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1. Engineering Escherichia coli Nicotinic Acid Mononucleotide Adenylyltransferase for Fully Active Amidated NAD Biosynthesis
by Xueying Wang and Yongjin J Zhou and Lei Wang and Wujun Liu and Yuxue Liu and Chang Peng and Zongbao K Zhao
Applied and Environmental Microbiology, ISSN 0099-2240, 07/2017, Volume 83, Issue 13
NAD and its reduced form NADH function as essential redox cofactors and have major roles in determining cellular metabolic features. NAD can be synthesized... 
NADPH | Nicotinic acid | Biosynthesis | Colorimetry | Cofactors | Proteins | Engineering | NADH | E coli | Vitamin B | Catalysis | Chemical synthesis | Stationary phase | Adenine | Protein biosynthesis | Metabolism | Malic enzyme | Mutants | NAD | Acids | Nicotinamide adenine dinucleotide | Metabolic engineering | Nicotinamide | Organic chemicals | Viability
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2. Homology modeling of human nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2: Insights into isoenzyme-specific differences using molecular docking simulatons
by Eren, Gokcen
Letters in Drug Design and Discovery, ISSN 1570-1808, 01/2017, Volume 14, Issue 6, pp. 727 - 736
Background: Nicotinamide adenine dinucleotide (NAD) is an essential coenzyme that plays crucial roles in energy metabolism, DNA repair and cell death. Due to... 
Gallotannin | NaMNAT | Isoenzyme | NMNAT | Molecular docking | Homology modeling | CHEMISTRY, MEDICINAL | isoenzyme | TIAZOFURIN | NMN/NAMN ADENYLYLTRANSFERASE | HUMAN NMN ADENYLYLTRANSFERASE | RESISTANT | molecular docking | ENZYME | BIOSYNTHESIS | SUBSTRATE | BIOLOGICAL EVALUATION | NAD ANALOGS | INHIBITORS | NADPH | Cell proliferation | Energy metabolism | Nicotinic acid | Homology | Biosynthesis | DNA repair | Coupling (molecular) | Mitochondria | Salvage | Catalysis | Deoxyribonucleic acid--DNA | Crystal structure | Computer simulation | Adenine | Metabolism | NAD | Inhibitors | Cell death | Isoforms | Nicotinamide adenine dinucleotide | Nicotinamide | Drug discovery | Three dimensional models | Cancer
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3. Full Text Crystal Structure of Nicotinic Acid Mononucleotide Adenylyltransferase from Staphyloccocus aureus: Structural Basis for NaAD Interaction in Functional Dimer
by Han, Seungil and Forman, Michael D and Loulakis, Pat and Rosner, Michelle H and Xie, Zhi and Wang, Hong and Danley, Dennis E and Yuan, Wei and Schafer, John and Xu, Zuoyu
Journal of Molecular Biology, ISSN 0022-2836, 2006, Volume 360, Issue 4, pp. 814 - 825
Bacterial nicotinic acid mononucleotide adenylyltransferase (NaMNAT; EC 2.7.7.18) encoded by the gene, is essential for cell survival and is thus an attractive... 
NAD | NaMNAT | functional dimer | nicotinic acid mononucleotide adenylyltransferase | Staphylococcus aureus | BACTERIA | PROTEIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | IDENTIFICATION | REFINEMENT | HUMAN NMN ADENYLYLTRANSFERASE | ENZYME | GENE | BACILLUS-SUBTILIS | NAD BIOSYNTHESIS | EXPRESSION | Amino Acid Sequence | Staphylococcus aureus - enzymology | NAD - analogs & derivatives | Protein Structure, Secondary | Nicotinamide-Nucleotide Adenylyltransferase - metabolism | Molecular Sequence Data | Crystallography, X-Ray | Nicotinamide-Nucleotide Adenylyltransferase - chemistry | Structure-Activity Relationship | NAD - chemistry | Sequence Alignment | Nuclear Magnetic Resonance, Biomolecular | Structural Homology, Protein | Dimerization | NAD - metabolism | Niacinamide | Histidine | Crystals | Adenine | NAD (Coenzyme) | Structure | Niacin
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4. Effect of overexpression of nicotinic acid mononucleotide adenylyltransferase on succinic acid production in Escherichia coli NZN111
by Gou, Dongmei and Liang, Liya and Liu, Rongming and Zhang, Changqing and Wu, Mingke and Ma, Jiangfeng and Chen, Kequan and Zhu, Jianguo and Jiang, Min
Shengwu Gongcheng Xuebao/Chinese Journal of Biotechnology, ISSN 1000-3061, 09/2012, Volume 28, Issue 9, pp. 1059 - 1069
Nicotinic acid mononucleotide adenylyltransferase | Escherichia coli NZN111 | Succinic acid | Anaerobic fermentation | NADH/NAD
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5. Full Text Characterization and application of a novel nicotinamide mononucleotide adenylyltransferase from Thermus thermophilus HB8
by Konishi, Kenji and Ueda, Shigeru and Kawano, Miki and Osawa, Susumu and Tamura, Tomohiro and Hokazono, Eisaku and Kayamori, Yuzo and Sakasegawa, Shin-ichi
Journal of Bioscience and Bioengineering, ISSN 1389-1723, 04/2018, Volume 125, Issue 4, pp. 385 - 389
Herein, we describe a novel enzymatic cycling method to measure nicotinamide mononucleotide (NMN) or nicotinic acid mononucleotide (NaMN), which are precursors... 
Nicotinic acid mononucleotide | Thermus thermophilus HB8 | Nicotinamide mononucleotide | Nicotinamide mononucleotide adenylyltransferase | Enzymatic cycling | CRYSTAL-STRUCTURE | FOOD SCIENCE & TECHNOLOGY | ESCHERICHIA-COLI | IDENTIFICATION | NMN ADENYLYLTRANSFERASE | NUCLEOTIDE | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | NAD(+) | Thermus thermophilus - enzymology | NAD - analogs & derivatives | Nicotinamide-Nucleotide Adenylyltransferase - metabolism | Nicotinamide Mononucleotide - metabolism | Enzyme Assays | Nicotinamide Mononucleotide - analogs & derivatives | Thermus thermophilus - genetics | Tetrazolium Salts - metabolism | Nicotinamide-Nucleotide Adenylyltransferase - isolation & purification | Escherichia coli - genetics | Escherichia coli - metabolism | Nicotinamide-Nucleotide Adenylyltransferase - genetics | NAD - metabolism | Niacinamide | Ligases | Niacin | Escherichia coli | College graduates
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6. Full Text Crystal Structure of Nicotinic Acid Mononucleotide Adenylyltransferase from Pseudomonas aeruginosa in its Apo and Substrate-complexed Forms Reveals a Fully Open Conformation
by Yoon, Hye-Jin and Kim, Hye Lee and Mikami, Bunzo and Suh, Se Won
Journal of Molecular Biology, ISSN 0022-2836, 2005, Volume 351, Issue 2, pp. 258 - 265
The enzyme nicotinic acid mononucleotide adenylyltransferase (NaMN AT; EC 2.7.7.18) is essential for the synthesis of nicotinamide adenine dinucleotide and is... 
nadD | Pseudomonas aeruginosa | nicotinic acid mononucleotide adenylyltransferase | nicotinic acid mononucleotide | NAD biosynthesis | Nicotinic acid mononucleotide adenylyltransferase | Nicotinic acid mononucleotide | GENE | BIOCHEMISTRY & MOLECULAR BIOLOGY | IDENTIFICATION | PROGRAM | Protein Structure, Tertiary | Amino Acid Sequence | Protein Structure, Secondary | Stereoisomerism | Models, Molecular | Molecular Sequence Data | Substrate Specificity | Crystallography, X-Ray | Nicotinamide-Nucleotide Adenylyltransferase - chemistry | Sequence Homology, Amino Acid | Pseudomonas aeruginosa - metabolism | Protein Binding | Protein Conformation | Catalysis | Kinetics | Binding Sites | Niacinamide | Crystals | Adenine | NAD (Coenzyme) | Universities and colleges | Structure | Niacin
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7. Full Text Identification of the nicotinamide mononucleotide adenylyltransferase of Trypanosoma cruzi
by Niño, Carlos H and Forero-Baena, Nicolás and Contreras, Luis E and Sánchez-Lancheros, Diana and Figarella, Katherine and Ramírez, María H
Memorias do Instituto Oswaldo Cruz, ISSN 0074-0276, 11/2015, Volume 110, Issue 7, pp. 890 - 897
The intracellular parasite Trypanosoma cruzi is the aetiological agent of Chagas disease, a public health concern with an increasing incidence rate. This... 
Chagas disease | Nicotinamide adenine dinucleotide | Nicotinic acid mononucleotide | Nicotinamide mononucleotide | Nicotinamide mononucleotide adenylyltransferase | Trypanosoma cruzi | PROTEIN SECONDARY STRUCTURE | nicotinamide mononucleotide adenylyltransferase | TROPICAL MEDICINE | ACCURACY | nicotinamide adenine dinucleotide | AMINO-ACID-SEQUENCE | METABOLISM | nicotinic acid mononucleotide | PROTOZOAN PARASITES | BIOSYNTHESIS | nicotinamide mononucleotide | EXPRESSION | STRUCTURE PREDICTION | I-TASSER | LEISHMANIA | PARASITOLOGY | Amino Acid Sequence | Sequence Alignment | Nicotinamide-Nucleotide Adenylyltransferase - metabolism | Models, Molecular | Molecular Sequence Data | Nicotinamide-Nucleotide Adenylyltransferase - genetics | Trypanosoma cruzi - enzymology
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8. Full Text Characterization of bacterial NMN deamidase as a Ser/Lys hydrolase expands diversity of serine amidohydrolases
by Sorci, Leonardo and Brunetti, Lucia and Cialabrini, Lucia and Mazzola, Francesca and Kazanov, Marat D and D’Auria, Sabato and Ruggieri, Silverio and Raffaelli, Nadia
FEBS Letters, ISSN 0014-5793, 03/2014, Volume 588, Issue 6, pp. 1016 - 1023
NMN deamidase (PncC) is a bacterial enzyme involved in NAD biosynthesis. We have previously demonstrated that PncC is structurally distinct from other known... 
Amidohydrolase | Pyridine nucleotide | NMN deamidase | Catalytic dyad | Site-directed mutagenesis | nicotinic acid adenine dinucleotide | circular dichroism | NMN | high pressure liquid chromatography | NaMN | NaAD | nicotinic acid mononucleotide | PMSF | phenylmethylsulfonylfluoride | nicotinamide mononucleotide | HPLC | CONVERGENT EVOLUTION | CRYSTAL-STRUCTURE | ACTIVE-SITES | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | DYAD MECHANISM | AMIDASE SIGNATURE ENZYMES | CELL BIOLOGY | BIOPHYSICS | PROTEINS | BINDING | PEPTIDASE | PROTEASE | Amino Acid Sequence | Catalytic Domain | Mutagenesis, Site-Directed | Protein Structure, Secondary | Amidohydrolases - genetics | Enzyme Stability | Models, Molecular | Molecular Sequence Data | Amidohydrolases - chemistry | Sequence Homology, Amino Acid | Apoenzymes - genetics | Apoenzymes - chemistry | Conserved Sequence | Escherichia coli Proteins - genetics | Kinetics | Nicotinamide Mononucleotide - chemistry | Escherichia coli Proteins - chemistry | Amino Acid Substitution | Enzymes | Hydrolases | Analysis | Serine | Index Medicus
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9. Full Text Identification of a nicotinamide/nicotinate mononucleotide adenylyltransferase in Giardia lamblia (GlNMNAT)
by Forero-Baena, Nicolás and Sánchez-Lancheros, Diana and Buitrago, July Constanza and Bustos, Victor and Ramírez-Hernández, María Helena
Biochimie Open, ISSN 2214-0085, 2015, Volume 1, Issue C, pp. 61 - 69
is an intestinal protozoan parasite that causes giardiasis, a disease of high prevalence in Latin America, Asia and Africa. Giardiasis leads to poor absorption... 
NAD metabolism | Giardia lamblia | Enzyme activity | NMNAT
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10. Full Text An Atypical SCF-like Ubiquitin Ligase Complex Promotes Wallerian Degeneration through Regulation of Axonal Nmnat2
by Yamagishi, Yuya and Tessier-Lavigne, Marc
Cell Reports, ISSN 2211-1247, 10/2016, Volume 17, Issue 3, pp. 774 - 782
Axon degeneration is a tightly regulated, self-destructive program that is a critical feature of many neurodegenerative diseases, but the molecular mechanisms... 
neurodegeneration | E3 ubiquitin ligase | Wallerian degeneration | nicotinamide/nicotinic acid mononucleotide adenylyltransferase | ACTIVATION | DEATH PATHWAY | SELF-DESTRUCTION | SYNAPSES | TRIGGERS | IN-VIVO | INJURY | CELL BIOLOGY | Optic Nerve - pathology | Axons - enzymology | Wallerian Degeneration - pathology | Nicotinamide-Nucleotide Adenylyltransferase - metabolism | RNA, Messenger - genetics | Cells, Cultured | Ubiquitin-Protein Ligases - metabolism | RNA, Messenger - metabolism | Retinal Ganglion Cells - metabolism | S-Phase Kinase-Associated Proteins - metabolism | Nicotinamide-Nucleotide Adenylyltransferase - deficiency | Retinal Ganglion Cells - pathology | Animals | Energy Metabolism | Axons - pathology | Mice | Sensory Receptor Cells - metabolism | Wallerian Degeneration - enzymology | Nicotinamide | nicotinic acid mononucleotide adenylyltransferase
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11. Identification, Characterization, and Crystal Structure of Bacillus subtilis Nicotinic Acid Mononucleotide Adenylyltransferase
by Olland, AM and Underwood, KW and Czerwinski, RM and Lo, M and Aulabaugh, A and Bard, J and Stahl, ML and Somers, WS and Sullivan, FX and Chopra, R
Journal of Biological Chemistry, ISSN 0021-9258, 02/2002, Volume 277, Issue 5, pp. 3698 - 3707
The nadD gene, encoding the enzyme nicotinic acid mononucleotide (NaMN) adenylyltransferase (AT), is essential for the synthesis of NAD and subsequent... 
nicotinic acid mononucleotide adenylyltransferase | nadD gene
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12. Full Text Retinal toxicity, in vivo and in vitro, associated with inhibition of nicotinamide phosphoribosyltransferase
by Zabka, Tanja S and Singh, Jatinder and Dhawan, Preeti and Liederer, Bianca M and Oeh, Jason and Kauss, Mara A and Xiao, Yang and Zak, Mark and Lin, Tori and McCray, Bobbi and La, Nghi and Nguyen, Trung and Beyer, Joseph and Farman, Cynthia and Uppal, Hirdesh and Dragovich, Peter S and O'Brien, Thomas and Sampath, Deepak and Misner, Dinah L
Toxicological Sciences, ISSN 1096-6080, 03/2015, Volume 144, Issue 1, pp. 163 - 172
Nicotinamide phosphoribosyltransferase (NAMPT) is a pleiotropic protein with intra-and extra-cellular functions as an enzyme, cytokine, growth factor, and... 
Eye | Pathology | Tumor metabolism | Messenger rna | Nicotinamide adenine dinucleotide | Retinal degeneration | Nicotinic acid mononucleotide | Retinal pigmented epithelial cell culture | retinal degeneration | pathology | ACID | EFFICACY | NAMPT INHIBITORS | DEGENERATION | eye | nicotinamide adenine dinucleotide | LEBER CONGENITAL AMAUROSIS | THERAPY | messenger RNA | nicotinic acid mononucleotide | PATHWAY | BIOSYNTHESIS | TOXICOLOGY | MUTATIONS | retinal pigmented epithelial cell culture | PHASE-I | tumor metabolism | Species Specificity | Nicotinamide-Nucleotide Adenylyltransferase - metabolism | Humans | Male | Structure-Activity Relationship | Nicotinamide Phosphoribosyltransferase - antagonists & inhibitors | Pentosyltransferases - metabolism | RNA, Messenger - metabolism | Niacin - pharmacology | Retinal Pigment Epithelium - pathology | Heterocyclic Compounds, 2-Ring - toxicity | Nicotinamide Phosphoribosyltransferase - metabolism | Enzyme Inhibitors - chemistry | Enzyme Inhibitors - toxicity | Female | Molecular Structure | Cytokines - genetics | Retinal Pigment Epithelium - drug effects | Cell Line | Cell Survival - drug effects | Cytokines - metabolism | Risk Assessment | Sulfones - toxicity | Cyanides - toxicity | Retinal Pigment Epithelium - enzymology | Rats, Sprague-Dawley | Gene Expression Regulation, Enzymologic | Nicotinamide Phosphoribosyltransferase - genetics | Animals | Mice, Nude | Guanidines - toxicity | Cytokines - antagonists & inhibitors | Index Medicus
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13. Full Text Crystal structure of human nicotinic acid phosphoribosyltransferase
by Marletta, Ada Serena and Massarotti, Alberto and Orsomando, Giuseppe and Magni, Giulio and Rizzi, Menico and Garavaglia, Silvia
FEBS Open Bio, ISSN 2211-5463, 2015, Volume 5, Issue 1, pp. 419 - 428
Nicotinic acid phosphoribosyltransferase (EC 2.4.2.11) (NaPRTase) is the rate-limiting enzyme in the three-step Preiss–Handler pathway for the biosynthesis of... 
Phosphoribosyltransferase | Preiss–Handler pathway | Nicotinic Acid | NAD biosynthesis | FK866 | Recycling NAD pathway | Preiss-Handler pathway | CONFORMER GENERATION | ENZYMOLOGY | BIOCHEMISTRY & MOLECULAR BIOLOGY | IDENTIFICATION | MAMMALIAN-CELLS | MOLECULAR-REPLACEMENT | ENZYME | METABOLISM | NAMPT | NIACIN | NADPH | Enzymes | Nicotinic acid | Clinical trials | Homeostasis | Biosynthesis | Roles | Mammals | Gene expression | Metabolism | Kinases | Quinolinate phosphoribosyltransferase | Monomers | NAD | Acids | Nicotinamide phosphoribosyltransferase | Physiology | Nicotinamide | Cancer | Crystal structure
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14. Full Text Structural and Kinetic Characterization of Quinolinate Phosphoribosyltransferase (hQPRTase) from Homo sapiens
by Liu, Huanting and Woznica, Kerry and Catton, Gemma and Crawford, Amanda and Botting, Nigel and Naismith, James H
Journal of Molecular Biology, ISSN 0022-2836, 10/2007, Volume 373, Issue 3, pp. 755 - 763
Human quinolinate phosphoribosyltransferase (EC 2.4.2.19) (hQPRTase) is a member of the type II phosphoribosyltransferase family involved in the catabolism of... 
quinolinic acid | 5-phosphoribosylpyrophosphate | Homo sapiens quinolinate phosphoribosyltransferase | nicotinic acid mononucleotide | NAD biosynthesis | CRYSTALLIZATION | MUSHROOM LENTINUS-EDODES | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | OROTATE PHOSPHORIBOSYLTRANSFERASE | ACID PHOSPHORIBOSYLTRANSFERASE | PURIFICATION | LIVER | RAT-BRAIN | HUNTINGTONS-DISEASE | TRANSFERASE | Pentosyltransferases - genetics | Amino Acid Sequence | Mutagenesis, Site-Directed | Humans | Phosphoribosyl Pyrophosphate - metabolism | Models, Molecular | Molecular Sequence Data | Substrate Specificity | Crystallography, X-Ray | Pentosyltransferases - metabolism | Sequence Homology, Amino Acid | Pentosyltransferases - chemistry | Protein Conformation | Catalysis | Kinetics | Binding Sites | Physiological aspects | Enzymes | Chemical properties | Knowledge-based systems | Niacin | quinolinic acid (QA) | nicotinic acid mononucleotide (NAMN) | Homo sapiens quinolinate phosphoribosyltransferase (hQPRTase) | kinetics | mutagenesis | 5-phosphoribosylpyrophosphate (PRPP)
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15. Full Text Crystallization and preliminary X-ray crystallographic analysis of nicotinic acid mononucleotide adenylyltransferase from Pseudomonas aeruginosa
by Kim, Hye-Lee and Yoon, Hye-Jin and Ha, Jun Yong and Lee, Byung Il and Lee, Hyung Ho and Mikami, Bunzo and Suh, Se Won
Acta Crystallographica Section D, ISSN 0907-4449, 05/2004, Volume 60, Issue 5, pp. 948 - 949
The enzyme nicotinic acid mononucleotide adenylyltransferase (NaMN AT; EC 2.7.7.18) is essential for the synthesis of nicotinamide adenine dinucleotide and is... 
nadD | nicotinamide adenine dinucleotide | Pseudomonas aeruginosa | nicotinic acid mononucleotide adenylyltransferase | nicotinic acid mononucleotide | NAD | BIOPHYSICS | GENE | BACILLUS-SUBTILIS | BIOSYNTHESIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | BIOCHEMICAL RESEARCH METHODS | CRYSTALLOGRAPHY | Recombinant Proteins - metabolism | Amino Acid Sequence | Nicotinamide-Nucleotide Adenylyltransferase - metabolism | Crystallization | Molecular Sequence Data | Recombinant Proteins - chemistry | Crystallography, X-Ray | Nicotinamide-Nucleotide Adenylyltransferase - chemistry | Recombinant Proteins - genetics | Escherichia coli - genetics | Pseudomonas aeruginosa - enzymology | Nicotinamide-Nucleotide Adenylyltransferase - genetics | Protein Conformation
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16. Full Text Cardiotoxicity Associated with Nicotinamide Phosphoribosyltransferase Inhibitors in Rodents and in Rat and Human-Derived Cells Lines
by Misner, D.L and Kauss, M.A and Singh, J and Uppal, H and Bruening-Wright, A and Liederer, B.M and Lin, T and McCray, B and La, N and Nguyen, T and Sampath, D and Dragovich, P.S and O’Brien, T and Zabka, T.S
Cardiovascular Toxicology, ISSN 1530-7905, 07/2017, Volume 17, Issue 3, pp. 307 - 318
Nicotinamide phosphoribosyltransferase (NAMPT) is a pleiotropic protein that functions as an enzyme, cytokine, growth factor and hormone. As a target for... 
Heart | Pathology | Myocardial degeneration | Tumor metabolism | Nicotinamide adenine dinucleotide | Cardiomyocytes | Nicotinic acid mononucleotide | Cardiotoxicity | Impedance | Viability | CARDIAC & CARDIOVASCULAR SYSTEMS | ACID | EFFICACY | VIVO | NAMPT INHIBITORS | FK866 | BIOSYNTHESIS | CHS-828 | TOXICOLOGY | PHASE-I | EXPRESSION | Induced Pluripotent Stem Cells - enzymology | Cytokines - metabolism | Induced Pluripotent Stem Cells - drug effects | Species Specificity | Sulfones - toxicity | Humans | Rats | Embryonic Stem Cells - enzymology | Male | Nicotinamide Phosphoribosyltransferase - antagonists & inhibitors | Rats, Sprague-Dawley | Dose-Response Relationship, Drug | Myocytes, Cardiac - enzymology | Heterocyclic Compounds, 2-Ring - toxicity | Animals | Myocytes, Cardiac - drug effects | Embryonic Stem Cells - drug effects | Nicotinamide Phosphoribosyltransferase - metabolism | Enzyme Inhibitors - toxicity | Female | Cytokines - antagonists & inhibitors | Heart failure | Niacinamide | Purines | Rodents | Physiological aspects | Rankings | Niacin | Cells | NADPH | Energy metabolism | Toxicity | Nicotinic acid | Congestive heart failure | Assaying | Salvage | Biocompatibility | Degeneration | Safety | Inhibition | Effusion | Pharmacology | Thorax | Metabolism | Mitigation | Inhibitors | Nicotinamide phosphoribosyltransferase | Death | In vivo methods and tests | Nicotinamide | In vitro methods and tests | ATP | Adenosine triphosphatase | Index Medicus
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