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Flavoenzyme

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https://www.readbyqxmd.com/read/28643772/cryptic-indole-hydroxylation-by-a-non-canonical-terpenoid-cyclase-parallels-bacterial-xenobiotic-detoxification
#1
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-fad-to-8-formyl-fad-in-formate-oxidase-results-in-modified-cofactor-with-enhanced-catalytic-properties
#2
John M Robbins, Michael G Souffrant, Donald Hamelberg, Giovanni Gadda, Andreas S Bommarius
Flavins, including flavin adenine dinucleotide (FAD), are fundamental catalytic cofactors 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 non-covalently bound FAD to 8-formyl FAD (8-fFAD), and that this conversion results in a nearly 10-fold increase in formate oxidase activity...
June 22, 2017: Biochemistry
https://www.readbyqxmd.com/read/28602956/structure-function-studies-of-mical-the-unusual-multidomain-flavoenzyme-involved-in-actin-cytoskeleton-dynamics
#3
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
#4
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
#5
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
#6
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 8, 2017: Biochemistry
https://www.readbyqxmd.com/read/28545445/identification-of-enterococcus-faecalis-enzymes-with-azoreductases-and-or-nitroreductase-activity
#7
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
#8
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
#9
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
#10
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
https://www.readbyqxmd.com/read/28475111/riboflavin-responsive-mitochondrial-dysfunction-in-neurodegenerative-diseases
#11
REVIEW
Tamilarasan Udhayabanu, Andreea Manole, Mohan Rajeshwari, Perumal Varalakshmi, Henry Houlden, Balasubramaniem Ashokkumar
Mitochondria are the repository for various metabolites involved in diverse energy-generating processes, like the TCA cycle, oxidative phosphorylation, and metabolism of amino acids, fatty acids, and nucleotides, which rely significantly on flavoenzymes, such as oxidases, reductases, and dehydrogenases. Flavoenzymes are functionally dependent on biologically active flavin adenine dinucleotide (FAD) or flavin mononucleotide (FMN), which are derived from the dietary component riboflavin, a water soluble vitamin...
May 5, 2017: Journal of Clinical Medicine
https://www.readbyqxmd.com/read/28420730/structure-and-characterization-of-a-class-3b-proline-utilization-a-ligand-induced-dimerization-and-importance-of-the-c-terminal-domain-for-catalysis
#12
David A Korasick, Thameesha T Gamage, Shelbi Christgen, Kyle M Stiers, Lesa J Beamer, Michael T Henzl, Donald F Becker, John J Tanner
The bifunctional flavoenzyme proline utilization A (PutA) catalyzes the two-step oxidation of proline to glutamate using separate proline dehydrogenase (PRODH) and l-glutamate-γ-semialdehyde dehydrogenase active sites. Because PutAs catalyze sequential reactions, they are good systems for studying how metabolic enzymes communicate via substrate channeling. Although mechanistically similar, PutAs vary widely in domain architecture, oligomeric state, and quaternary structure, and these variations represent different structural solutions to the problem of sequestering a reactive metabolite...
June 9, 2017: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/28397795/the-structure-of-lactococcus-lactis-thioredoxin-reductase-reveals-molecular-features-of-photo-oxidative-damage
#13
Nicklas Skjoldager, Maria Blanner Bang, Martin Rykær, Olof Björnberg, Michael J Davies, Birte Svensson, Pernille Harris, Per Hägglund
The NADPH-dependent homodimeric flavoenzyme thioredoxin reductase (TrxR) provides reducing equivalents to thioredoxin, a key regulator of various cellular redox processes. Crystal structures of photo-inactivated thioredoxin reductase (TrxR) from the Gram-positive bacterium Lactococcus lactis have been determined. These structures reveal novel molecular features that provide further insight into the mechanisms behind the sensitivity of this enzyme toward visible light. We propose that a pocket on the si-face of the isoalloxazine ring accommodates oxygen that reacts with photo-excited FAD generating superoxide and a flavin radical that oxidize the isoalloxazine ring C7α methyl group and a nearby tyrosine residue...
April 11, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28355481/mechanistic-studies-of-an-amine-oxidase-derived-from-d-amino-acid-oxidase
#14
Elizabeth E Trimmer, Udayanga S Wanninayake, Paul F Fitzpatrick
The flavoprotein d-amino acid oxidase has long served as a paradigm for understanding the mechanism of oxidation of amino acids by flavoproteins. Recently, a mutant d-amino acid oxidase (Y228L/R283G) that catalyzed the oxidation of amines rather than amino acids was described [Yasukawa, K., et al. (2014) Angew. Chem., Int. Ed. 53, 4428-4431]. We describe here the use of pH and kinetic isotope effects with (R)-α-methylbenzylamine as a substrate to determine whether the mutant enzyme utilizes the same catalytic mechanism as the wild-type enzyme...
April 11, 2017: Biochemistry
https://www.readbyqxmd.com/read/28336409/development-and-crystallographic-evaluation-of-histone-h3-peptide-with-n-terminal-serine-substitution-as-a-potent-inhibitor-of-lysine-specific-demethylase-1
#15
Yuichi Amano, Masaki Kikuchi, Shin Sato, Shigeyuki Yokoyama, Takashi Umehara, Naoki Umezawa, Tsunehiko Higuchi
Lysine-specific demethylase 1 (LSD1/KDM1A) is a flavoenzyme demethylase, which removes mono- and dimethyl groups from histone H3 Lys4 (H3K4) or Lys9 (H3K9) in complexes with several nuclear proteins. Since LSD1 is implicated in the tumorigenesis and progression of various cancers, LSD1-specific inhibitors are considered as potential anti-cancer agents. A modified H3 peptide with substitution of Lys4 to Met [H3K4M] is already known to be a potent competitive inhibitor of LSD1. In this study, we synthesized a series of H3K4M peptide derivatives and evaluated their LSD1-inhibitory activities in vitro...
March 9, 2017: Bioorganic & Medicinal Chemistry
https://www.readbyqxmd.com/read/28288625/functional-differentiation-of-3-ketosteroid-%C3%AE-1-dehydrogenase-isozymes-in-rhodococcus-ruber-strain-chol-4
#16
Govinda Guevara, Laura Fernández de Las Heras, Julián Perera, Juana María Navarro Llorens
BACKGROUND: The Rhodococcus ruber strain Chol-4 genome contains at least three putative 3-ketosteroid Δ(1)-dehydrogenase ORFs (kstD1, kstD2 and kstD3) that code for flavoenzymes involved in the steroid ring degradation. The aim of this work is the functional characterization of these enzymes prior to the developing of different biotechnological applications. RESULTS: The three R. ruber KstD enzymes have different substrate profiles. KstD1 shows preference for 9OHAD and testosterone, followed by progesterone, deoxy corticosterone AD and, finally, 4-BNC, corticosterone and 19OHAD...
March 14, 2017: Microbial Cell Factories
https://www.readbyqxmd.com/read/28274732/flavins-as-covalent-catalysts-new-mechanisms-emerge
#17
REVIEW
Valentina Piano, Bruce A Palfey, Andrea Mattevi
With approximately 1% of proteins being flavoproteins, flavins are at the heart of a plethora of redox reactions in all areas of biology. Thanks to a series of fascinating recent discoveries, in addition to redox chemistry, covalent catalysis is now being recognized more frequently as a common strategy in flavoenzymes, with unprecedented mechanisms becoming apparent. Thus, noncanonical covalent reactions by flavins are emerging as a new pervasive concept in basic enzymology and biochemistry. These diverse enzymes are engaged in most biological processes, positioning the knowledge being gained from these new mechanisms to be translated into drugs that function through covalent mechanisms...
March 5, 2017: Trends in Biochemical Sciences
https://www.readbyqxmd.com/read/28256579/proline-dehydrogenase-from-thermus-thermophilus-does-not-discriminate-between-fad-and-fmn-as-cofactor
#18
Mieke M E Huijbers, Marta Martínez-Júlvez, Adrie H Westphal, Estela Delgado-Arciniega, Milagros Medina, Willem J H van Berkel
Flavoenzymes are versatile biocatalysts containing either FAD or FMN as cofactor. FAD often binds to a Rossmann fold, while FMN prefers a TIM-barrel or flavodoxin-like fold. Proline dehydrogenase is denoted as an exception: it possesses a TIM barrel-like fold while binding FAD. Using a riboflavin auxotrophic Escherichia coli strain and maltose-binding protein as solubility tag, we produced the apoprotein of Thermus thermophilus ProDH (MBP-TtProDH). Remarkably, reconstitution with FAD or FMN revealed that MBP-TtProDH has no preference for either of the two prosthetic groups...
March 3, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28225078/distribution-of-valence-electrons-of-the-flavin-cofactor-in-nadh-cytochrome-b5-reductase
#19
Kiyofumi Takaba, Kazuki Takeda, Masayuki Kosugi, Taro Tamada, Kunio Miki
Flavin compounds such as flavin adenine dinucleotide (FAD), flavin mononucleotide and riboflavin make up the active centers in flavoproteins that facilitate various oxidoreductive processes. The fine structural features of the hydrogens and valence electrons of the flavin molecules in the protein environment are critical to the functions of the flavoproteins. However, information on these features cannot be obtained from conventional protein X-ray analyses at ordinary resolution. Here we report the charge density analysis of a flavoenzyme, NADH-cytochrome b5 reductase (b5R), at an ultra-high resolution of 0...
February 22, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28192293/the-intrinsic-fluorescence-of-fad-and-its-application-in-analytical-chemistry-a-review
#20
Javier Galbán, Isabel Sanz-Vicente, Jesús Navarro, Susana de Marcos
This review (with 106 references) mainly deals with the analytical applications of flavin-adenine dinucleotide (FAD) fluorescence. In the first section, the spectroscopic properties of this compound are reviewed at the light of his different acid-base, oxidation and structural forms; the chemical and spectroscopic properties of flavin mononucleotide (FMN) and other flavins will be also briefly discussed. The second section discusses how the properties of FAD fluorescence changes in flavoenzymes (FvEs), again considering the different chemical and structural forms; the glucose oxidase (GOx) and the choline oxidase (ChOx) cases will be commented...
December 19, 2016: Methods and Applications in Fluorescence
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