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FAD binding protein

Fatemeh Janati-Fard, Mohammad Reza Housaindokht, Hassan Monhemi, Abbas Ali Esmaeili, Ali Nakhaei Pour
The search for ionic liquids (ILs) with biochemical and biomedical applications has recently gained great attention. IL containing solvents can change the structure, stability and function of proteins. The study of protein conformation in ILs is important to understand enzymatic activity. In this work, conformational stability and activity of the enzyme in two imidazolium-based ILs (1-butyl 3-methyl-imidozolium and 1-hexyl 3-methyl-imidozoliumbromides) were investigated. We treated glucose oxidase as dimer-active enzyme in different IL concentration and seen that GOx activity was inhibited in the presence of ILs...
March 17, 2018: International Journal of Biological Macromolecules
Filipa V Sena, Filipe M Sousa, A Sofia F Oliveira, Cláudio M Soares, Teresa Catarino, Manuela M Pereira
Type-II NADH:quinone oxidoreductases (NDH-2s) are membrane proteins involved in respiratory chains and the only enzymes with NADH:quinone oxidoreductase activity expressed in Staphylococcus aureus (S. aureus), one of the most common causes of clinical infections. NDH-2s are members of the two-Dinucleotide Binding Domains Flavoprotein (tDBDF) superfamily, having a flavin adenine dinucleotide, FAD, as prosthetic group and NAD(P)H as substrate. The establishment of a Charge-Transfer Complex (CTC) between the isoalloxazine ring of the reduced flavin and the nicotinamide ring of NAD+ in NDH-2 was described, and in this work we explored its role in the kinetic mechanism using different electron donors and electron acceptors...
February 17, 2018: Redox Biology
Samuel L Freeman, Anne Martel, Juliette Devos, Jaswir Basran, Emma L Raven, Gordon C K Roberts
Electron transfer in all living organisms critically relies on formation of complexes between the proteins involved. The function of these complexes requires specificity of the interaction to allow for selective electron transfer but also a fast turnover of the complex and they are therefore often transient in nature, making them challenging to study. Here, using small-angle neutron scattering with contrast matching with deuterated protein, we report the solution structure of the electron transfer complex between cytochrome P450 reductase (CPR) and its electron transfer partner cytochrome c...
February 23, 2018: Journal of Biological Chemistry
Manuel Benedetti, Ilaria Verrascina, Daniela Pontiggia, Federica Locci, Benedetta Mattei, Giulia De Lorenzo, Felice Cervone
Recognition of endogenous molecules acting as "damage-associated molecular patterns" (DAMPs) is a key feature of immunity in both animals and plants. Oligogalacturonides (OGs), i.e. fragments derived from the hydrolysis of homogalacturonan, a major component of pectin are a well-known class of DAMPs that activate immunity and protect plants against several microbes. However, hyper-accumulation of OGs severely affects growth, eventually leading to cell death and clearly pointing to OGs as players in the growth-defence trade-off...
February 3, 2018: Plant Journal: for Cell and Molecular Biology
Senwen Deng, Ping Li, Yiping Wang, Jia Zeng
Acyl-coA oxidase (ACO) is an important flavoenzyme responsible for the first step of peroxisomal fatty acid β-oxidation. In this study, the roles of Tyr232 and Tyr401 in flavin adenine dinucleotide (FAD) binding and enzyme catalysis of ACO were explored using site-directed mutagenesis. For mutant proteins, different levels of activity loss were observed. Wavelength scanning of Y232 and Y401 mutant proteins indicated that there is no FAD binding in Y401S and Y401G mutant ACO. Structure analysis indicated that the phenolic hydroxyl and benzene ring of the side chain could stabilize FAD binding through hydrogen bonds network and hydrophobic pocket formation...
January 25, 2018: Applied Biochemistry and Biotechnology
Yewei Dong, Jianhong Zhao, Junliang Chen, Shuqi Wang, Yang Liu, Qinghao Zhang, Cuihong You, Óscar Monroig, Douglas R Tocher, Yuanyou Li
The rabbitfish Siganus canaliculatus was the first marine teleost demonstrated to have the ability of biosynthesizing long-chain polyunsaturated fatty acids (LC-PUFA) from C18 PUFA precursors, and all genes encoding the key enzymes for LC-PUFA biosynthesis have been cloned and functionally characterized, which provides us a potential model to study the regulatory mechanisms of LC-PUFA biosynthesis in teleosts. As the primary step to clarify such mechanisms, present research focused on promoter analysis of gene encoding ∆6/∆5 fatty acyl desaturase (Fad), a rate-limiting enzyme catalyzing the first step in the conversion of C18 PUFA to LC-PUFA...
January 9, 2018: Gene
Giora I Morozov, Nurith Porat, Tatyana Kushnir, Hastyar Najmuldeen, Asad Adawi, Vered Chalifa-Caspi, Rachel Benisty, Ariel Ohayon, Ofir Liron, Shalhevet Azriel, Itai Malka, Shahar Dotan, Maxim Portnoi, Andrew A Piotrowski, Daniel Kafka, Barak Hajaj, Tali Fishilevich, Marilou Shagan, Michael Tal, Ron Ellis, Donald A Morrison, Andrea M Mitchell, Timothy J Mitchell, Ron Dagan, Hasan Yesilkaya, Yaffa Mizrachi Nebenzahl
Pneumococcal flavin reductase (FlaR) is known to be cell-wall associated and possess age dependent antigenicity in children. This study aimed at characterizing FlaR and elucidating its involvement in pneumococcal physiology and virulence. Bioinformatic analysis of FlaR sequence identified three-conserved cysteine residues, suggesting a transition metal-binding capacity. Recombinant FlaR (rFlaR) bound Fe2+ and exhibited FAD-dependent NADP-reductase activity, which increased in the presence of cysteine or excess Fe2+ and inhibited by divalent-chelating agents...
January 10, 2018: Scientific Reports
Piero Leone, Michele Galluccio, Alberto Barbiroli, Ivano Eberini, Maria Tolomeo, Flavia Vrenna, Elisabetta Gianazza, Stefania Iametti, Francesco Bonomi, Cesare Indiveri, Maria Barile
FAD synthase (FADS, EC is the last essential enzyme involved in the pathway of biosynthesis of Flavin cofactors starting from Riboflavin (Rf). Alternative splicing of the human FLAD1 gene generates different isoforms of the enzyme FAD synthase. Besides the well characterized isoform 1 and 2, other FADS isoforms with different catalytic domains have been detected, which are splice variants. We report the characterization of one of these novel isoforms, a 320 amino acid protein, consisting of the sole C-terminal 3'-phosphoadenosine 5'-phosphosulfate (PAPS) reductase domain (named FADS6)...
January 6, 2018: Molecules: a Journal of Synthetic Chemistry and Natural Product Chemistry
David Siegel, Donna D Dehn, Samantha S Bokatzian, Kevin Quinn, Donald S Backos, Andrea Di Francesco, Michel Bernier, Nichole Reisdorph, Rafael de Cabo, David Ross
NQO1 is a FAD containing NAD(P)H-dependent oxidoreductase that catalyzes the reduction of quinones and related substrates. In cells, NQO1 participates in a number of binding interactions with other proteins and mRNA and these interactions may be influenced by the concentrations of reduced pyridine nucleotides. NAD(P)H can protect NQO1 from proteolytic digestion suggesting that binding of reduced pyridine nucleotides results in a change in NQO1 structure. We have used purified NQO1 to demonstrate the addition of NAD(P)H induces a change in the structure of NQO1; this results in the loss of immunoreactivity to antibodies that bind to the C-terminal domain and to helix 7 of the catalytic core domain...
2018: PloS One
Almog Bregman-Cohen, Batel Deri, Shiran Maimon, Yael Pazy, Ayelet Fishman
2-Hydroxybiphenyl 3-monooxygenase (HbpA) is a flavin-containing NADH-dependent aromatic hydroxylase that oxidizes a broad range of 2-substituted phenols. In order to modulate its activity and selectivity, several residues in the active site pocket were investigated by saturation mutagenesis. Variant M321A demonstrated altered regioselectivity by oxidizing for the first time 3-hydroxybiphenyl, thus enabling the production of a new antioxidant, 3,4-dihydroxybiphenyl, with similar ferric reducing capacity as the well-studied piceatannol...
January 3, 2018: Chembiochem: a European Journal of Chemical Biology
María Alejandra Vorphal, Carola Bruna, Traudy Wandersleben, Jorge Dagnino-Leone, Francisco Lobos-González, Elena Uribe, José Martínez-Oyanedel, Marta Bunster
BACKGROUD: Ferredoxin NADP(H) oxidoreductases (EC (FNR) are flavoenzymes present in photosynthetic organisms; they are relevant for the production of reduced donors to redox reactions, i.e. in photosynthesis, the reduction of NADP+ to NADPH using the electrons provided by Ferredoxin (Fd), a small FeS soluble protein acceptor of electrons from PSI in chloroplasts. In rhodophyta no information about this system has been reported, this work is a contribution to the molecular and functional characterization of FNR from Gracilaria chilensis, also providing a structural analysis of the complex FNR/Fd...
December 8, 2017: Biological Research
Yan Wang, Wei Qi, Li Zhang, Zhenguang Ying, Ou Sha, Chunman Li, Lanhai Lü, Xiangyan Chen, Zhenzhong Li, Feng Niu, Fang Xue, Dong Wang, Tzi-Bun Ng, Lihong Zhang
Background: DL-3-n-butylphthalide (NBP) is a drug for treating acute ischemic stroke, and may play a neuroprotective role by acting on multiple active targets. The aim of this study was to predict the target proteins of NBP in mammalian cells. Methods: The similarity ensemble approach search tool (SEArch), one of the commonly used public bioinformatics tools for target prediction, was employed in the experiment. The molecular docking of NBP to target proteins was performed by using the three-dimensional (3-D) crystal structure, substrate free...
October 2017: Quantitative Imaging in Medicine and Surgery
Israel Hanukoglu
FAD and NAD(P) together represent an ideal pair for coupled redox reactions in their capacity to accept two electrons and their redox potentials. Enzymes that bind both NAD(P) and FAD represent large superfamilies that fulfill essential roles in numerous metabolic pathways. Adrenodoxin reductase (AdxR) shares Rossmann fold features with some of these superfamilies but remains in a group of its own in the absence of sequence homology. This article documents the phylogenetic distribution of AdxR by examining whole genome databases for Metazoa, Plantae, Fungi, and Protista, and determines the conserved structural features of AdxR...
December 2017: Journal of Molecular Evolution
Cheng Chen, Qiang Li, Qiangfeng Wang, Daihua Lu, Hong Zhang, Jian Wang, Rongtao Fu
Ganoderma is well known for its use in traditional Chinese medicine and is widely cultivated in China, Korea, and Japan. Increased temperatures associated with global warming are negatively influencing the growth and development of Ganoderma. Nitric oxide is reported to play an important role in alleviating fungal heat stress (HS). However, the transcriptional profiling of Ganoderma oregonense in response to HS, as well as the transcriptional response regulated by NO to cope with HS has not been reported. We used RNA-Seq technology to generate large-scale transcriptome data from G...
November 16, 2017: Scientific Reports
Signe Mosegaard, Gitte Hoffmann Bruun, Karen Freund Flyvbjerg, Yngve Thomas Bliksrud, Niels Gregersen, Maja Dembic, Ellen Annexstad, Trine Tangeraas, Rikke Katrine Jentoft Olsen, Brage S Andresen
Vitamin B2, riboflavin is essential for cellular function, as it participates in a diversity of redox reactions central to human metabolism, through its role as precursor for the cofactors flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD), which are electron carriers. The electron transfer flavoprotein (ETF) and its dehydrogenase (ETFDH), uses FAD as cofactor. The ETF and ETFDH are forming the electron transport pathway for many mitochondrial flavoprotein dehydrogenases involved in fatty acid, amino acid and choline metabolism...
December 2017: Molecular Genetics and Metabolism
Vinita Jagannath, Zacharias Faidon Brotzakis, Michele Parrinello, Susanne Walitza, Edna Grünblatt
Dysfunction of D-amino acid oxidase (DAO) and DAO activator (DAOA)/G72 genes have been linked to neuropsychiatric disorders. The glutamate hypothesis of schizophrenia has proposed that increased DAO activity leads to decreased D-serine, which subsequently may lead to N-methyl-D-aspartate (NMDA) receptor hypofunction. It has been shown that DAOA binds to DAO and increases its activity. However, there are also studies showing DAOA decreases DAO activity. Thus, the effect of DAOA on DAO is controversial. We aimed to understand the effect of DAOA on DAO activity in neuron-like (SH-SY5Y), astrocyte-like (1321N1) and kidney-like (HEK293) human cell lines...
2017: Frontiers in Molecular Neuroscience
Ryan A Kelley, Muayyad R Al-Ubaidi, Tirthankar Sinha, Ayse M Genc, Mustafa S Makia, Larissa Ikelle, Muna I Naash
The interface between the neural retina and the retinal pigment epithelium (RPE) is critical for several processes, including visual pigment regeneration and retinal attachment to the RPE. One of its most important functions is the exchange of metabolites between the photoreceptors and RPE because photoreceptor cells have very high energy demands, largely satisfied by oxidative metabolism. The riboflavin (RF) cofactors, flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN) are two key cofactors involved in oxidative metabolism...
October 27, 2017: Journal of Biological Chemistry
Negar Babaei Omali, Lakshman N Subbaraman, Miriam Heynen, Zohra Fadli, Chantal Coles-Brennan, Lyndon W Jones
SIGNIFICANCE: Albumin deposition on contact lenses could be detrimental to contact lens (CL) wear because this may increase the risk of bacterial binding and reduce comfort. Lysozyme deposition on selected lens materials would reduce albumin deposition on lenses. PURPOSE: This study aims to determine if lysozyme deposition on CLs could act as a barrier against subsequent albumin adsorption, using an in vitro model. METHODS: Six hydrogel CL materials (etafilcon A, polymacon, nelfilcon A, omafilcon A, ocufilcon B, and nesofilcon A) were evaluated...
November 2017: Optometry and Vision Science: Official Publication of the American Academy of Optometry
Yoshio Nakatani, Wanting Jiao, David Aragão, Yosuke Shimaki, Jessica Petri, Emily J Parker, Gregory M Cook
Type II NADH:quinone oxidoreductase (NDH-2) is a respiratory enzyme found in the electron-transport chain of many species, with the exception of mammals. It is a 40-70 kDa single-subunit monotopic membrane protein that catalyses the oxidation of NADH and the reduction of quinone molecules via the cofactor FAD. NDH-2 is a promising new target for drug development given its essential role in many bacterial species and intracellular parasites. Only two bacterial NDH-2 structures have been reported and these structures are at moderate resolution (2...
October 1, 2017: Acta Crystallographica. Section F, Structural Biology Communications
Hirak R Dash, Mousumi Sahu, Bibekanand Mallick, Surajit Das
MerA protein of mer operon in mercury resistant bacteria influences transformation of Hg(2+) to Hg(0). Both in-silico and in-vivo studies have been carried out and MerA sequences, conserved motifs for mercury binding and NADPH (GCVPSK and LSCCA) varied widely in both Gram-positive and Gram-negative bacteria. As MerA-NADPH-FAD complex plays an important role in mercury volatilization, molecular interaction studies between MerA, NADPH, FAD and Hg(2+) was carried out to study the efficiency of transformation of Hg(2+) to Hg(0) in mercury resistant bacteria...
November 2017: Biochimie
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