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FAD binding protein

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https://www.readbyqxmd.com/read/28911204/enhanced-vulnerability-of-human-proteins-towards-disease-associated-inactivation-through-divergent-evolution
#1
Encarnación Medina-Carmona, Julian E Fuchs, Jose A Gavira, Noel Mesa-Torres, Jose L Neira, Eduardo Salido, Rogelio Palomino-Morales, Miguel Burgos, David J Timson, Angel L Pey
Human proteins are vulnerable towards disease-associated single amino acid replacements affecting protein stability and function. Interestingly, a few studies have shown that consensus amino acids from mammals or vertebrates can enhance protein stability when incorporated into human proteins. Here, we investigate yet unexplored relationships between the high vulnerability of human proteins towards disease-associated inactivation and recent evolutionary site-specific divergence of stabilizing amino acids. Using phylogenetic, structural and experimental analyses, we show that divergence from the consensus amino acids at several sites during mammalian evolution has caused local protein destabilization in two human proteins linked to disease: cancer-associated NQO1 and alanine:glyoxylate aminotransferase, mutated in primary hyperoxaluria type I...
September 15, 2017: Human Molecular Genetics
https://www.readbyqxmd.com/read/28890319/arctic-a%C3%AE-40-blocks-the-nicotine-induced-neuroprotective-effect-of-chrna7-by-inhibiting-the-erk1-2-pathway-in-human-neuroblastoma-cells
#2
Ye Ju, Toru Asahi, Naoya Sawamura
Amyloid β protein (Aβ) plays a central role in Alzheimer's disease (AD) pathogenesis. Point mutations in the Aβ sequence, which cluster around the central hydrophobic core of the peptide, are associated with familial AD (FAD). Several mutations have been identified, with the Arctic mutation exhibiting a purely cognitive phenotype that is typical of AD. Our previous findings suggest that Arctic Aβ40 binds to and aggregates with CHRNA7, thereby inhibiting the calcium response and signaling pathways downstream of the receptor...
September 8, 2017: Neurochemistry International
https://www.readbyqxmd.com/read/28889232/modulation-of-the-flavin-protein-interactions-in-nadh-peroxidase-and-mercuric-ion-reductase-a-resonance-raman-study
#3
Julie Keirsse-Haquin, Thierry Picaud, Luc Bordes, Adrienne Gomez de Gracia, Alain Desbois
NADH peroxidase (Npx) and mercuric ion reductase (MerA) are flavoproteins belonging to the pyridine nucleotide:disulfide oxidoreductases (PNDO) and catalyzing the reduction of toxic substrates, i.e., hydrogen peroxide and mercuric ion, respectively. To determine the role of the flavin adenine dinucleotide (FAD) in the detoxification mechanism, the resonance Raman (RR) spectra of these enzymes under various redox and ligation states have been investigated using blue and/or near-UV excitation(s). These data were compared to those previously obtained for glutathione reductase (GR), another enzyme of the PNDO family, but catalyzing the reduction of oxidized glutathione...
September 9, 2017: European Biophysics Journal: EBJ
https://www.readbyqxmd.com/read/28888693/n-terminus-determines-activity-and-specificity-of-styrene-monooxygenase-reductases
#4
Thomas Heine, Anika Scholtissek, Adrie H Westphal, Willem J H van Berkel, Dirk Tischler
Styrene monooxygenases (SMOs) are two-enzyme systems that catalyze the enantioselective epoxidation of styrene to (S)-styrene oxide. The FADH2 co-substrate of the epoxidase component (StyA) is supplied by an NADH-dependent flavin reductase (StyB). The genome of Rhodococcus opacus 1CP encodes two SMO systems. One system, which we define as E1-type, displays homology to the SMO from Pseudomonas taiwanensis VLB120. The other system, originally reported as a fused system (RoStyA2B), is defined as E2-type. Here we found that E1-type RoStyB is inhibited by FMN, while RoStyA2B is known to be active with FMN...
September 6, 2017: Biochimica et Biophysica Acta
https://www.readbyqxmd.com/read/28887045/the-molten-globule-residual-structure-is-critical-for-reflavination-of-glucose-oxidase
#5
Katarína Garajová, Martina Zimmermann, Martina Petrenčáková, Lenka Dzurová, Michal Nemergut, Ľudovít Škultéty, Gabriel Žoldák, Erik Sedlák
Glucose oxidase (GOX) is a homodimeric glycoprotein with tightly bound one molecule of FAD cofactor per monomer of the protein. GOX has numerous applications, but the preparation of biotechnologically interesting GOX sensors requires a removal of the native FAD cofactor. This process often leads to unwanted irreversible deflavination and, as a consequence, to the low enzyme recovery. Molecular mechanisms of reversible reflavination are poorly understood; our current knowledge is based only on empiric rules, which is clearly insufficient for further development...
September 1, 2017: Biophysical Chemistry
https://www.readbyqxmd.com/read/28876066/photoactivation-of-the-bluf-protein-pixd-probed-by-the-site-specific-incorporation-of-fluorotyrosine-residues
#6
Agnieszka A Gil, Sergey P Laptenok, James N Iuliano, Andras Lukacs, Anil Verma, Christopher R Hall, EunBin Yoon, Richard Brust, Gregory M Greetham, Michael Towrie, Jarrod B French, Stephen R Meech, Peter J Tonge
The flavin chromophore in blue light using FAD (BLUF) photoreceptors is surrounded by a hydrogen bond network that senses and responds to changes in the electronic structure of the flavin on the ultrafast time scale. The hydrogen bond network includes a strictly conserved Tyr residue, and previously we explored the role of this residue, Y21, in the photoactivation mechanism of the BLUF protein AppA by the introduction of fluorotyrosine (F-Tyr) analogs that modulated the pKa and reduction potential of Y21 by 3...
September 6, 2017: Journal of the American Chemical Society
https://www.readbyqxmd.com/read/28860382/an-algal-photoenzyme-converts-fatty-acids-to-hydrocarbons
#7
Damien Sorigué, Bertrand Légeret, Stéphan Cuiné, Stéphanie Blangy, Solène Moulin, Emmanuelle Billon, Pierre Richaud, Sabine Brugière, Yohann Couté, Didier Nurizzo, Pavel Müller, Klaus Brettel, David Pignol, Pascal Arnoux, Yonghua Li-Beisson, Gilles Peltier, Fred Beisson
Although many organisms capture or respond to sunlight, few enzymes are known to be driven by light. Among these are DNA photolyases and the photosynthetic reaction centers. Here, we show that the microalga Chlorella variabilis NC64A harbors a photoenzyme that acts in lipid metabolism. This enzyme belongs to an algae-specific clade of the glucose-methanol-choline oxidoreductase family and catalyzes the decarboxylation of free fatty acids to n-alkanes or -alkenes in response to blue light. Crystal structure of the protein reveals a fatty acid-binding site in a hydrophobic tunnel leading to the light-capturing flavin adenine dinucleotide (FAD) cofactor...
September 1, 2017: Science
https://www.readbyqxmd.com/read/28842420/conditional-deletion-of-prnp-rescues-behavioral-and-synaptic-deficits-after-disease-onset-in-transgenic-alzheimer-s-disease
#8
Santiago V Salazar, Christopher Gallardo, Adam C Kaufman, Charlotte S Herber, Laura T Haas, Sophie Robinson, Jean C Manson, Michael K Lee, Stephen M Strittmatter
Biochemical and genetic evidence implicate soluble oligomeric amyloid-beta (Aβo) in triggering Alzheimer's disease (AD) pathophysiology. Moreover, constitutive deletion of the Aβo-binding cellular prion protein (PrP(C)) prevents development of memory deficits in APPswe/PS1ΔE9 mice, a model of familial AD. Here, we define the role of PrP(C) to rescue or halt established AD endophenotypes in a therapeutic disease-modifying time window after symptom onset. Deletion of Prnp at either 12 or 16 months of age fully reverses hippocampal synapse loss, and completely rescues pre-existing behavioral deficits by 17 months...
August 21, 2017: Journal of Neuroscience: the Official Journal of the Society for Neuroscience
https://www.readbyqxmd.com/read/28837770/background-nutrients-affect-the-biotransformation-of-tetracycline-by-stenotrophomonas-maltophilia-as-revealed-by-genomics-and-proteomics
#9
Yifei Leng, Jianguo Bao, Dandan Song, Jing Li, Mao Ye, Xu Li
Certain bacteria are resistant to antibiotics and can even transform antibiotics in the environment. It is unclear how the molecular mechanisms underlying the resistance and biotransformation processes vary under different environmental conditions. The objective of this study is to investigate the molecular mechanisms of tetracycline resistance and biotransformation by Stenotrophomonas maltophilia strain DT1 under various background nutrient conditions. Strain DT1 was exposed to tetracycline for 7 days with four background nutrient conditions: no background (NB), peptone (P), peptone plus citrate (PC), and peptone plus glucose (PG)...
September 11, 2017: Environmental Science & Technology
https://www.readbyqxmd.com/read/28833218/arabidopsis-fnrl-protein-is-an-nadph-dependent-chloroplast-oxidoreductase-resembling-bacterial-ferredoxin-nadp-reductases
#10
Minna M Koskela, Käthe M Dahlström, Guillermina Goñi, Nina Lehtimäki, Markus Nurmi, Adrian Velazquez-Campoy, Guy Hanke, Bettina Bölter, Tiina A Salminen, Milagros Medina, Paula Mulo
Plastidic ferredoxin-NADP(+) oxidoreductases (FNRs; EC:1.18.1.2) together with bacterial type FNRs (FPRs) form the plant-type FNR family. Members of this group contain a two-domain scaffold that forms the basis of an extended superfamily of FAD dependent oxidoreductases. In the present study, we show that the Arabidopsis thaliana At1g15140 (FERREDOXIN-NADP(+) OXIDOREDUCTASE -LIKE, FNRL) is an FAD-containing NADPH dependent oxidoreductase present in the chloroplast stroma. Determination of the kinetic parameters using the DCPIP NADPH-dependent diaphorase assay revealed that the reaction catalysed by a recombinant FNRL protein followed a saturation Michaelis-Menten profile on the NADPH concentration with kcat = 3...
August 18, 2017: Physiologia Plantarum
https://www.readbyqxmd.com/read/28821467/in-vitro-characterization-of-cyp102g4-from-streptomyces-cattleya-a-self-sufficient-p450-naturally-producing-indigo
#11
Joonwon Kim, Pyung-Gang Lee, Eun-Ok Jung, Byung-Gee Kim
Self-sufficient CYP102As possess outstanding hydroxylating activity to fatty acids such as myristic acid. Other CYP102 subfamily members share substrate specificity of CYP102As, but, occasionally, unusual characteristics of its own subfamily have been found. In this study, only one self-sufficient cytochrome P450 from Streptomyces cattleya was renamed from CYP102A_scat to CYP102G4, purified and characterized. UV-Vis spectrometry pattern, FAD/FMN analysis, and protein sequence comparison among CYP102s have shown that CYP102 from Streptomyces cattleya belongs to CYP102G subfamily...
August 15, 2017: Biochimica et Biophysica Acta
https://www.readbyqxmd.com/read/28818427/molecular-cloning-and-functional-characterization-of-nadph-dependent-cytochrome-p450-reductase-from-the-green-microalga-botryococcus-braunii-b-race
#12
Chung-Yau Tsou, Shigeki Matsunaga, Shigeru Okada
The green microalga Botryococcus braunii of the B race accumulates various lipophilic compounds containing a 10,11-oxidosqualene epoxide moiety in addition to large amounts of triterpene hydrocarbons. While 2,3-squalene epoxidases have already been isolated and characterized from the alga, the enzyme that catalyzes the 10,11-epoxidation of squalene has remained elusive. In order to obtain a molecular tool to explore a 10,11-squalene epoxidase, cDNA cloning of an NADPH-dependent cytochrome P450 reductase (CPR) that is required by both squalene epoxidases and cytochrome P450 enzymes was carried out...
August 14, 2017: Journal of Bioscience and Bioengineering
https://www.readbyqxmd.com/read/28808132/defining-electron-bifurcation-in-the-electron-transferring-flavoprotein-family
#13
Amaya M Garcia Costas, Saroj Poudel, Anne-Frances Miller, Gerrit J Schut, Rhesa N Ledbetter, Kathryn R Fixen, Lance C Seefeldt, Michael W W Adams, Caroline S Harwood, Eric S Boyd, John W Peters
Electron bifurcation is the coupling of exergonic and endergonic redox reactions to simultaneously generate (or utilize) low and high potential electrons. It is the third recognized form of energy conservation in biology and has recently been described in select electron transferring flavoproteins (Etfs). Etfs are flavin-containing heterodimers best known for donating electrons derived from fatty acid and amino acid oxidation to an electron transfer respiratory chain via ETF quinone oxidoreductase. Canonical examples contain a flavin adenine dinucleotide (FAD) that is involved in electron transfer as well as a non-redox active adenosine monophosphate (AMP)...
August 14, 2017: Journal of Bacteriology
https://www.readbyqxmd.com/read/28782614/how-a-multimeric-macromolecule-is-affected-by-divalent-salts-experimental-and-simulation-study
#14
Fatemeh Janati-Fard, Mohammad R Housaindokht, Hassan Monhemi, Ali Nakhaei Pour
Salts exist in any cell and living organism in contact with biological macromolecules. How these salts affect biomolecules such as enzyme is important from both basic sciences and practical technologies. It was observed that divalent salts can change structure and function of protein at higher concentrations. Here, we investigated the effect of divalent salt on the behavior of a multimeric enzyme. We treated glucose oxidase as dimer-active enzyme in different CaCl2 concentration and seen that the enzyme become inactive at high concentration of salt...
August 4, 2017: International Journal of Biological Macromolecules
https://www.readbyqxmd.com/read/28782586/breaking-the-mirror-l-amino-acid-deaminase-a-novel-stereoselective-biocatalyst
#15
REVIEW
Gianluca Molla, Roberta Melis, Loredano Pollegioni
Enantiomerically pure amino acids are of increasing interest for the fine chemical, agrochemicals and pharmaceutical industries. During past years l-amino acids have been produced from deracemization of dl-solution employing the stereoselective flavoenzyme d-amino acid oxidase. On the other hand, the isolation of corresponding d-isomer was hampered by the scarce availability of a suitable l-amino acid oxidase activity. On this side, l-amino acid deaminase (LAAD), only present in the Proteus bacteria, represents a suitable alternative...
November 1, 2017: Biotechnology Advances
https://www.readbyqxmd.com/read/28754701/genome-sequence-and-composition-of-a-tolyporphin-producing-cyanobacterium-microbial-community
#16
Rebecca-Ayme Hughes, Yunlong Zhang, Ran Zhang, Philip G Williams, Jonathan S Lindsey, Eric S Miller
The cyanobacterial culture HT-58-2 was originally described as a strain of Tolypothrix nodosa with the ability to produce tolyporphins, which comprise a family of distinct tetrapyrrole macrocycles with reported efflux pump inhibition properties. Upon reviving the culture from what was thought to be a non-extant collection, studies of culture conditions, strain characterization, phylogeny, and genomics have been undertaken. Herein, HT-58-2 was shown by 16S rRNA analysis to closely align with Brasilonema strains and not with Tolypothrix isolates...
July 28, 2017: Applied and Environmental Microbiology
https://www.readbyqxmd.com/read/28739446/crystallographic-insights-into-a-cobalt-iii-sepulchrate-based-alternative-cofactor-system-of-p450-bm3-monooxygenase
#17
Saravanan Panneerselvam, Aamir Shehzad, Jochen Mueller-Dieckmann, Matthias Wilmanns, Marco Bocola, Mehdi D Davari, Ulrich Schwaneberg
P450 BM3 is a multi-domain heme-containing soluble bacterial monooxygenase. P450 BM3 and variants are known to oxidize structurally diverse substrates. Crystal structures of individual domains of P450 BM3 are available. However, the spatial organization of the full-length protein is unknown. In this study, crystal structures of the P450 BM3 M7 heme domain variant with and without cobalt (III) sepulchrate are reported. Cobalt (III) sepulchrate acts as an electron shuttle in an alternative cofactor system employing zinc dust as the electron source...
July 21, 2017: Biochimica et Biophysica Acta
https://www.readbyqxmd.com/read/28726126/characterization-of-a-cold-adapted-dna-photolyase-from-c-psychrerythraea-34h
#18
Sudipto Munshi, Ananthi Rajamoorthi, Robert J Stanley
The phrB gene encoding a putative cold-adapted DNA photolyase was cloned from the bacterial genomic DNA of Colwellia psychrerythraea 34H, a psychrophilic bacterium. Recombinant DNA photolyase, rCpPL, was overexpressed and purified from three different vectors. rCpPL binds its DNA substrate by flipping a cyclobutane pyrimidine dimer (CPD) into its active site and repairs CPD-containing DNA in vitro. rCpPL contains one catalytic flavin adenine dinucleotide (FAD) cofactor, but displays promiscuity in cofactor binding, in which either a flavin mononucleotide (FMN) or a methenyltetrahydrofolate (MTHF) molecule is bound as an antenna molecule and found in sub-stoichiometric amounts...
July 19, 2017: Extremophiles: Life Under Extreme Conditions
https://www.readbyqxmd.com/read/28712956/refolding-of-a-novel-cholesterol-oxidase-from-pimelobacter-simplex-reveals-dehydrogenation-activity
#19
Hui-Min Qin, Jian-Wen Wang, Qianqian Guo, Songtao Li, Panpan Xu, Zhangliang Zhu, Dengyue Sun, Fuping Lu
Cholesterol oxidases, which catalyze the degradation of cholesterol to cholest-4-en-3-one, are widely used in the pharmaceutical and food processing industries. The cholesterol oxidase from Pimelobacter simplex (PsChO3) was transformed into E. coli BL21(DE3), but it was expressed mainly as inclusion bodies, and any soluble PsChO3 failed to bind to Ni-NTA resin. To overcome this obstacle, we devised a simple yet efficient purification and refolding process using 8 M urea for the solubilization of PsChO3 and achieved a high yield of the enzyme in its active form...
November 2017: Protein Expression and Purification
https://www.readbyqxmd.com/read/28712849/structure-function-and-mechanism-of-proline-utilization-a-puta
#20
REVIEW
Li-Kai Liu, Donald F Becker, John J Tanner
Proline has important roles in multiple biological processes such as cellular bioenergetics, cell growth, oxidative and osmotic stress response, protein folding and stability, and redox signaling. The proline catabolic pathway, which forms glutamate, enables organisms to utilize proline as a carbon, nitrogen, and energy source. FAD-dependent proline dehydrogenase (PRODH) and NAD(+)-dependent glutamate semialdehyde dehydrogenase (GSALDH) convert proline to glutamate in two sequential oxidative steps. Depletion of PRODH and GSALDH in humans leads to hyperprolinemia, which is associated with mental disorders such as schizophrenia...
July 14, 2017: Archives of Biochemistry and Biophysics
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