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Journal articles on the topic 'NAD-bound'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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1

Kalinina, Sviatlana, Christian Freymueller, Nilanjon Naskar, et al. "Bioenergetic Alterations of Metabolic Redox Coenzymes as NADH, FAD and FMN by Means of Fluorescence Lifetime Imaging Techniques." International Journal of Molecular Sciences 22, no. 11 (2021): 5952. http://dx.doi.org/10.3390/ijms22115952.

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Metabolic FLIM (fluorescence lifetime imaging) is used to image bioenergetic status in cells and tissue. Whereas an attribution of the fluorescence lifetime of coenzymes as an indicator for cell metabolism is mainly accepted, it is debated whether this is valid for the redox state of cells. In this regard, an innovative algorithm using the lifetime characteristics of nicotinamide adenine dinucleotide (phosphate) (NAD(P)H) and flavin adenine dinucleotide (FAD) to calculate the fluorescence lifetime induced redox ratio (FLIRR) has been reported so far. We extended the FLIRR approach and present

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2

Kim, Yong Ju. "A cryoprotectant induces conformational change in glyceraldehyde-3-phosphate dehydrogenase." Acta Crystallographica Section F Structural Biology Communications 74, no. 5 (2018): 277–82. http://dx.doi.org/10.1107/s2053230x18004557.

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Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), a glycolytic enzyme, catalyses the conversion of D-glyceraldehyde 3-phosphate to 1,3-bisphosphoglycerate. While mammalian and yeast GAPDHs are multifunctional proteins that have additional functions beyond those involved in glycolysis, including reactions related to nuclear RNA transport, DNA replication/repair, membrane fusion and cellular apoptosis, Escherichia coli GAPDH (ecGAPDH) has only been reported to function in glycolysis. The S-loop of GAPDH is required for interaction with its cofactor and with other proteins. In this study, the thr

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3

Galloway, T. S., R. M. Tait, and S. van Heyningen. "Photolabelling of cholera toxin by NAD+." Biochemical Journal 242, no. 3 (1987): 927–30. http://dx.doi.org/10.1042/bj2420927.

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When cholera toxin is incubated under u.v. light with NAD+ labelled in either the adenine or the nicotinamide moiety, radioactivity becomes covalently bound to the protein. The reaction is specific for cholera toxin, and is inhibited by excess unlabelled NAD+ or NAD analogues. Only the active A 1 chain of the toxin is labelled. The u.v.-absorption spectrum of the product is very similar to that of NAD+, and shows the same reaction with cyanide. The nature of the product is therefore different from that found when diphtheria toxin is photolabelled [Carroll & Collier (1984) Proc. Natl. Acad.

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4

Bell, Charles E., Todd O. Yeates, and David Eisenberg. "Unusual conformation of nicotinamide adenine dinucleotide (NAD) bound to diphtheria toxin: A comparison with NAD bound to the oxidoreductase enzymes." Protein Science 6, no. 10 (2008): 2084–96. http://dx.doi.org/10.1002/pro.5560061004.

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5

Aguilar-Arnal, Lorena, Suman Ranjit, Chiara Stringari, Ricardo Orozco-Solis, Enrico Gratton, and Paolo Sassone-Corsi. "Spatial dynamics of SIRT1 and the subnuclear distribution of NADH species." Proceedings of the National Academy of Sciences 113, no. 45 (2016): 12715–20. http://dx.doi.org/10.1073/pnas.1609227113.

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Sirtuin 1 (SIRT1) is an NAD+-dependent deacetylase that functions as metabolic sensor of cellular energy and modulates biochemical pathways in the adaptation to changes in the environment. SIRT1 substrates include histones and proteins related to enhancement of mitochondrial function as well as antioxidant protection. Fluctuations in intracellular NAD+ levels regulate SIRT1 activity, but how SIRT1 enzymatic activity impacts on NAD+ levels and its intracellular distribution remains unclear. Here, we show that SIRT1 determines the nuclear organization of protein-bound NADH. Using multiphoton mic

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6

Hu, Yumei, Weidong Liu, Satish R. Malwal, et al. "Structures of Iridoid Synthase fromCantharanthus roseuswith Bound NAD+, NADPH, or NAD+/10-Oxogeranial: Reaction Mechanisms." Angewandte Chemie 127, no. 51 (2015): 15698–702. http://dx.doi.org/10.1002/ange.201508310.

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7

Hu, Yumei, Weidong Liu, Satish R. Malwal, et al. "Structures of Iridoid Synthase fromCantharanthus roseuswith Bound NAD+, NADPH, or NAD+/10-Oxogeranial: Reaction Mechanisms." Angewandte Chemie International Edition 54, no. 51 (2015): 15478–82. http://dx.doi.org/10.1002/anie.201508310.

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8

Cummings, M. D., T. N. Hart, B. Hazes, and R. J. Read. "Modeling the structure of NAD bound to pertussis toxin." Acta Crystallographica Section A Foundations of Crystallography 52, a1 (1996): C88. http://dx.doi.org/10.1107/s0108767396095566.

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9

Thomas, Leonard M., Angelica R. Harper, Whitney A. Miner, et al. "Structure ofEscherichia coliAdhP (ethanol-inducible dehydrogenase) with bound NAD." Acta Crystallographica Section F Structural Biology and Crystallization Communications 69, no. 7 (2013): 730–32. http://dx.doi.org/10.1107/s1744309113015170.

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10

Niesner, R., P. Narang, H. Spiecker, V. Andresen, K. H. Gericke, and M. Gunzer. "Selective Detection of NADPH Oxidase in Polymorphonuclear Cells by Means of NAD(P)H-Based Fluorescence Lifetime Imaging." Journal of Biophysics 2008 (November 16, 2008): 1–13. http://dx.doi.org/10.1155/2008/602639.

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NADPH oxidase (NOX2) is a multisubunit membrane-bound enzyme complex that, upon assembly in activated cells, catalyses the reduction of free oxygen to its superoxide anion, which further leads to reactive oxygen species (ROS) that are toxic to invading pathogens, for example, the fungus Aspergillus fumigatus. Polymorphonuclear cells (PMNs) employ both nonoxidative and oxidative mechanisms to clear this fungus from the lung. The oxidative mechanisms mainly depend on the proper assembly and function of NOX2. We identified for the first time the NAD(P)H-dependent enzymes involved in such oxidativ

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11

Anderlund, Mikael, Torben L. Nissen, Jens Nielsen, et al. "Expression of the Escherichia coli pntA andpntB Genes, Encoding Nicotinamide Nucleotide Transhydrogenase, in Saccharomyces cerevisiae and Its Effect on Product Formation during Anaerobic Glucose Fermentation." Applied and Environmental Microbiology 65, no. 6 (1999): 2333–40. http://dx.doi.org/10.1128/aem.65.6.2333-2340.1999.

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ABSTRACT We studied the physiological effect of the interconversion between the NAD(H) and NADP(H) coenzyme systems in recombinantSaccharomyces cerevisiae expressing the membrane-bound transhydrogenase from Escherichia coli. Our objective was to determine if the membrane-bound transhydrogenase could work in reoxidation of NADH to NAD+ in S. cerevisiaeand thereby reduce glycerol formation during anaerobic fermentation. Membranes isolated from the recombinant strains exhibited reduction of 3-acetylpyridine-NAD+ by NADPH and by NADH in the presence of NADP+, which demonstrated that an active enzy

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12

Moller, I. M., and W. Lin. "Membrane-Bound NAD(P)H Dehydrogenases in Higher Plant Cells." Annual Review of Plant Physiology 37, no. 1 (1986): 309–34. http://dx.doi.org/10.1146/annurev.pp.37.060186.001521.

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13

Joannou, C. L., and P. R. Brown. "NAD-dependent glutamate dehydrogenase fromPseudomonas aeruginosais a membrane-bound enzyme." FEMS Microbiology Letters 90, no. 2 (1992): 205–10. http://dx.doi.org/10.1111/j.1574-6968.1992.tb05153.x.

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14

Tsai, C. Stan, and D. J. Senior. "Dual coenzyme activities of high-Km aldehyde dehydrogenase from rat liver mitochondria." Biochemistry and Cell Biology 68, no. 4 (1990): 751–57. http://dx.doi.org/10.1139/o90-108.

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Various kinetic approaches were carried out to investigate kinetic attributes for the dual coenzyme activities of mitochondrial aldehyde dehydrogenase from rat liver. The enzyme catalyses NAD+- and NADP+-dependent oxidations of ethanal by an ordered bi-bi mechanism with NAD(P)+ as the first reactant bound and NAD(P)H as the last product released. The two coenzymes presumably interact with the kinetically identical site. NAD+ forms the dynamic binary complex with the enzyme, while the enzyme-NAD(P)H complex formation is associated with conformation change(s). A stopped-flow burst of NAD(P)H for

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15

Okai, Masahiko, Norio Kudo, Woo Cheol Lee, Masayuki Kamo, Koji Nagata, and Masaru Tanokura. "Crystal Structures of the Short-Chain Flavin Reductase HpaC fromSulfolobus tokodaiiStrain 7 in Its Three States: NAD(P)+-Free, NAD+-Bound, and NADP+-Bound†,‡." Biochemistry 45, no. 16 (2006): 5103–10. http://dx.doi.org/10.1021/bi052313i.

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16

Zhang, Chunxiang, Jian Yang, Jonathan D. Jacobs, and Lisa K. Jennings. "Interaction of myeloperoxidase with vascular NAD(P)H oxidase-derived reactive oxygen species in vasculature: implications for vascular diseases." American Journal of Physiology-Heart and Circulatory Physiology 285, no. 6 (2003): H2563—H2572. http://dx.doi.org/10.1152/ajpheart.00435.2003.

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Vascular NAD(P)H oxidase-derived reactive oxygen species (ROS) such as hydrogen peroxide (H2O2) have emerged as important molecules in the pathogenesis of atherosclerosis, hypertension, and diabetic vascular complications. Additionally, myeloperoxidase (MPO), a transcytosable heme protein that is derived from leukocytes, is also believed to play important roles in the above-mentioned inflammatory vascular diseases. Previous studies have shown that MPO-induced vascular injury responses are H2O2 dependent. It is well known that MPO can use leukocyte-derived H2O2; however, it is unknown whether t

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17

Franza, Thierry, Annika Rogstam, Saravanamuthu Thiyagarajan, et al. "NAD+ pool depletion as a signal for the Rex regulon involved in Streptococcus agalactiae virulence." PLOS Pathogens 17, no. 8 (2021): e1009791. http://dx.doi.org/10.1371/journal.ppat.1009791.

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In many Gram-positive bacteria, the redox-sensing transcriptional repressor Rex controls central carbon and energy metabolism by sensing the intra cellular balance between the reduced and oxidized forms of nicotinamide adenine dinucleotide; the NADH/NAD+ ratio. Here, we report high-resolution crystal structures and characterization of a Rex ortholog (Gbs1167) in the opportunistic pathogen, Streptococcus agalactiae, also known as group B streptococcus (GBS). We present structures of Rex bound to NAD+ and to a DNA operator which are the first structures of a Rex-family member from a pathogenic b

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18

Penfound, Thomas, and John W. Foster. "NAD-Dependent DNA-Binding Activity of the Bifunctional NadR Regulator of Salmonella typhimurium." Journal of Bacteriology 181, no. 2 (1999): 648–55. http://dx.doi.org/10.1128/jb.181.2.648-655.1999.

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ABSTRACT NadR is a 45-kDa bifunctional regulator protein. In vivo genetic studies indicate that NadR represses three genes involved in the biosynthesis of NAD. It also participates with an integral membrane protein (PnuC) in the import of nicotinamide mononucleotide, an NAD precursor. NadR was overexpressed and purified as a His-tagged fusion in order to study its DNA-binding properties. The protein bound to DNA fragments containing NAD box consensus sequences. NAD proved to be the relevant in vivo corepressor, but full NAD dependence of repressor activity required nucleotide triphosphates. DN

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19

Kishimoto, Toshihiko, Masaaki Itami, Tetsuya Yomo, Itaru Urabe, Yasuhiro Yamada, and Hirosuke Okada. "Improved methods for the preparation of N6-(2-carboxyethyl)-NAD and poly(ethylene glycol)-bound NAD(H)." Journal of Fermentation and Bioengineering 71, no. 6 (1991): 447–49. http://dx.doi.org/10.1016/0922-338x(91)90262-f.

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20

Vanhommerig, Sylvia A. M., Lamoraal A. Æ. Sluyterman, and Emmo M. Meijer. "Kinetic and modelling studies of NAD+ and poly(ethylene glycol)-bound NAD+ in horse liver alcohol dehydrogenase." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1295, no. 2 (1996): 125–38. http://dx.doi.org/10.1016/0167-4838(96)00026-x.

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21

Gallais, Stéphane, Marie-Anne Pou de Crescenzo, and Danielle L. Laval-Martin. "Changes in soluble and membrane-bound isoforms of calcium-calmodulin-dependent and -independent NAD+ kinase, during the culture of after-ripened and dormant seeds of Avena sativa." Functional Plant Biology 27, no. 7 (2000): 649. http://dx.doi.org/10.1071/pp00010.

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Activities of the soluble and membrane-boundisoforms of Ca 2+ calmodulin (CaCam)-dependent and-independent NAD + kinases, were followed in theembryos during the culture of dormant (D) and after-ripened (AR) seeds ofAvena sativa L. Embryos of D and AR seeds differ mainly in the evolution ofmembrane-bound activities, the majority of which are CaCam-dependent andlinked to mitochondria. The in vivo application ofgibberellic acid, CaCl2 andH2O2, which enhanced germination,induced an enhancement of all CaCam-dependent isoforms. Trifluoperazine (TFP),a calmodulin antagonist, greatly enhanced all CaCa

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22

Chen, Meirong, Zuoqi Gai, Chiaki Okada, Yuxin Ye, Jian Yu, and Min Yao. "Flexible NAD+ Binding in Deoxyhypusine Synthase Reflects the Dynamic Hypusine Modification of Translation Factor IF5A." International Journal of Molecular Sciences 21, no. 15 (2020): 5509. http://dx.doi.org/10.3390/ijms21155509.

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The eukaryotic and archaeal translation factor IF5A requires a post-translational hypusine modification, which is catalyzed by deoxyhypusine synthase (DHS) at a single lysine residue of IF5A with NAD+ and spermidine as cofactors, followed by hydroxylation to form hypusine. While human DHS catalyzed reactions have been well characterized, the mechanism of the hypusination of archaeal IF5A by DHS is not clear. Here we report a DHS structure from Pyrococcus horikoshii OT3 (PhoDHS) at 2.2 Å resolution. The structure reveals two states in a single functional unit (tetramer): two NAD+-bound monomers

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23

Jacobi, Tobias, and Christoph Woenckhaus. "NAD covalent-bound to dehydrogenases — a model compound for enzyme electrodes." Fresenius' Zeitschrift für analytische Chemie 324, no. 3-4 (1986): 274. http://dx.doi.org/10.1007/bf00487919.

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24

Chen, Yong-Qing, Jeroen van Beek, Hua Deng, John Burgner, and Robert Callender. "Vibrational Structure of NAD(P) Cofactors Bound to Three NAD(P) Dependent Enzymes: an Investigation of Ground State Activation." Journal of Physical Chemistry B 106, no. 41 (2002): 10733–40. http://dx.doi.org/10.1021/jp025635u.

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25

Kirby, Christina A., Atwood Cheung, Aleem Fazal, Michael D. Shultz, and Travis Stams. "Structure of human tankyrase 1 in complex with small-molecule inhibitors PJ34 and XAV939." Acta Crystallographica Section F Structural Biology and Crystallization Communications 68, no. 2 (2012): 115–18. http://dx.doi.org/10.1107/s1744309111051219.

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The crystal structures of tankyrase 1 (TNKS1) in complex with two small-molecule inhibitors, PJ34 and XAV939, both at 2.0 Å resolution, are reported. The structure of TNKS1 in complex with PJ34 reveals two molecules of PJ34 bound in the NAD+donor pocket. One molecule is in the nicotinamide portion of the pocket, as previously observed in other PARP structures, while the second molecule is bound in the adenosine portion of the pocket. Additionally, unlike the unliganded crystallization system, the TNKS1–PJ34 crystallization system has the NAD+donor site accessible to bulk solvent in the crystal

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26

Steuber, Julia, Walter Krebs, Michael Bott, and Peter Dimroth. "A Membrane-Bound NAD(P)+-Reducing Hydrogenase Provides Reduced Pyridine Nucleotides during Citrate Fermentation by Klebsiella pneumoniae." Journal of Bacteriology 181, no. 1 (1999): 241–45. http://dx.doi.org/10.1128/jb.181.1.241-245.1999.

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ABSTRACT During anaerobic growth of Klebsiella pneumoniae on citrate, 9.4 mmol of H2/mol of citrate (4-kPa partial pressure) was formed at the end of growth besides acetate, formate, and CO2. Upon addition of NiCl2 (36 μM) to the growth medium, hydrogen formation increased about 36% to 14.8 mmol/mol of citrate (6 kPa), and the cell yield increased about 15%. Cells that had been harvested and washed under anoxic conditions exhibited an H2-dependent formation of NAD(P)H in vivo. The reduction of internal NAD(P)+ was also achieved by the addition of formate. In crude extracts, the H2:NAD+oxidored

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27

Nakamura, S., M. Koga, S. Kataoka, M. Oda, T. Ohkubo та Y. Kobayashi. "Structures of NADH and NAD+bound 3α-hydroxysteroid dehydrogenase fromPseudomonassp. B-0831". Acta Crystallographica Section A Foundations of Crystallography 64, a1 (2008): C267. http://dx.doi.org/10.1107/s0108767308091460.

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28

LIN, LI-SHENG, LI-NA LIU, HUI-FANG HUANG, YUAN-ZHONG CHEN, BU-HONG LI, and ZHENG HUANG. "CHARACTERIZING FLUORESCENCE LIFETIME OF NAD(P)H IN HUMAN LEUKEMIC MYELOID CELLS AND MONONUCLEAR CELLS." Journal of Innovative Optical Health Sciences 06, no. 04 (2013): 1350042. http://dx.doi.org/10.1142/s1793545813500429.

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The aim of this ex vivo study was to explore the potential of using the fluorescence lifetime of intracellular reduced nicotinamide adenine dinucleotide (phosphate) (NAD(P)H) as a label-free indicator to characterize the differences between human leukemic myeloid cells and normal mononuclear cells (MNC). The steady-state and time-resolved autofluorescence of two human leukemic myeloid cell lines (K562, HL60) and MNC were measured by a spectrofluorimeter. According to excitation–emission matrix (EEM) analysis, the optimal emission of NAD(P)H in these cells suspensions occurred at 445 nm. Furthe

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29

de Crescenzo, Marie-Anne Pou, Ken Goto, Isabelle A. Carré, and Danielle L. Laval-Martin. "Regulation of a NAD + Kinase Activity Isolated from Asynchronous Cultures of the Achlorophyllous ZC Mutant of Euglena gracilis." Zeitschrift für Naturforschung C 52, no. 9-10 (1997): 623–35. http://dx.doi.org/10.1515/znc-1997-9-1009.

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NAD+ kinase was isolated by chromatography steps from asynchronous cultures of the achlorophyllous ZC mutant of Euglena gracilis. A non Ca2+-calmodulin dependent form, whose activity was stimulated by EGTA, was selected for its large quantity and high specific activity. Studies of the kinetic parameters revealed two kinds of NAD+ binding site, depending on NAD+ concentrations, and changes induced by EGTA, Ca2+ and Ca2+-calmodulin. The search for effectors, soluble (S) and membrane-bound (P), in Euglena gracilis synchronously grown (in a light-dark regime of 12h:12h), and collected at circadian

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30

Hu, Yumei, Weidong Liu, Satish R. Malwal, et al. "Titelbild: Structures of Iridoid Synthase fromCantharanthus roseuswith Bound NAD+, NADPH, or NAD+/10-Oxogeranial: Reaction Mechanisms (Angew. Chem. 51/2015)." Angewandte Chemie 127, no. 51 (2015): 15517. http://dx.doi.org/10.1002/ange.201510890.

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31

Unciuleac, Mihaela-Carmen, Yehuda Goldgur, and Stewart Shuman. "Two-metal versus one-metal mechanisms of lysine adenylylation by ATP-dependent and NAD+-dependent polynucleotide ligases." Proceedings of the National Academy of Sciences 114, no. 10 (2017): 2592–97. http://dx.doi.org/10.1073/pnas.1619220114.

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Polynucleotide ligases comprise a ubiquitous superfamily of nucleic acid repair enzymes that join 3′-OH and 5′-PO4DNA or RNA ends. Ligases react with ATP or NAD+and a divalent cation cofactor to form a covalent enzyme-(lysine-Nζ)–adenylate intermediate. Here, we report crystal structures of the founding members of the ATP-dependent RNA ligase family (T4 RNA ligase 1; Rnl1) and the NAD+-dependent DNA ligase family (Escherichia coliLigA), captured as their respective Michaelis complexes, which illuminate distinctive catalytic mechanisms of the lysine adenylylation reaction. The 2.2-Å Rnl1•ATP•(M

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32

Czygier, M., and S. A. Strumiło. "Basic properties of the pyruvate dehydrogenase complex isolated from aurochs heart." Acta Biochimica Polonica 41, no. 4 (1994): 453–57. http://dx.doi.org/10.18388/abp.1994_4696.

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The purified aurochs (Bison bonasus, European bison) heart pyruvate dehydrogenase complex (PDC) has a set of subunits typical of mammalian PDC. PDC from aurochs heart contains firmly bound tiamine pyrophosphate in the amount providing over 50% of the maximal activity of the complex. The apparent value for activation energy of PDC is 60 kJ/mol. The Michaelis constant values for aurochs heart PDC are 22.4 +/- 1.0, 3.3 +/- 0.1 and 24.4 +/- 3.6 microM for pyruvate, CoA and NAD, accordingly. Acetyl-CoA is a competitive inhibitor with respect to CoA (Ki = 14.2 +/- 0.4 microM), whereas NADH gives the

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33

Kitson, T. M., and K. E. Kitson. "Probing the active site of cytoplasmic aldehyde dehydrogenase with a chromophoric reporter group." Biochemical Journal 300, no. 1 (1994): 25–30. http://dx.doi.org/10.1042/bj3000025.

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3,4-Dihydro-3-methyl-6-nitro-2H-1,3-benzoxazin-2-one (‘DMNB’) reacts with cytoplasmic aldehyde dehydrogenase in a similar way to that previously observed with the structurally related p-nitrophenyl dimethylcarbamate, but provides a covalently linked p-nitrophenol-containing reporter group at the enzyme's active site. The pKa of the enzyme-linked reporter group is much higher than that of free p-nitrophenol, which is consistent with its being in a very hydrophobic environment, or possibly one containing negative charge. Upon binding of NAD+ to the modified enzyme, the pKa falls dramatically, by

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34

González, Javier M., Ricardo Marti-Arbona, Julian C. H. Chen, Brian Broom-Peltz, and Clifford J. Unkefer. "Conformational changes on substrate binding revealed by structures of Methylobacterium extorquens malate dehydrogenase." Acta Crystallographica Section F Structural Biology Communications 74, no. 10 (2018): 610–16. http://dx.doi.org/10.1107/s2053230x18011809.

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Three high-resolution X-ray crystal structures of malate dehydrogenase (MDH; EC 1.1.1.37) from the methylotroph Methylobacterium extorquens AM1 are presented. By comparing the structures of apo MDH, a binary complex of MDH and NAD+, and a ternary complex of MDH and oxaloacetate with ADP-ribose occupying the pyridine nucleotide-binding site, conformational changes associated with the formation of the catalytic complex were characterized. While the substrate-binding site is accessible in the enzyme resting state or NAD+-bound forms, the substrate-bound form exhibits a closed conformation. This c

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35

MONTAINE, France, Jean-Pierre LENDERS, and Robert R. CRICHTON. "Use of a polymer-bound flavin derivative for the rapid regeneration of NAD(P)+ from NAD(P)H in dehydrogenase systems." European Journal of Biochemistry 164, no. 2 (1987): 329–36. http://dx.doi.org/10.1111/j.1432-1033.1987.tb11062.x.

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36

Deng, Hua, John Burgner, and Robert Callender. "Raman spectroscopic studies of NAD coenzymes bound to malate dehydrogenases by difference techniques." Biochemistry 30, no. 36 (1991): 8804–11. http://dx.doi.org/10.1021/bi00100a011.

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37

Koide, S., S. Yokoyama, H. Matsuzawa, T. Miyazawa, and T. Ohta. "Conformation of NAD+ Bound to Allosteric L-Lactate Dehydrogenase Activated by Chemical Modification." Journal of Biological Chemistry 264, no. 15 (1989): 8676–79. http://dx.doi.org/10.1016/s0021-9258(18)81845-2.

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38

Jin, Xiangshu, and James H. Geiger. "Structures of NAD+- and NADH-bound 1-L-myo-inositol 1-phosphate synthase." Acta Crystallographica Section D Biological Crystallography 59, no. 7 (2003): 1154–64. http://dx.doi.org/10.1107/s0907444903008205.

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39

Kato, Nobuo, Tomohide Yamagami, Masayuki Shimao, and Chikahiro Sakazawa. "Regeneration of NAD(H) covalently bound to formate dehydrogenase with several second enzymes." Applied Microbiology and Biotechnology 25, no. 5 (1987): 415–18. http://dx.doi.org/10.1007/bf00253310.

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40

Li, Mingguang, Brian J. Petteys, Julie M. McClure, et al. "Thiamine Biosynthesis in Saccharomyces cerevisiae Is Regulated by the NAD+-Dependent Histone Deacetylase Hst1." Molecular and Cellular Biology 30, no. 13 (2010): 3329–41. http://dx.doi.org/10.1128/mcb.01590-09.

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ABSTRACT Genes encoding thiamine biosynthesis enzymes in microorganisms are tightly regulated such that low environmental thiamine concentrations activate transcription and high concentrations are repressive. We have determined that multiple thiamine (THI) genes in Saccharomyces cerevisiae are also regulated by the intracellular NAD+ concentration via the NAD+-dependent histone deacetylase (HDAC) Hst1 and, to a lesser extent, Sir2. Both of these HDACs associate with a distal region of the affected THI gene promoters that does not overlap with a previously defined enhancer region bound by the t

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EGUCHI, Tamotsu, Takashi IIZUKA, Tadashi KAGOTANI, Joung Hee LEE, Itaru URABE, and Hirosuke OKADA. "Covalent linking of poly(ethyleneglycol)-bound NAD with Thermus thermophilus malate dehydrogenase. NAD(H)-regeneration unit for a coupled second-enzyme reaction." European Journal of Biochemistry 155, no. 2 (1986): 415–21. http://dx.doi.org/10.1111/j.1432-1033.1986.tb09507.x.

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42

Leben, Köhler, Radbruch, Hauser, and Niesner. "Systematic Enzyme Mapping of Cellular Metabolism by Phasor-Analyzed Label-Free NAD(P)H Fluorescence Lifetime Imaging." International Journal of Molecular Sciences 20, no. 22 (2019): 5565. http://dx.doi.org/10.3390/ijms20225565.

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In the past years, cellular metabolism of the immune system experienced a revival, as it has become clear that it is not merely responsible for the cellular energy supply, but also impacts on many signaling pathways and, thus, on diverse cellular functions. Label-free fluorescence lifetime imaging of the ubiquitous coenzymes NADH and NADPH (NAD(P)H-FLIM) makes it possible to monitor cellular metabolism in living cells and tissues and has already been applied to study metabolic changes both under physiologic and pathologic conditions. However, due to the complex distribution of NAD(P)H-dependen

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Choe, Hyunjun, Jung Min Ha, Jeong Chan Joo, et al. "Structural insights into the efficient CO2-reducing activity of an NAD-dependent formate dehydrogenase fromThiobacillussp. KNK65MA." Acta Crystallographica Section D Biological Crystallography 71, no. 2 (2015): 313–23. http://dx.doi.org/10.1107/s1399004714025474.

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CO2fixation is thought to be one of the key factors in mitigating global warming. Of the various methods for removing CO2, the NAD-dependent formate dehydrogenase fromCandida boidinii(CbFDH) has been widely used in various biological CO2-reduction systems; however, practical applications of CbFDH have often been impeded owing to its low CO2-reducing activity. It has recently been demonstrated that the NAD-dependent formate dehydrogenase fromThiobacillussp. KNK65MA (TsFDH) has a higher CO2-reducing activity compared with CbFDH. The crystal structure of TsFDH revealed that the biological unit in

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Sugishima, Masakazu, Kei Wada, and Keiichi Fukuyama. "Recent Advances in the Understanding of the Reaction Chemistries of the Heme Catabolizing Enzymes HO and BVR Based on High Resolution Protein Structures." Current Medicinal Chemistry 27, no. 21 (2020): 3499–518. http://dx.doi.org/10.2174/0929867326666181217142715.

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In mammals, catabolism of the heme group is indispensable for life. Heme is first cleaved by the enzyme Heme Oxygenase (HO) to the linear tetrapyrrole Biliverdin IXα (BV), and BV is then converted into bilirubin by Biliverdin Reductase (BVR). HO utilizes three Oxygen molecules (O2) and seven electrons supplied by NADPH-cytochrome P450 oxidoreductase (CPR) to open the heme ring and BVR reduces BV through the use of NAD(P)H. Structural studies of HOs, including substrate-bound, reaction intermediate-bound, and several specific inhibitor-bound forms, reveal details explaining substrate binding to

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Agnellini, Dario, Mario Pace, Sergio Cinquanta, Claudio Gardana, Pier Giorgio Pietta, and Pier Luigi Mauri. "Characteristics of Bioreactors Made with Urease and Nad Glycohydrolase Reversibly Bound to Immobilized Antibodies." Biocatalysis 6, no. 4 (1992): 251–65. http://dx.doi.org/10.3109/10242429209065246.

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PETTERSSON, Gosta, and Hans EKLUND. "Electrostatic effects of bound NADH and NAD+ on ionizing groups in liver alcohol dehydrogenase." European Journal of Biochemistry 165, no. 1 (1987): 157–61. http://dx.doi.org/10.1111/j.1432-1033.1987.tb11206.x.

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Hu, Yumei, Weidong Liu, Satish R. Malwal, et al. "Cover Picture: Structures of Iridoid Synthase fromCantharanthus roseuswith Bound NAD+, NADPH, or NAD+/10-Oxogeranial: Reaction Mechanisms (Angew. Chem. Int. Ed. 51/2015)." Angewandte Chemie International Edition 54, no. 51 (2015): 15301. http://dx.doi.org/10.1002/anie.201510890.

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Akinterinwa, Olubolaji, and Patrick C. Cirino. "Anaerobic Obligatory Xylitol Production inEscherichia coliStrains Devoid of Native Fermentation Pathways." Applied and Environmental Microbiology 77, no. 2 (2010): 706–9. http://dx.doi.org/10.1128/aem.01890-10.

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ABSTRACTAnaerobic glucose oxidation was coupled to xylose reduction in a nonfermentativeEscherichia colistrain expressing NADPH-dependent xylose reductase. Xylitol production serves as the primary means of NAD(P)+regeneration, as glucose is converted primarily to acetate and CO2. The membrane-bound transhydrogenase PntAB is required to achieve the maximum theoretical yield of four moles of xylitol per mole of glucose consumed.

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Liu, Si-Qi, Hongjun Jin, Albert Zacarias, Sanjay Srivastava та Aruni Bhatnagar. "Binding of Pyridine Nucleotide Coenzymes to the β-Subunit of the Voltage-sensitive K+Channel". Journal of Biological Chemistry 276, № 15 (2001): 11812–20. http://dx.doi.org/10.1074/jbc.m008259200.

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The β-subunit of the voltage-sensitive K+(Kv) channels belongs to the aldo-keto reductase superfamily, and the crystal structure of Kvβ2 shows NADP bound in its active site. Here we report that Kvβ2 displays a high affinity for NADPH (Kd= 0.1 μm) and NADP+(Kd= 0.3 μm), as determined by fluorometric titrations of the recombinant protein. The Kvβ2 also bound NAD(H) but with 10-fold lower affinity. The site-directed mutants R264E and N333W did not bind NADPH, whereas, theKdNADPHof Q214R was 10-fold greater than the wild-type protein. TheKdNADPHwas unaffected by the R189M, W243Y, W243A, or Y255F m

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Kratzer, Regina, and Bernd Nidetzky. "Electrostatic stabilization in a pre-organized polar active site: the catalytic role of Lys-80 in Candida tenuis xylose reductase (AKR2B5) probed by site-directed mutagenesis and functional complementation studies." Biochemical Journal 389, no. 2 (2005): 507–15. http://dx.doi.org/10.1042/bj20050167.

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Lys-80 of Candida tenuis xylose reductase (AKR2B5) is conserved throughout the aldo–keto reductase protein superfamily and may prime the nearby Tyr-51 for general acid catalysis to NAD(P)H-dependent carbonyl group reduction. We have examined the catalytic significance of side-chain substitutions in two AKR2B5 mutants, Lys-80→Ala (K80A) and Asp-46→Asn Lys-80→Ala (D46N K80A), using steady-state kinetic analysis and restoration of activity with external amines. Binding of NAD+ (Kd=24 μM) and NADP+ (Kd=0.03 μM) was 10- and 40-fold tighter in K80A than the wild-type enzyme, whereas binding of NADH

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