Nicotinamide Riboside Kinase Structures Reveal New Pathways to NAD+
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{"title"=>"Nicotinamide riboside kinase structures reveal new pathways to NAD+", "type"=>"journal", "authors"=>[{"first_name"=>"Wolfram", "last_name"=>"Tempel", "scopus_author_id"=>"8557158400"}, {"first_name"=>"Wael M.", "last_name"=>"Rabeh", "scopus_author_id"=>"8279664700"}, {"first_name"=>"Katrina L.", "last_name"=>"Bogan", "scopus_author_id"=>"15755042000"}, {"first_name"=>"Peter", "last_name"=>"Belenky", "scopus_author_id"=>"15755453000"}, {"first_name"=>"Marzena", "last_name"=>"Wojcik", "scopus_author_id"=>"7102148990"}, {"first_name"=>"Heather F.", "last_name"=>"Seidle", "scopus_author_id"=>"8603893400"}, {"first_name"=>"Lyudmila", "last_name"=>"Nedyalkova", "scopus_author_id"=>"22951390100"}, {"first_name"=>"Tianle", "last_name"=>"Yang", "scopus_author_id"=>"14030843200"}, {"first_name"=>"Anthony A.", "last_name"=>"Sauve", "scopus_author_id"=>"6603026242"}, {"first_name"=>"Hee Won", "last_name"=>"Park", "scopus_author_id"=>"7601568314"}, {"first_name"=>"Charles", "last_name"=>"Brenner", "scopus_author_id"=>"56324992800"}], "year"=>2007, "source"=>"PLoS Biology", "identifiers"=>{"scopus"=>"2-s2.0-35648939287", "sgr"=>"35648939287", "issn"=>"15449173", "doi"=>"10.1371/journal.pbio.0050263", "pmid"=>"17914902", "isbn"=>"1545-7885 (Electronic)\\r1544-9173 (Linking)", "pui"=>"350035424"}, "id"=>"a819ca1f-e0e7-31a6-b401-554ce797a708", "abstract"=>"The eukaryotic nicotinamide riboside kinase (Nrk) pathway, which is induced in response to nerve damage and promotes replicative life span in yeast, converts nicotinamide riboside to nicotinamide adenine dinucleotide (NAD+) by phosphorylation and adenylylation. Crystal structures of human Nrk1 bound to nucleoside and nucleotide substrates and products revealed an enzyme structurally similar to Rossmann fold metabolite kinases and allowed the identification of active site residues, which were shown to be essential for human Nrk1 and Nrk2 activity in vivo. Although the structures account for the 500-fold discrimination between nicotinamide riboside and pyrimidine nucleosides, no enzyme feature was identified to recognize the distinctive carboxamide group of nicotinamide riboside. Indeed, nicotinic acid riboside is a specific substrate of human Nrk enzymes and is utilized in yeast in a novel biosynthetic pathway that depends on Nrk and NAD+ synthetase. Additionally, nicotinic acid riboside is utilized in vivo by Urh1, Pnp1, and Preiss-Handler salvage. Thus, crystal structures of Nrk1 led to the identification of new pathways to NAD+.", "link"=>"http://www.mendeley.com/research/nicotinamide-riboside-kinase-structures-reveal-new-pathways-nad", "reader_count"=>67, "reader_count_by_academic_status"=>{"Unspecified"=>2, "Professor > Associate Professor"=>2, "Researcher"=>22, "Student > Ph. D. Student"=>18, "Student > Postgraduate"=>4, "Other"=>2, "Student > Master"=>6, "Student > Bachelor"=>7, "Professor"=>4}, "reader_count_by_user_role"=>{"Unspecified"=>2, "Professor > Associate Professor"=>2, "Researcher"=>22, "Student > Ph. D. Student"=>18, "Student > Postgraduate"=>4, "Other"=>2, "Student > Master"=>6, "Student > Bachelor"=>7, "Professor"=>4}, "reader_count_by_subject_area"=>{"Unspecified"=>3, "Biochemistry, Genetics and Molecular Biology"=>10, "Agricultural and Biological Sciences"=>34, "Medicine and Dentistry"=>6, "Neuroscience"=>2, "Sports and Recreations"=>1, "Pharmacology, Toxicology and Pharmaceutical Science"=>2, "Physics and Astronomy"=>1, "Chemical Engineering"=>1, "Chemistry"=>6, "Computer Science"=>1}, "reader_count_by_subdiscipline"=>{"Medicine and Dentistry"=>{"Medicine and Dentistry"=>6}, "Neuroscience"=>{"Neuroscience"=>2}, "Chemistry"=>{"Chemistry"=>6}, "Sports and Recreations"=>{"Sports and Recreations"=>1}, "Physics and Astronomy"=>{"Physics and Astronomy"=>1}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>34}, "Computer Science"=>{"Computer Science"=>1}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>10}, "Unspecified"=>{"Unspecified"=>3}, "Pharmacology, Toxicology and Pharmaceutical Science"=>{"Pharmacology, Toxicology and Pharmaceutical Science"=>2}, "Chemical Engineering"=>{"Chemical Engineering"=>1}}, "reader_count_by_country"=>{"Belgium"=>1, "United States"=>2, "Serbia and Montenegro"=>1, "Brazil"=>1, "France"=>1, "Switzerland"=>1}, "group_count"=>5}

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/943815"], "description"=>"<p>Stereo diagrams of Nrk1 are provided in a consistent orientation using the main chain backbone colors from <a href=\"http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.0050263#pbio-0050263-g001\" target=\"_blank\">Figure 1</a>A. (A) ADP•Mg<sup>2</sup> product complex with the corresponding difference electron density map, contoured at 3.0 Å. (B) NR substrate complex. (C) Bisubstrate analog complex of AppNHp•Mg<sup>2</sup> plus NR. (D) NMN product complex.</p>", "links"=>[], "tags"=>["nucleotide"], "article_id"=>614208, "categories"=>["Biochemistry", "Medicine", "Genetics", "Cell Biology"], "users"=>["Wolfram Tempel", "Wael M Rabeh", "Katrina L Bogan", "Peter Belenky", "Marzena Wojcik", "Heather F Seidle", "Lyudmila Nedyalkova", "Tianle Yang", "Anthony A Sauve", "Hee-Won Park", "Charles Brenner"], "doi"=>"https://dx.doi.org/10.1371/journal.pbio.0050263.g002", "stats"=>{"downloads"=>1, "page_views"=>2, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Nucleoside_and_Nucleotide_Recognition_by_Nrk1_/614208", "title"=>"Nucleoside and Nucleotide Recognition by Nrk1", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2007-10-02 01:10:08"}
  • {"files"=>["https://ndownloader.figshare.com/files/943916"], "description"=>"<p>The conserved carboxylates of human Nrk1, Asp36 and Glu98, and the corresponding carboxylates of Nrk2 are required for biological activity in yeast.</p>", "links"=>[], "tags"=>["nrk1"], "article_id"=>614306, "categories"=>["Biochemistry", "Medicine", "Genetics", "Cell Biology"], "users"=>["Wolfram Tempel", "Wael M Rabeh", "Katrina L Bogan", "Peter Belenky", "Marzena Wojcik", "Heather F Seidle", "Lyudmila Nedyalkova", "Tianle Yang", "Anthony A Sauve", "Hee-Won Park", "Charles Brenner"], "doi"=>"https://dx.doi.org/10.1371/journal.pbio.0050263.g003", "stats"=>{"downloads"=>4, "page_views"=>3, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Active_Site_Requirement_of_Nrk1_and_Nrk2_/614306", "title"=>"Active Site Requirement of Nrk1 and Nrk2", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2007-10-02 01:11:46"}
  • {"files"=>["https://ndownloader.figshare.com/files/943993"], "description"=>"<p>In stereo, the 2- and 4-oxy functions (black) of a hypothetical uridine substrate are shown superimposed onto NR coordinates in the Nrk1 NR co-crystal structure. At a distance of 2.55 Å, the 4 oxygen would be in van der Waals conflict with the carbonyl oxygen of Gln135, which is in a <i>cis</i> peptide linkage with Pro136.</p>", "links"=>[], "tags"=>["Biochemistry", "cell biology", "genetics and genomics", "nutrition"], "article_id"=>614377, "categories"=>["Biochemistry", "Medicine", "Genetics", "Cell Biology"], "users"=>["Wolfram Tempel", "Wael M Rabeh", "Katrina L Bogan", "Peter Belenky", "Marzena Wojcik", "Heather F Seidle", "Lyudmila Nedyalkova", "Tianle Yang", "Anthony A Sauve", "Hee-Won Park", "Charles Brenner"], "doi"=>"https://dx.doi.org/10.1371/journal.pbio.0050263.g004", "stats"=>{"downloads"=>1, "page_views"=>11, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_NR_Uridine_Discrimination_by_Nrk1_/614377", "title"=>"NR/Uridine Discrimination by Nrk1", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2007-10-02 01:12:57"}
  • {"files"=>["https://ndownloader.figshare.com/files/465024"], "description"=>"<div><p>The eukaryotic nicotinamide riboside kinase (Nrk) pathway, which is induced in response to nerve damage and promotes replicative life span in yeast, converts nicotinamide riboside to nicotinamide adenine dinucleotide (NAD<sup>+</sup>) by phosphorylation and adenylylation. Crystal structures of human Nrk1 bound to nucleoside and nucleotide substrates and products revealed an enzyme structurally similar to Rossmann fold metabolite kinases and allowed the identification of active site residues, which were shown to be essential for human Nrk1 and Nrk2 activity in vivo. Although the structures account for the 500-fold discrimination between nicotinamide riboside and pyrimidine nucleosides, no enzyme feature was identified to recognize the distinctive carboxamide group of nicotinamide riboside. Indeed, nicotinic acid riboside is a specific substrate of human Nrk enzymes and is utilized in yeast in a novel biosynthetic pathway that depends on Nrk and NAD<sup>+</sup> synthetase. Additionally, nicotinic acid riboside is utilized in vivo by Urh1, Pnp1, and Preiss-Handler salvage. Thus, crystal structures of Nrk1 led to the identification of new pathways to NAD<sup>+</sup>.</p> </div>", "links"=>[], "tags"=>["nicotinamide", "riboside", "kinase", "structures", "pathways"], "article_id"=>151658, "categories"=>["Biochemistry", "Medicine", "Genetics", "Cell Biology"], "users"=>["Wolfram Tempel", "Wael M Rabeh", "Katrina L Bogan", "Peter Belenky", "Marzena Wojcik", "Heather F Seidle", "Lyudmila Nedyalkova", "Tianle Yang", "Anthony A Sauve", "Hee-Won Park", "Charles Brenner"], "doi"=>"https://dx.doi.org/10.1371/journal.pbio.0050263", "stats"=>{"downloads"=>5, "page_views"=>45, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/Nicotinamide_Riboside_Kinase_Structures_Reveal_New_Pathways_to_NAD_/151658", "title"=>"Nicotinamide Riboside Kinase Structures Reveal New Pathways to NAD<sup>+</sup>", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2007-10-02 00:27:38"}
  • {"files"=>["https://ndownloader.figshare.com/files/944259"], "description"=>"<p>Previously reported NAD<sup>+</sup> metabolic pathways are shown in black[<a href=\"http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.0050263#pbio-0050263-b015\" target=\"_blank\">15</a>]. In blue and green, respectively, are Nrk1-dependent and Nrk1-independent routes from NaR to NaMN.</p>", "links"=>[], "tags"=>["metabolism", "pathways"], "article_id"=>614639, "categories"=>["Biochemistry", "Medicine", "Genetics", "Cell Biology"], "users"=>["Wolfram Tempel", "Wael M Rabeh", "Katrina L Bogan", "Peter Belenky", "Marzena Wojcik", "Heather F Seidle", "Lyudmila Nedyalkova", "Tianle Yang", "Anthony A Sauve", "Hee-Won Park", "Charles Brenner"], "doi"=>"https://dx.doi.org/10.1371/journal.pbio.0050263.g007", "stats"=>{"downloads"=>1, "page_views"=>16, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_NAD_Metabolism_in_Yeast_Two_New_Pathways_to_NaMN_/614639", "title"=>"NAD<sup>+</sup> Metabolism in Yeast: Two New Pathways to NaMN", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2007-10-02 01:17:19"}
  • {"files"=>["https://ndownloader.figshare.com/files/944092"], "description"=>"<p>(A) Coordinates of tiazofurin, in yellow, are superimposed with those of NR in isomorphous crystal structures. The sulfur atom of tiazofurin was localized by the 3 Å anomalous difference Fourier map, contoured in purple at 2.7 Å. (B) A surface representation of the Nam binding-site of NR reveals no specific recognition of the carboxamide group, which is exposed to solvent.</p>", "links"=>[], "tags"=>["tiazofurin"], "article_id"=>614481, "categories"=>["Biochemistry", "Medicine", "Genetics", "Cell Biology"], "users"=>["Wolfram Tempel", "Wael M Rabeh", "Katrina L Bogan", "Peter Belenky", "Marzena Wojcik", "Heather F Seidle", "Lyudmila Nedyalkova", "Tianle Yang", "Anthony A Sauve", "Hee-Won Park", "Charles Brenner"], "doi"=>"https://dx.doi.org/10.1371/journal.pbio.0050263.g005", "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_NR_and_Tiazofurin_Recognition_by_Nrk1_/614481", "title"=>"NR and Tiazofurin Recognition by Nrk1", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2007-10-02 01:14:41"}
  • {"files"=>["https://ndownloader.figshare.com/files/944170"], "description"=>"<p>In (A), the vitamin requirement of de novo mutant <i>bna1</i> and glutamine-dependent NAD<sup>+</sup> synthetase mutant <i>qns1</i> is illustrated. The fact that <i>bna1</i>, <i>bna1 nrk1</i>, <i>bna1 npt1</i>, <i>and qns1</i> strains are satisfied by addition of NR is shown in (B). In (C), the vitamin activity of NaR is demonstrated for the de novo mutant <i>bna1</i>, even when either the Nrk pathway or the Preiss-Handler pathway is mutationally inactivated by <i>nrk1</i> or <i>npt1</i> mutation, respectively. Establishing the uniqueness of NaR as a vitamin, NaR fails to support the growth of <i>qns1</i>. In (D), the intracellular NAD<sup>+</sup> concentration is calculated for wild-type, <i>npt1</i>, <i>nrk1</i>, <i>urh1 pnp1</i>, and <i>nrk1 urh1 pnp1</i> mutants in vitamin-free (gray bars) and in vitamin-free media supplemented with 10 μM NaR (black bars). The unique lack of utilization by the <i>nrk1 urh1 pnp1</i> strain shows that NaR makes use of Nrk1, Urh1, and Pnp1 for conversion to NAD<sup>+</sup>.</p>", "links"=>[], "tags"=>["Biochemistry", "cell biology", "genetics and genomics", "nutrition"], "article_id"=>614548, "categories"=>["Biochemistry", "Medicine", "Genetics", "Cell Biology"], "users"=>["Wolfram Tempel", "Wael M Rabeh", "Katrina L Bogan", "Peter Belenky", "Marzena Wojcik", "Heather F Seidle", "Lyudmila Nedyalkova", "Tianle Yang", "Anthony A Sauve", "Hee-Won Park", "Charles Brenner"], "doi"=>"https://dx.doi.org/10.1371/journal.pbio.0050263.g006", "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_NaR_Utilization_In_Vivo_/614548", "title"=>"NaR Utilization In Vivo", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2007-10-02 01:15:48"}
  • {"files"=>["https://ndownloader.figshare.com/files/943687"], "description"=>"<p>(A) Ribbon diagram of Nrk1 bound to ADP with rainbow coloring from the N terminus (violet) to the C terminus (red). Helices A through E, strands 1 through 5, and the lid domain are indicated. (B) Structural superposition of Nrk1 (blue) with human Uck2 (red).</p>", "links"=>[], "tags"=>["rossmann", "metabolite"], "article_id"=>614075, "categories"=>["Biochemistry", "Medicine", "Genetics", "Cell Biology"], "users"=>["Wolfram Tempel", "Wael M Rabeh", "Katrina L Bogan", "Peter Belenky", "Marzena Wojcik", "Heather F Seidle", "Lyudmila Nedyalkova", "Tianle Yang", "Anthony A Sauve", "Hee-Won Park", "Charles Brenner"], "doi"=>"https://dx.doi.org/10.1371/journal.pbio.0050263.g001", "stats"=>{"downloads"=>1, "page_views"=>5, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Nrk1_Is_a_Rossmann_Fold_Metabolite_Kinase_/614075", "title"=>"Nrk1 Is a Rossmann Fold Metabolite Kinase", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2007-10-02 01:07:55"}

PMC Usage Stats | Further Information

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Relative Metric

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