprotein ... more details
Protein Name Electron transferring flavoprotein dehydrogenase image 2GMH colored structure.gif caption Ribbon diagram of electron transferring flavoprotein dehydrogenase with each functional domain differentially colored. Blue band is membrane area. 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 doi 10.1046 j.1432 1033.2003.03946.x title Acyl CoA dehydrogenases. A mechanistic overview year 2004 last1 Ghisla first1 Sandro last2 Thorpe first2 Colin journal European Journal of Biochemistry volume 271 issue 3 pages 494 508 pmid 14728676 ref ref cite journal doi 10.1086 519219 title A New Genetic Disorder in Mitochondrial Fatty ... The electron transfer flavoprotein Ubiquinone oxidoreductases year 2010 last1 Watmough first1 Nicholas ... first2 DJ last3 Husain first3 M title Reactions of electron transfer flavoprotein and electron transfer flavoprotein ubiquinone oxidoreductase volume 241 issue 3 pages 883 92 pmc 1147643 journal The Biochemical ... transfer flavoprotein with electron transfer flavoprotein ubiquinone oxidoreductase year 1985 ... in electron transfer flavoprotein ubiquinone oxidoreductase fluorescence quenching by a brominated ... flavoprotein ubiquinone oxidoreductase and electron transfer to the mitochondrial ubiquinone pool year ... the transfer of electrons from electron transferring flavoprotein ETF to ubiquinone, reducing ... Transfer Flavoprotein or Electron Transfer Flavoprotein Ubiquinone Oxidoreductase in Glutaric Acidemia ... structure and mutations of the electron transfer flavoprotein ubiquinone oxidoreductase ETF QO gene ... more details
conserved flavoprotein reductase in bacteria and mammals journal Trends Biochem. Sci. volume 16 issue ... MJ title Characterization of the flavoprotein moieties of NADPH sulfite reductase from Salmonella ..., Correll CC, Ludwig ML title Structural prototypes for an extended family of flavoprotein reductases ... ref , and various other flavoprotein s. Human proteins containing this domain MTRR NDOR1 NOS1 ... 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
Infobox protein family Symbol FAD oxidase C Name FAD linked oxidases, C terminal domain image PDB 1wve EBI.jpg width caption p cresol methylhydroxylase alteration of the structure of the flavoprotein subunit upon its binding to the cytochrome subunit Pfam PF02913 Pfam clan CL0277 InterPro IPR004113 SMART PROSITE MEROPS SCOP 1ahu TCDB OPM family OPM protein CAZy CDD In molecular biology FAD oxidases are a family of FAD dependent oxidoreductases . They are flavoprotein s that contain a covalently bound FAD group which is attached to a histidine via an 8 alpha N3 histidyl riboflavin linkage. The region around the histidine that binds the FAD group is conserved sequence conserved in these enzyme s. ref name pmid9141139 Cite pmid 9141139 ref References reflist InterPro content IPR004113 Category Protein domains ... 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
Infobox protein family Symbol FCSD flav bind Name Flavocytochrome c sulfide dehydrogenase, flavin binding image PDB 1fcd EBI.jpg width caption the structure of flavocytochrome c sulfide dehydrogenase from a purple phototrophic bacterium chromatium vinosum at 2.5 angstroms resolution Pfam PF09242 Pfam clan InterPro IPR015323 SMART PROSITE MEROPS SCOP 1fcd TCDB OPM family OPM protein CAZy CDD In molecular biology, flavocytochrome c sulfide dehydrogenase is an enzyme found in sulfur oxidising bacteria such as the purple phototrophic bacterium bacteria Chromatium vinosum . ref name pmid7939681 cite journal author Chen ZW, Koh M, Van Driessche G, Van Beeumen JJ, Bartsch RG, Meyer TE, Cusanovich MA, Mathews FS title The structure of flavocytochrome c sulfide dehydrogenase from a purple phototrophic bacterium journal Science volume 266 issue 5184 pages 430 2 year 1994 month October pmid 7939681 doi 10.1126 science.7939681 url ref ref name pmid15544340 cite journal author Quentmeier A, Hellwig P, Bardischewsky F, Wichmann R, Friedrich CG title Sulfide dehydrogenase activity of the monomeric flavoprotein SoxF of Paracoccus pantotrophus journal Biochemistry volume 43 issue 46 pages 14696 703 year 2004 month November pmid 15544340 doi 10.1021 bi048568y url ref These enzymes are dimers of a flavoprotein and a dihaem cytochrome that carry out hydrogen sulfide dependent cytochrome C Redox reduction . The dihaem cytochrome protein folding fold s into two domains, each of which resembles mitochondrion mitochondrial cytochrome c, with the two haem groups bound to the interior of the subunit. The flavoprotein subunit has a glutathione reductase like fold consisting of a beta 3,4 alpha 3 core, and an alpha beta sandwich. The active site of the flavoprotein subunit contains a catalyst catalytically important disulfide bridge located above the pyrimidine portion of the Flavin group flavin ring. The flavoprotein contains a C terminal domain required for binding to flavin, and subsequent ... 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 Enriched text format Environmental Technologies Fund , a UK based venture and growth capital fund 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 Electrothermal feedback Elektrotehnicki fakultet disambig Category Initialisms cs ETF de ETF fr ETF ko ETF it ETF nl ETF ja 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
unreferenced date March 2012 A chromoprotein is a conjugated protein that contains a pigment ed prosthetic group or cofactor . A common example is hemoglobin , which contains a heme cofactor, which is the iron containing molecule that makes Hemoglobin Oxyhemoglobin oxygenated blood appear red. Other examples of chromoproteins are myoglobin , cytochrome s and flavoprotein s. In hemoglobin chromoprotein tetramer MW 4 x 16.125 64.500 Heme Fe four pyrrol rings. Category Carotenoids Category Hemoproteins Category Pigments Category Proteins protein stub ca Cromoprote na de Chromoproteine mk pl Chromoproteiny ru uk zh ... 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
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, to be specific 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
Orphan date January 2012 A styrene monooxygenase SMO EC 1.14.14.11 is an enzyme that catalyzes the chemical reaction styrene FADH sub 2 sub O sub 2 sub S 2 phenyloxirane FAD H sub 2 sub O as the first step of the aerobic styrene degradation pathway. ref name eins Mooney, A., P. G. Ward, and K. E. O Connor. 2006. Microbial degradation of styrene biochemistry, molecular genetics, and perspectives for biotechnological applications. Appl. Microbiol. Biotechnol. 72 1 10. PMID 16823552 ref The product 2 phenyloxirane is also known as styrene oxide and can be converted by a styrene oxide isomerase SOI to obtain phenylacetaldehyde, which can be transformed into the key intermediate phenylacetic acid by a phenylacetaldehyde dehydrogenase PAD . The enzyme belongs to the group of oxidoreductases according EC classification and is dependent on FAD as cofactor, thus it was classified as an external flavoprotein monooxygenase designated as type E . ref name zwei Montersino, S., D. Tischler, G. T. Gassner, and W. J. H. van Berkel. 2011. Catalytic and structural features of flavoprotein hydroxylases and epoxidases. Adv. Synth. Catal. 353 2301 2319. ref ref name drei van Berkel, W. J. H., N. M. Kamerbeek, and M. W. Fraaije. 2006. Flavoprotein monooxygenases, a diverse class of oxidative biocatalysts. J. Biotechnol. 124 670 689. PMID 16712999 ref It forms a two component system with a reductase StyB, StyA2B . The reductase utilizes solely NADH to reduce the FAD, which is then transferred to the styrene monooxygenase StyA, StyA1 . Two types of that enzyme are described so far StyA StyB designated E1 , first described from Pseudomonas species, and StyA1 StyA2B designated E2 , first described from Actinobacteria. The E1 type is more abundant in nature and comprises a single monooxygenase StyA supported by a single reductase StyB , whereas the E2 type has a major monooxygenase StyA1 which is supported by fusion protein of a monooxygenase and reductase StyA2B . The latter one is the sourc ... 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. Hemoglobin contains the prosthetic group containing iron, which is the heme . It is within the heme group that carries the oxygen molecule through the binding of the oxygen molecule to the iron ion Fe2 found in the heme 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 AH BH sub 2 sub O sub 2 sub AOH B H sub 2 sub O h2o as catalyst References reflist Category Oxidoreductases biochem stub pl Monooksygenaza zh ... more details
enzyme Name Methylenetetrahydrofolate reductase ferredoxin EC number 1.5.7.1 CAS number IUBMB EC number 1 5 7 1 GO code image width caption In enzymology , a methylenetetrahydrofolate reductase ferredoxin EC number 1.5.7.1 is an enzyme that catalysis catalyzes the chemical reaction 5 methyltetrahydrofolate 2 oxidized ferredoxin math rightleftharpoons math 5,10 methylenetetrahydrofolate 2 reduced ferredoxin 2 H sup sup Thus, the two substrate biochemistry substrates of this enzyme are 5 methyltetrahydrofolate and oxidized ferredoxin , whereas its 3 product chemistry products are 5,10 methylenetetrahydrofolate , reduced ferredoxin , and hydrogen ion H sup sup . This enzyme belongs to the family of oxidoreductase s, specifically those acting on the CH NH group of donors with an iron sulfur protein as acceptor. The systematic name of this enzyme class is 5 methyltetrahydrofolate ferredoxin oxidoreductase . This enzyme is also called 5,10 methylenetetrahydrofolate reductase . This enzyme participates in one carbon pool by folate . References reflist 1 cite journal author Clark JE, Ljungdahl LG date 1984 title Purification and properties of 5,10 methylenetetrahydrofolate reductase, an iron sulfur flavoprotein from Clostridium formicoaceticum journal J. Biol. Chem. volume 259 pages 10845&ndash 9 pmid 6381490 issue 17 1.5 enzyme stub Category EC 1.5.7 Category Enzymes of unknown structure it Metilenetetraidrofolato reduttasi ferredossina ja ... more details
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