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https://www.readbyqxmd.com/read/28802828/photolyase-dynamics-and-electron-transfer-mechanisms-of-dna-repair
#1
REVIEW
Meng Zhang, Lijuan Wang, Dongping Zhong
Photolyase, a flavoenzyme containing flavin adenine dinucleotide (FAD) molecule as a catalytic cofactor, repairs UV-induced DNA damage of cyclobutane pyrimidine dimer (CPD) and pyrimidine-pyrimidone (6-4) photoproduct using blue light. The FAD cofactor, conserved in the whole protein superfamily of photolyase/cryptochromes, adopts a unique folded configuration at the active site that plays a critical functional role in DNA repair. Here, we review our comprehensive characterization of the dynamics of flavin cofactor and its repair photocycles by different classes of photolyases on the most fundamental level...
August 9, 2017: Archives of Biochemistry and Biophysics
https://www.readbyqxmd.com/read/28796306/enzyme-activation-with-a-synthetic-catalytic-coenzyme-intermediate-nucleotide-methylation-by-new-flavoenzymes
#2
Charles Bou-Nader, Cornu David, Vincent Guerineau, Marc Fontecave, Djemel Hamdane
To facilitate production of functional enzymes and to study their mechanisms, especially in the complex cases of coenzyme-dependent systems, activation of an inactive apoenzyme preparation with a catalytically competent coenzyme intermediate is an attractive strategy. This is illustrated with the simple chemical synthesis of a flavin-methylene iminium compound previously proposed as a key intermediate in the catalytic cycle of several important flavoenzymes involved in nucleic acids metabolism. Reconstitution of both flavin-dependent RNA methyltransferase and thymidylate synthase apoproteins with this synthetic compound led to active enzymes for the C5-uracil methylation within their respective transfer RNA and dUMP substrate...
August 10, 2017: Angewandte Chemie
https://www.readbyqxmd.com/read/28782586/breaking-the-mirror-l-amino-acid-deaminase-a-novel-stereoselective-biocatalyst
#3
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...
August 3, 2017: Biotechnology Advances
https://www.readbyqxmd.com/read/28750088/a-single-nucleotide-polymorphism-causes-enhanced-radical-oxygen-species-production-by-human-aldehyde-oxidase
#4
Alessandro Foti, Frank Dorendorf, Silke Leimkühler
Aldehyde oxidases (AOXs) are molybdo-flavoenzymes characterized by broad substrate specificity, oxidizing aromatic/aliphatic aldehydes into the corresponding carboxylic acids and hydroxylating various heteroaromatic rings. The enzymes use oxygen as the terminal electron acceptor and produce reduced oxygen species during turnover. The physiological function of mammalian AOX isoenzymes is still unclear, however, human AOX (hAOX1) is an emerging enzyme in phase-I drug metabolism. Indeed, the number of xenobiotics acting as hAOX1 substrates is increasing...
2017: PloS One
https://www.readbyqxmd.com/read/28745052/identification-of-the-tyroh-%C3%A2-radical-cation-in-the-flavoenzyme-trmfo
#5
Lipsa Nag, Pierre Sournia, Hannu Myllykallio, Ursula Liebl, Marten H Vos
Tyrosine (TyrOH) and tryptophan radicals play important roles as intermediates in biochemical charge-transfer reactions. Tryptophanyl radicals have been observed both in their protonated cation form and in their unprotonated neutral form, but to date, tyrosyl radicals have only been observed in their unprotonated form. With a genetically modified form of the flavoenzyme TrmFO as a suitable model system and using ultrafast fluorescence and absorption spectroscopy, we characterize its protonated precursor TyrOH(•+), and we show this species to have a distinct visible absorption band and a transition moment that we suggest to lie close to the phenol symmetry axis...
August 8, 2017: Journal of the American Chemical Society
https://www.readbyqxmd.com/read/28712849/structure-function-and-mechanism-of-proline-utilization-a-puta
#6
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
https://www.readbyqxmd.com/read/28694766/flavoenzyme-mediated-reduction-reactions-and-antitumor-activity-of-nitrogen-containing-tetracyclic-ortho-quinone-compounds-and-their-nitrated-derivatives
#7
Milda Peciukaityte-Alksne, Jonas Šarlauskas, Lina Miseviciene, Audrone Maroziene, Narimantas Cenas, Kastis Krikštopaitis, Zita Staniulyte, Žilvinas Anusevicius
Nitrogen-based tetracyclic ortho-quinones (naphtho[1'2':4.5]imidazo[1,2-a]pyridine-5,6-diones, NPDOs) and their nitro-substituted derivatives (nitro-(P)NPDOs) were obtained by condensation of substituted 2,3-dichloro-1,4-naphthoquinones with 2-amino-pyridine and -pyrimidine and nitration at an elevated temperature. The structural features of the compounds as well as their global and regional electrophilic potency were characterized by means of DFT computation. The compounds were highly reactive substrates of single- and two-electron (hydride) - transferring P-450R (CPR; EC 1...
2017: EXCLI journal
https://www.readbyqxmd.com/read/28666740/the-dihydroorotate-dehydrogenases-past-and-present
#8
REVIEW
Renata A G Reis, Felipe Antunes Calil, Patricia Rosa Feliciano, Matheus Pinto Pinheiro, M Cristina Nonato
The flavoenzyme dihydroorotate dehydrogenase catalyzes the stereoselective oxidation of (S)-dihydroorotate to orotate in the fourth of the six conserved enzymatic reactions involved in the de novo pyrimidine biosynthetic pathway. Inhibition of pyrimidine metabolism by selectively targeting DHODHs has been exploited in the development of new therapies against cancer, immunological disorders, bacterial and viral infections, and parasitic diseases. Through a chronological narrative, this review summarizes the efforts of the scientific community to achieve our current understanding of structural and biochemical properties of DHODHs...
June 27, 2017: Archives of Biochemistry and Biophysics
https://www.readbyqxmd.com/read/28661684/ruta-catalyzed-oxidative-cleavage-of-the-uracil-amide-involves-formation-of-a-flavin-n5-oxide
#9
Sanjoy Adak, Tadhg P Begley
RutA is a novel flavoenzyme on the uracil catabolic pathway that catalyzes uracil ring opening by a unique amide oxidation reaction. Here we provide evidence that this reaction also involves the formation of a flavin-N5-oxide.
July 25, 2017: Biochemistry
https://www.readbyqxmd.com/read/28652025/multiple-functionalities-of-reduced-flavin-in-the-non-redox-reaction-catalyzed-by-udp-galactopyranose-mutase
#10
REVIEW
Pablo Sobrado, John J Tanner
Flavin cofactors are widely used by enzymes to catalyze a broad range of chemical reactions. Traditionally, flavins in enzymes are regarded as redox centers, which enable enzymes to catalyze the oxidation or reduction of substrates. However, a new class of flavoenzyme has emerged over the past quarter century in which the flavin functions as a catalytic center in a non-redox reaction. Here we introduce the unifying concept of flavin hot spots to understand and categorize the mechanisms and reactivities of both traditional and noncanonical flavoenzymes...
June 24, 2017: Archives of Biochemistry and Biophysics
https://www.readbyqxmd.com/read/28643772/cryptic-indole-hydroxylation-by-a-non-canonical-terpenoid-cyclase-parallels-bacterial-xenobiotic-detoxification
#11
Susann Kugel, Martin Baunach, Philipp Baer, Mie Ishida-Ito, Srividhya Sundaram, Zhongli Xu, Michael Groll, Christian Hertweck
Terpenoid natural products comprise a wide range of molecular architectures that typically result from C-C bond formations catalysed by classical type I/II terpene cyclases. However, the molecular diversity of biologically active terpenoids is substantially increased by fully unrelated, non-canonical terpenoid cyclases. Their evolutionary origin has remained enigmatic. Here we report the in vitro reconstitution of an unusual flavin-dependent bacterial indoloterpenoid cyclase, XiaF, together with a designated flavoenzyme-reductase (XiaP) that mediates a key step in xiamycin biosynthesis...
June 15, 2017: Nature Communications
https://www.readbyqxmd.com/read/28640638/enzyme-mediated-conversion-of-flavin-adenine-dinucleotide-fad-to-8-formyl-fad-in-formate-oxidase-results-in-a-modified-cofactor-with-enhanced-catalytic-properties
#12
John M Robbins, Michael G Souffrant, Donald Hamelberg, Giovanni Gadda, Andreas S Bommarius
Flavins, including flavin adenine dinucleotide (FAD), are fundamental catalytic cofactors that are responsible for the redox functionality of a diverse set of proteins. Alternatively, modified flavin analogues are rarely found in nature as their incorporation typically results in inactivation of flavoproteins, thus leading to the disruption of important cellular pathways. Here, we report that the fungal flavoenzyme formate oxidase (FOX) catalyzes the slow conversion of noncovalently bound FAD to 8-formyl FAD and that this conversion results in a nearly 10-fold increase in formate oxidase activity...
July 25, 2017: Biochemistry
https://www.readbyqxmd.com/read/28602956/structure-function-studies-of-mical-the-unusual-multidomain-flavoenzyme-involved-in-actin-cytoskeleton-dynamics
#13
REVIEW
Maria Antonietta Vanoni
MICAL (from the Molecule Interacting with CasL) indicates a family of multidomain proteins conserved from insects to humans, which are increasingly attracting attention for their participation in the control of actin cytoskeleton dynamics, and, therefore, in the several related key processes in health and disease. MICAL is unique among actin binding proteins because it catalyzes a NADPH-dependent F-actin depolymerizing reaction. This unprecedented reaction is associated with its N-terminal FAD-containing domain that is structurally related to p-hydroxybenzoate hydroxylase, the prototype of aromatic monooxygenases, but catalyzes a strong NADPH oxidase activity in the free state...
June 8, 2017: Archives of Biochemistry and Biophysics
https://www.readbyqxmd.com/read/28583428/multiscale-simulation-of-monoamine-oxidase-catalyzed-decomposition-of-phenylethylamine-analogs
#14
Gabriel Oanca, Jernej Stare, Robert Vianello, Janez Mavri
Phenylethylamine (PEA) is an endogenous amphetamine and its levels are increased by physical activity. As other biogenic monoamines, it is decomposed by monoamine oxidase (MAO) enzymes. The chemical mechanism of MAO, and flavoenzymes in general, is a subject of heated debate. We have previously shown that the rate-limiting step of MAO catalysis involves a hydride transfer from the substrate methylene group vicinal to the amino group to the N5 atom of the lumiflavin co-factor moiety. By using multiscale simulation on the Empirical Valence Bond (EVB) level, we studied the chemical reactivity of the monoamine oxidase B catalyzed decomposition of PEA and its two derivatives: p-chloro-β-methylphenylamine (p-CMP) and p-methoxy-β-methylphenethylamine (p-MMP)...
June 3, 2017: European Journal of Pharmacology
https://www.readbyqxmd.com/read/28577910/the-type-ii-isopentenyl-diphosphate-dimethylallyl-diphosphate-isomerase-idi-2-a-model-for-acid-base-chemistry-in-flavoenzyme-catalysis
#15
REVIEW
Christopher J Thibodeaux, Hung-Wen Liu
The chemical versatility of the flavin coenzyme is nearly unparalleled in enzyme catalysis. An interesting illustration of this versatility can be found in the reaction catalyzed by the type II isopentenyl diphosphate:dimethylallyl diphosphate isomerase (IDI-2) - an enzyme that interconverts the two essential isoprene units (isopentenyl pyrophosphate and dimethylallyl pyrophosphate) that are needed to initiate the biosynthesis of all isoprenoids. Over the past decade, a variety of biochemical, spectroscopic, structural and mechanistic studies of IDI-2 have provided mounting evidence that the flavin coenzyme of IDI-2 acts in a most unusual manner - as an acid/base catalyst to mediate a 1,3-proton addition/elimination reaction...
May 31, 2017: Archives of Biochemistry and Biophysics
https://www.readbyqxmd.com/read/28558236/identification-of-a-conserved-histidine-as-being-critical-for-the-catalytic-mechanism-and-functional-switching-of-the-multifunctional-proline-utilization-a-protein
#16
Michael A Moxley, Lu Zhang, Shelbi Christgen, John J Tanner, Donald F Becker
Proline utilization A from Escherichia coli (EcPutA) is a multifunctional flavoenzyme that oxidizes proline to glutamate through proline dehydrogenase (PRODH) and Δ(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH) activities, while also switching roles as a DNA-bound transcriptional repressor and a membrane-bound catabolic enzyme. This phenomenon, termed functional switching, occurs through a redox-mediated mechanism in which flavin reduction triggers a conformational change that increases EcPutA membrane binding affinity...
June 20, 2017: Biochemistry
https://www.readbyqxmd.com/read/28545445/identification-of-enterococcus-faecalis-enzymes-with-azoreductases-and-or-nitroreductase-activity
#17
Valérie Chalansonnet, Claire Mercier, Sylvain Orenga, Christophe Gilbert
BACKGROUND: Nitroreductases, NAD(P)H dependent flavoenzymes, are found in most of bacterial species. Even if Enterococcus faecalis strains seems to present such activity because of their sensitivity to nitrofurans, no enzyme has been described. Nitroreductases were separated of others reductases due to their capacity to reduce nitro compounds. They are further classified based on their preference in cofactor: NADH and/or NADPH. However, recently, azoreductases have been studied for their strong activity on nitro compounds, especially nitro pro-drugs...
May 25, 2017: BMC Microbiology
https://www.readbyqxmd.com/read/28528298/emerging-role-of-monoamine-oxidase-as-a-therapeutic-target-for-cardiovascular-disease
#18
REVIEW
Soni Deshwal, Moises Di Sante, Fabio Di Lisa, Nina Kaludercic
In the past decade, accumulating evidence highlighted the role of monoamine oxidases (MAOs) in cardiovascular disease (CVD). MAOs are flavoenzymes located in the outer mitochondrial membrane, responsible for the degradation of neurotransmitters and biogenic amines. During this process they generate hydrogen peroxide, aldehydes and ammonia, species that can target mitochondria and induce mitochondrial dysfunction and cardiomyocyte death. Indeed, MAO inhibition affords cardioprotection in several models of CVD, such as ischemia/reperfusion, heart failure and diabetes...
May 18, 2017: Current Opinion in Pharmacology
https://www.readbyqxmd.com/read/28508424/computational-site-directed-mutagenesis-studies-of-the-role-of-the-hydrophobic-triad-on-substrate-binding-in-cholesterol-oxidase
#19
Laith Hisham Harb, Mahreen Arooj, Alice Vrielink, Ricardo L Mancera
Cholesterol oxidase (ChOx) is a flavoenzyme that oxidizes and isomerizes cholesterol (CHL) to form cholest-4-en-3-one. Molecular docking and molecular dynamics simulations were conducted to predict the binding interactions of CHL in the active site. Several key interactions (E361-CHL, N485-FAD, and H447-CHL) were identified and which are likely to determine the correct positioning of CHL relative to flavin-adenine dinucleotide (FAD). Binding of CHL also induced changes in key residues of the active site leading to the closure of the oxygen channel...
May 15, 2017: Proteins
https://www.readbyqxmd.com/read/28481346/plasticity-dynamics-and-inhibition-of-emerging-tetracycline-resistance-enzymes
#20
Jooyoung Park, Andrew J Gasparrini, Margaret R Reck, Chanez T Symister, Jennifer L Elliott, Joseph P Vogel, Timothy A Wencewicz, Gautam Dantas, Niraj H Tolia
Although tetracyclines are an important class of antibiotics for use in agriculture and the clinic, their efficacy is threatened by increasing resistance. Resistance to tetracyclines can occur through efflux, ribosomal protection, or enzymatic inactivation. Surprisingly, tetracycline enzymatic inactivation has remained largely unexplored, despite providing the distinct advantage of antibiotic clearance. The tetracycline destructases are a recently discovered family of tetracycline-inactivating flavoenzymes from pathogens and soil metagenomes that have a high potential for broad dissemination...
July 2017: Nature Chemical Biology
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