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Flavoenzyme

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https://www.readbyqxmd.com/read/29417050/d-amino-acid-oxidase-plg72-interaction-and-d-serine-modulation
#1
REVIEW
Loredano Pollegioni, Luciano Piubelli, Gianluca Molla, Elena Rosini
pLG72 is a small, primate-specific protein of 153 amino acids. It is the product of the G72 gene, expressed in testis, spinal cord, and brain. The presence of G72 transcript and pLG72 has recurrently been called into question, however G72 mRNA and pLG72 protein levels were higher in blood and brain of patients with schizophrenia than in healthy controls. On the one hand, the SNP rs2391191 corresponding to the R30K substitution in pLG72 was genetically linked to schizophrenia, reduced thickness of the brain cortex in schizophrenia-affected individuals, and altered memory function...
2018: Frontiers in Molecular Biosciences
https://www.readbyqxmd.com/read/29400320/structural-characterization-of-porphyromonas-gingivalis-enoyl-acp-reductase-ii-fabk
#2
Kirk E Hevener, Bernard D Santarsiero, Hyun Lee, Jesse A Jones, Teuta Boci, Michael E Johnson, Shahila Mehboob
Enoyl-acyl carrier protein (ACP) reductase II (FabK) is a critical rate-limiting enzyme in the bacterial type II fatty-acid synthesis (FAS II) pathway. FAS II pathway enzymes are markedly disparate from their mammalian analogs in the FAS I pathway in both structure and mechanism. Enzymes involved in bacterial fatty-acid synthesis represent viable drug targets for Gram-negative pathogens, and historical precedent exists for targeting them in the treatment of diseases of the oral cavity. The Gram-negative organism Porphyromonas gingivalis represents a key causative agent of the costly and highly prevalent disease known as chronic periodontitis, and exclusively expresses FabK as its enoyl reductase enzyme in the FAS-II pathway...
February 1, 2018: Acta Crystallographica. Section F, Structural Biology Communications
https://www.readbyqxmd.com/read/29372418/tyrosine-residues-232-and-401-play-a-critical-role-in-the-binding-of-the-cofactor-fad-of-acyl-coa-oxidase
#3
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
https://www.readbyqxmd.com/read/29370288/direct-comparison-of-the-four-aldehyde-oxidase-enzymes-present-in-mouse-gives-insight-into-their-substrate-specificities
#4
Gökhan Kücükgöze, Silke Leimkühler
Mammalian aldehyde oxidases (AOXs) are molybdo-flavoenzymes which are present in many tissues in various mammalian species, including humans and rodents. Different species contain a different number of AOX isoforms. In particular, the reasons why mammals other than humans express a multiplicity of tissue-specific AOX enzymes is unknown. In mouse, the isoforms mAOX1, mAOX3, mAOX4 and mAOX2 are present. We previously established a codon-optimized heterologous expression systems for the mAOX1-4 isoforms in Escherichia coli that gives yield to sufficient amounts of active protein for kinetic characterizations and sets the basis in this study for site-directed mutagenesis and structure-function studies...
2018: PloS One
https://www.readbyqxmd.com/read/29359850/bioorthogonal-catalytic-activation-of-pt-and-ru-anticancer-complexes-by-fad-and-flavoproteins
#5
Silvia Alonso-de Castro, Aitziber Lopez Cortajarena, Fernando Lopez-Gallego, Luca Salassa
Recent advances in bioorthogonal catalysis promise to deliver new chemical tools for performing chemoselective transformations in complex biological environments. Herein we report how FAD (flavin adenine dinucleotide), FMN (flavin mononucleotide) and four flavoproteins behave as unconventional photocatalysts capable of converting PtIV and RuII complexes into potentially toxic PtII or RuII-OH2 species. Using electron donors and low doses of visible light, the flavoproteins mini Singlet Oxygen Generator (miniSOG) and NADH oxidase (NOX) catalytically activate PtIV prodrugs with bioorthogonal selectivity...
January 23, 2018: Angewandte Chemie
https://www.readbyqxmd.com/read/29348404/crystal-structure-of-an-assembly-intermediate-of-respiratory-complex-ii
#6
Pankaj Sharma, Elena Maklashina, Gary Cecchini, T M Iverson
Flavin is covalently attached to the protein scaffold in ~10% of flavoenzymes. However, the mechanism of covalent modification is unclear, due in part to challenges in stabilizing assembly intermediates. Here, we capture the structure of an assembly intermediate of the Escherichia coli Complex II (quinol:fumarate reductase (FrdABCD)). The structure contains the E. coli FrdA subunit bound to covalent FAD and crosslinked with its assembly factor, SdhE. The structure contains two global conformational changes as compared to prior structures of the mature protein: the rotation of a domain within the FrdA subunit, and the destabilization of two large loops of the FrdA subunit, which may create a tunnel to the active site...
January 18, 2018: Nature Communications
https://www.readbyqxmd.com/read/29341594/designing-flavoprotein-gfp-fusion-probes-for-analyte-specific-ratiometric-fluorescence-imaging
#7
Devin A Hudson, Jeffrey L Caplan, Colin Thorpe
The development of genetically encoded fluorescent probes for analyte-specific imaging has revolutionized our understanding of intracellular processes. Current classes of intracellular probes depend on the selection of binding domains that either undergo conformational changes on analyte binding or can be linked to thiol redox chemistry. Here we have designed novel probes by fusing a flavoenzyme, whose fluorescence is quenched on reduction by the analyte of interest, with a GFP domain to allow for rapid and specific ratiometric sensing...
January 17, 2018: Biochemistry
https://www.readbyqxmd.com/read/29337919/functional-impact-of-the-n-terminal-arm-of-proline-dehydrogenase-from-thermus-thermophilus
#8
Mieke M E Huijbers, Ilona van Alen, Jenny W Wu, Arjan Barendregt, Albert J R Heck, Willem J H van Berkel
Proline dehydrogenase (ProDH) is a ubiquitous flavoenzyme that catalyzes the oxidation of proline to Δ¹-pyrroline-5-carboxylate. Thermus thermophilus ProDH (TtProDH) contains in addition to its flavin-binding domain an N-terminal arm, consisting of helices αA, αB, and αC. Here, we report the biochemical properties of the helical arm truncated TtProDH variants ΔA, ΔAB, and ΔABC, produced with maltose-binding protein as solubility tag. All three truncated variants show similar spectral properties as TtProDH, indicative of a conserved flavin-binding pocket...
January 16, 2018: Molecules: a Journal of Synthetic Chemistry and Natural Product Chemistry
https://www.readbyqxmd.com/read/29332274/callitriche-cophocarpa-water-starwort-proteome-under-chromate-stress-evidence-for-induction-of-a-quinone-reductase
#9
Paweł Kaszycki, Aleksandra Dubicka-Lisowska, Joanna Augustynowicz, Barbara Piwowarczyk, Wojciech Wesołowski
Chromate-induced physiological stress in a water-submerged macrophyte Callitriche cophocarpa Sendtn. (water starwort) was tested at the proteomic level. The oxidative stress status of the plant treated with 1 mM Cr(VI) for 3 days revealed stimulation of peroxidases whereas catalase and superoxide dismutase activities were similar to the control levels. Employing two-dimensional electrophoresis, comparative proteomics enabled to detect five differentiating proteins subjected to identification with mass spectrometry followed by an NCBI database search...
January 13, 2018: Environmental Science and Pollution Research International
https://www.readbyqxmd.com/read/29325897/an-improved-cell-permeable-fluorogenic-substrate-as-the-basis-for-a-highly-sensitive-test-for-nad-p-h-quinone-oxidoreductase-1-nqo1-in-living-cells
#10
Simone Cuff, Ruth D Lewis, Edwin Chinje, Mohammed Jaffar, Richard Knox, Ian Weeks
NAD(P)H:quinone oxidoreductase 1 (NQO1) is a flavoenzyme upregulated in response to oxidative stress and in some cancers. Its upregulation by compounds has been used as an indicator of their potential anti-cancer properties. In this study we have designed, produced and tested a fluorogenic coumarin conjugate which selectively releases highly fluorescent 4-methylumbelliferone (4-MU) in the presence of NQO1. It was found that measuring 4-MU release rapidly and specifically quantitated NQO1 levels in vitro and in live cells...
January 8, 2018: Free Radical Biology & Medicine
https://www.readbyqxmd.com/read/29323892/same-substrate-many-reactions-oxygen-activation-in-flavoenzymes
#11
Elvira Romero, J Rubén Gómez Castellanos, Giovanni Gadda, Marco W Fraaije, Andrea Mattevi
Over time, organisms have evolved strategies to cope with the abundance of dioxygen on Earth. Oxygen-utilizing enzymes tightly control the reactions involving O2 mostly by modulating the reactivity of their cofactors. Flavins are extremely versatile cofactors that are capable of undergoing redox reactions by accepting either one electron or two electrons, alternating between the oxidized and the reduced states. The physical and chemical principles of flavin-based chemistry have been investigated widely. In the following pages we summarize the state of the art on a key area of research in flavin enzymology: the molecular basis for the activation of O2 by flavin-dependent oxidases and monooxygenases...
January 11, 2018: Chemical Reviews
https://www.readbyqxmd.com/read/29295473/structural-basis-for-the-substrate-inhibition-of-proline-utilization-a-by-proline
#12
David A Korasick, Travis A Pemberton, Benjamin W Arentson, Donald F Becker, John J Tanner
Proline utilization A (PutA) is a bifunctional flavoenzyme that catalyzes the two-step oxidation of l-proline to l-glutamate using spatially separated proline dehydrogenase (PRODH) and l-glutamate-γ-semialdehyde dehydrogenase (GSALDH) active sites. Substrate inhibition of the coupled PRODH-GSALDH reaction by proline is a common kinetic feature of PutAs, yet the structural basis for this phenomenon remains unknown. To understand the mechanism of substrate inhibition, we determined the 2.15 Å resolution crystal structure of Bradyrhizobium japonicum PutA complexed with proline...
December 23, 2017: Molecules: a Journal of Synthetic Chemistry and Natural Product Chemistry
https://www.readbyqxmd.com/read/29283425/molecular-basis-for-converting-2s-methylsuccinyl-coa-dehydrogenase-into-an-oxidase
#13
Simon Burgener, Thomas Schwander, Elvira Romero, Marco W Fraaije, Tobias J Erb
Although flavoenzymes have been studied in detail, the molecular basis of their dioxygen reactivity is only partially understood. The members of the flavin adenosine dinucleotide (FAD)-dependent acyl-CoA dehydrogenase and acyl-CoA oxidase families catalyze similar reactions and share common structural features. However, both enzyme families feature opposing reaction specificities in respect to dioxygen. Dehydrogenases react with electron transfer flavoproteins as terminal electron acceptors and do not show a considerable reactivity with dioxygen, whereas dioxygen serves as a bona fide substrate for oxidases...
December 28, 2017: Molecules: a Journal of Synthetic Chemistry and Natural Product Chemistry
https://www.readbyqxmd.com/read/29250527/competitive-inhibitors-unveil-structure-function-relationships-in-human-d-amino-acid-oxidase
#14
REVIEW
Gianluca Molla
D-amino acid oxidase (DAAO) catalyzes the oxidative deamination of several neutral D-amino acids and is the enzyme mainly responsible (together with serine racemase) for degrading D-serine (D-Ser) in the central nervous system of mammals. This D-amino acid, which binds the coagonist site of the N-methyl-D-aspartate receptor, is thus a key neuromodulator of glutamatergic neurotransmission. Altered D-Ser metabolism results in several pathological conditions (e.g., amylotrophic lateral sclerosis or schizophrenia, SZ) for which effective "broad spectrum" pharmaceutical drugs are not yet available...
2017: Frontiers in Molecular Biosciences
https://www.readbyqxmd.com/read/29240409/from-experiments-to-a-fast-easy-to-use-computational-methodology-to-predict-human-aldehyde-oxidase-selectivity-and-metabolic-reactions
#15
Gabriele Cruciani, Nicolò Milani, Paolo Benedetti, Susan Lepri, Lucia Cesarini, Massimo Baroni, Francesca Spyrakis, Sara Tortorella, Edoardo Mosconi, Laura Goracci
Aldehyde oxidase (AOX) is a molibdo-flavoenzyme that raised great interest in recent years, since its contribution in xenobiotics metabolism has not always been identified before clinical trials, with consequent negative effects on the fate of new potential drugs. The fundamental role of AOX in metabolizing xenobiotics is also due to the attempt of medicinal chemists to stabilize candidates toward cytochrome P450 activity, which increases the risk for new compounds to be susceptible to AOX nucleophile attack...
December 14, 2017: Journal of Medicinal Chemistry
https://www.readbyqxmd.com/read/29221464/molecular-and-functional-characterization-of-ferredoxin-nadp-h-oxidoreductase-from-gracilaria-chilensis-and-its-complex-with-ferredoxin
#16
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 1.18.1.2) (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
https://www.readbyqxmd.com/read/29168057/-1-h-15-n-and-13-c-backbone-resonance-assignments-of-pentaerythritol-tetranitrate-reductase-from-enterobacter-cloacae-pb2
#17
Andreea I Iorgu, Nicola J Baxter, Matthew J Cliff, Jonathan P Waltho, Sam Hay, Nigel S Scrutton
Pentaerythritol tetranitrate reductase (PETNR) is a flavoenzyme possessing a broad substrate specificity and is a member of the Old Yellow Enzyme family of oxidoreductases. As well as having high potential as an industrial biocatalyst, PETNR is an excellent model system for studying hydrogen transfer reactions. Mechanistic studies performed with PETNR using stopped-flow methods have shown that tunneling contributes towards hydride transfer from the NAD(P)H coenzyme to the flavin mononucleotide (FMN) cofactor and fast protein dynamics have been inferred to facilitate this catalytic step...
November 22, 2017: Biomolecular NMR Assignments
https://www.readbyqxmd.com/read/29133410/unprecedented-pathway-of-reducing-equivalents-in-a-diflavin-linked-disulfide-oxidoreductase
#18
Rubén M Buey, Juan B Arellano, Luis López-Maury, Sergio Galindo-Trigo, Adrián Velázquez-Campoy, José L Revuelta, José M de Pereda, Francisco J Florencio, Peter Schürmann, Bob B Buchanan, Monica Balsera
Flavoproteins participate in a wide variety of physiologically relevant processes that typically involve redox reactions. Within this protein superfamily, there exists a group that is able to transfer reducing equivalents from FAD to a redox-active disulfide bridge, which further reduces disulfide bridges in target proteins to regulate their structure and function. We have identified a previously undescribed type of flavin enzyme that is exclusive to oxygenic photosynthetic prokaryotes and that is based on the primary sequence that had been assigned as an NADPH-dependent thioredoxin reductase (NTR)...
November 13, 2017: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/29124817/why-the-flavin-dinucleotide-cofactor-needs-to-be-covalently-linked-to-complex-ii-of-the-electron-transport-chain-for-conversion-of-fadh2-to-fad
#19
Daniel F A R Dourado, Marcel Swart, Alexandra Teresa Pires Carvalho
A covalently bound flavin cofactor is predominant in the succinate:ubiquinone oxidoreductase (SQR, Complex II), an essential component of the aerobic electron transport, and in the menaquinol:fumarate oxidoreductase (QFR), the anaerobic counterpart, albeit being only present in ~10% of the known flavoenzymes. Here, we investigated the role of this 8α-N(3)-histidyl linkage between the flavin dinucleotide (FAD) cofactor and the respiratory Complex II. After parameterization with DFT we performed classical molecular dynamics simulations and quantum mechanics calculations of Complex II:FAD and Complex II:FADH2, covalently bound and unbound to His-A57...
November 10, 2017: Chemistry: a European Journal
https://www.readbyqxmd.com/read/29116682/flavin-n5-covalent-intermediate-in-the-non-redox-dehalogenation-reaction-catalyzed-by-an-atypical-flavoenzyme
#20
Yumin Dai, Karina Kizjakina, Ashley C Campbell, David A Korasick, John J Tanner, Pablo Sobrado
The flavin-dependent enzyme 2-haloacrylate hydratase (2-HAH) catalyzes the conversion of 2-chloroacrylate, a major component in the manufacture of acrylic polymers, to pyruvate. The enzyme from has been expressed in Escherichia coli, purified, and characterized. 2-HAH is monomeric in solution and contains a non-covalent, yet tightly bound, FAD. Although the reaction catalyzed is redox neutral, 2-HAH is active only in the reduced state. A covalent flavin-substrate intermediate, consistent with the flavin-acrylate iminium ion, was trapped with cyanoborohydride and characterized by mass spectrometry...
November 8, 2017: Chembiochem: a European Journal of Chemical Biology
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