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    ATCC nadv gene
    Nadv Gene, supplied by ATCC, used in various techniques. Bioz Stars score: 93/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/nadv+gene/Haemophilus+ducreyi+(Neveu-Lamaire)+Bergey+et+al/pmc06095924-155-68-74
    Average 93 stars, based on 11 article reviews
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    Expressing:

    Article Title: β-nicotinamide mononucleotide (NMN) production in Escherichia coli
    Article Snippet: Recombinant Nicotinamide phosphoribosyltransferase (Nampt) gene was cloned in pET-28a(+) expression vector from Novagen which permits protein expression under the control of T7 lac promoter . .. Three such plasmids, carrying expression DNA corresponding to each of the amino acid sequences compared in Fig. were produced as follows: Nampt-PET28a vector containing Nampt gene from Mus musculus strain C57BL/6 J, a gift from dr. Cynthia Wolberger (Addgene plasmid # 25630), was cloned in E . coli DH5α and maintained (as a glycerol stock) at −80 °C. pET28a-hdNadV and pET28a-soNadV plasmids carrying the nucleotide sequence corresponding to nadV gene from Haemophilus ducreyi (strain: ATCC 27722), respectively Shewanella oneidensis (strain: MR-1) were constructed as follows: The gene sequences were selected from the GenBank database (Gene ID: 2716561 respectively 1169740), optimized for expression in E . coli (using Genome Compiler software v. 2.2.55 (Genome Compiler Corporation 2015), considering the frequency of codon usage and GC content, eliminating unwanted restriction sequences), synthesized de novo (GenScript) and ligated into pET-28a(+) vector which was first double digested with NcoI and XhoI restriction enzymes. ..

    Produced:

    Article Title: β-nicotinamide mononucleotide (NMN) production in Escherichia coli
    Article Snippet: Recombinant Nicotinamide phosphoribosyltransferase (Nampt) gene was cloned in pET-28a(+) expression vector from Novagen which permits protein expression under the control of T7 lac promoter . .. Three such plasmids, carrying expression DNA corresponding to each of the amino acid sequences compared in Fig. were produced as follows: Nampt-PET28a vector containing Nampt gene from Mus musculus strain C57BL/6 J, a gift from dr. Cynthia Wolberger (Addgene plasmid # 25630), was cloned in E . coli DH5α and maintained (as a glycerol stock) at −80 °C. pET28a-hdNadV and pET28a-soNadV plasmids carrying the nucleotide sequence corresponding to nadV gene from Haemophilus ducreyi (strain: ATCC 27722), respectively Shewanella oneidensis (strain: MR-1) were constructed as follows: The gene sequences were selected from the GenBank database (Gene ID: 2716561 respectively 1169740), optimized for expression in E . coli (using Genome Compiler software v. 2.2.55 (Genome Compiler Corporation 2015), considering the frequency of codon usage and GC content, eliminating unwanted restriction sequences), synthesized de novo (GenScript) and ligated into pET-28a(+) vector which was first double digested with NcoI and XhoI restriction enzymes. ..

    Plasmid Preparation:

    Article Title: β-nicotinamide mononucleotide (NMN) production in Escherichia coli
    Article Snippet: Recombinant Nicotinamide phosphoribosyltransferase (Nampt) gene was cloned in pET-28a(+) expression vector from Novagen which permits protein expression under the control of T7 lac promoter . .. Three such plasmids, carrying expression DNA corresponding to each of the amino acid sequences compared in Fig. were produced as follows: Nampt-PET28a vector containing Nampt gene from Mus musculus strain C57BL/6 J, a gift from dr. Cynthia Wolberger (Addgene plasmid # 25630), was cloned in E . coli DH5α and maintained (as a glycerol stock) at −80 °C. pET28a-hdNadV and pET28a-soNadV plasmids carrying the nucleotide sequence corresponding to nadV gene from Haemophilus ducreyi (strain: ATCC 27722), respectively Shewanella oneidensis (strain: MR-1) were constructed as follows: The gene sequences were selected from the GenBank database (Gene ID: 2716561 respectively 1169740), optimized for expression in E . coli (using Genome Compiler software v. 2.2.55 (Genome Compiler Corporation 2015), considering the frequency of codon usage and GC content, eliminating unwanted restriction sequences), synthesized de novo (GenScript) and ligated into pET-28a(+) vector which was first double digested with NcoI and XhoI restriction enzymes. ..

    Clone Assay:

    Article Title: β-nicotinamide mononucleotide (NMN) production in Escherichia coli
    Article Snippet: Recombinant Nicotinamide phosphoribosyltransferase (Nampt) gene was cloned in pET-28a(+) expression vector from Novagen which permits protein expression under the control of T7 lac promoter . .. Three such plasmids, carrying expression DNA corresponding to each of the amino acid sequences compared in Fig. were produced as follows: Nampt-PET28a vector containing Nampt gene from Mus musculus strain C57BL/6 J, a gift from dr. Cynthia Wolberger (Addgene plasmid # 25630), was cloned in E . coli DH5α and maintained (as a glycerol stock) at −80 °C. pET28a-hdNadV and pET28a-soNadV plasmids carrying the nucleotide sequence corresponding to nadV gene from Haemophilus ducreyi (strain: ATCC 27722), respectively Shewanella oneidensis (strain: MR-1) were constructed as follows: The gene sequences were selected from the GenBank database (Gene ID: 2716561 respectively 1169740), optimized for expression in E . coli (using Genome Compiler software v. 2.2.55 (Genome Compiler Corporation 2015), considering the frequency of codon usage and GC content, eliminating unwanted restriction sequences), synthesized de novo (GenScript) and ligated into pET-28a(+) vector which was first double digested with NcoI and XhoI restriction enzymes. ..

    Sequencing:

    Article Title: β-nicotinamide mononucleotide (NMN) production in Escherichia coli
    Article Snippet: Recombinant Nicotinamide phosphoribosyltransferase (Nampt) gene was cloned in pET-28a(+) expression vector from Novagen which permits protein expression under the control of T7 lac promoter . .. Three such plasmids, carrying expression DNA corresponding to each of the amino acid sequences compared in Fig. were produced as follows: Nampt-PET28a vector containing Nampt gene from Mus musculus strain C57BL/6 J, a gift from dr. Cynthia Wolberger (Addgene plasmid # 25630), was cloned in E . coli DH5α and maintained (as a glycerol stock) at −80 °C. pET28a-hdNadV and pET28a-soNadV plasmids carrying the nucleotide sequence corresponding to nadV gene from Haemophilus ducreyi (strain: ATCC 27722), respectively Shewanella oneidensis (strain: MR-1) were constructed as follows: The gene sequences were selected from the GenBank database (Gene ID: 2716561 respectively 1169740), optimized for expression in E . coli (using Genome Compiler software v. 2.2.55 (Genome Compiler Corporation 2015), considering the frequency of codon usage and GC content, eliminating unwanted restriction sequences), synthesized de novo (GenScript) and ligated into pET-28a(+) vector which was first double digested with NcoI and XhoI restriction enzymes. ..

    Construct:

    Article Title: β-nicotinamide mononucleotide (NMN) production in Escherichia coli
    Article Snippet: Recombinant Nicotinamide phosphoribosyltransferase (Nampt) gene was cloned in pET-28a(+) expression vector from Novagen which permits protein expression under the control of T7 lac promoter . .. Three such plasmids, carrying expression DNA corresponding to each of the amino acid sequences compared in Fig. were produced as follows: Nampt-PET28a vector containing Nampt gene from Mus musculus strain C57BL/6 J, a gift from dr. Cynthia Wolberger (Addgene plasmid # 25630), was cloned in E . coli DH5α and maintained (as a glycerol stock) at −80 °C. pET28a-hdNadV and pET28a-soNadV plasmids carrying the nucleotide sequence corresponding to nadV gene from Haemophilus ducreyi (strain: ATCC 27722), respectively Shewanella oneidensis (strain: MR-1) were constructed as follows: The gene sequences were selected from the GenBank database (Gene ID: 2716561 respectively 1169740), optimized for expression in E . coli (using Genome Compiler software v. 2.2.55 (Genome Compiler Corporation 2015), considering the frequency of codon usage and GC content, eliminating unwanted restriction sequences), synthesized de novo (GenScript) and ligated into pET-28a(+) vector which was first double digested with NcoI and XhoI restriction enzymes. ..

    Software:

    Article Title: β-nicotinamide mononucleotide (NMN) production in Escherichia coli
    Article Snippet: Recombinant Nicotinamide phosphoribosyltransferase (Nampt) gene was cloned in pET-28a(+) expression vector from Novagen which permits protein expression under the control of T7 lac promoter . .. Three such plasmids, carrying expression DNA corresponding to each of the amino acid sequences compared in Fig. were produced as follows: Nampt-PET28a vector containing Nampt gene from Mus musculus strain C57BL/6 J, a gift from dr. Cynthia Wolberger (Addgene plasmid # 25630), was cloned in E . coli DH5α and maintained (as a glycerol stock) at −80 °C. pET28a-hdNadV and pET28a-soNadV plasmids carrying the nucleotide sequence corresponding to nadV gene from Haemophilus ducreyi (strain: ATCC 27722), respectively Shewanella oneidensis (strain: MR-1) were constructed as follows: The gene sequences were selected from the GenBank database (Gene ID: 2716561 respectively 1169740), optimized for expression in E . coli (using Genome Compiler software v. 2.2.55 (Genome Compiler Corporation 2015), considering the frequency of codon usage and GC content, eliminating unwanted restriction sequences), synthesized de novo (GenScript) and ligated into pET-28a(+) vector which was first double digested with NcoI and XhoI restriction enzymes. ..

    Synthesized:

    Article Title: β-nicotinamide mononucleotide (NMN) production in Escherichia coli
    Article Snippet: Recombinant Nicotinamide phosphoribosyltransferase (Nampt) gene was cloned in pET-28a(+) expression vector from Novagen which permits protein expression under the control of T7 lac promoter . .. Three such plasmids, carrying expression DNA corresponding to each of the amino acid sequences compared in Fig. were produced as follows: Nampt-PET28a vector containing Nampt gene from Mus musculus strain C57BL/6 J, a gift from dr. Cynthia Wolberger (Addgene plasmid # 25630), was cloned in E . coli DH5α and maintained (as a glycerol stock) at −80 °C. pET28a-hdNadV and pET28a-soNadV plasmids carrying the nucleotide sequence corresponding to nadV gene from Haemophilus ducreyi (strain: ATCC 27722), respectively Shewanella oneidensis (strain: MR-1) were constructed as follows: The gene sequences were selected from the GenBank database (Gene ID: 2716561 respectively 1169740), optimized for expression in E . coli (using Genome Compiler software v. 2.2.55 (Genome Compiler Corporation 2015), considering the frequency of codon usage and GC content, eliminating unwanted restriction sequences), synthesized de novo (GenScript) and ligated into pET-28a(+) vector which was first double digested with NcoI and XhoI restriction enzymes. ..



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    Production pathway and precursors of NMN in <t>L.</t> <t>reuteri</t> JCM 1112 T . ( A ) Putative NMN production pathway in bacteria ( , ). FtNadE: NMN synthase of Francisella tularensis ; MazG: nucleoside triphosphate pyrophosphohydrolase; NadC: quinolinate phosphoribosyl transferase; NadD: NAMN adenylyl transferase; NadE: NAD⁺ synthetase; <t>NadV:</t> NAM phosphoribosyl transferase (NAMPT); NudE: NADH hydrolase; PncA: nicotinamidase; PncB: nicotinic acid phosphoribosyl transferase; UshA: UDP-sugar hydrolase. Dotted lines from Asp and Trp to quinolinic acid represent multiple reactions. ( B–F ) Production of labeled NMN by L. reuteri JCM 1112 T in MRS broth supplemented with 13 C 6 -NA ( B ), 13 C 6 -NAM ( C ), 13 C 5 -NAD + ( D ), 13 C 4 - 15 N-Asp ( E ), or 13 C - 15 N 2 -Trp ( F ). The cultivation time was 12 h. The blank bars represent the percentages of labeled compounds (with respect to the total of labeled and unlabeled compounds) at the start of cultivation. The gray bars represent the percentages of labeled NMN (with respect to the total of labeled and unlabeled NMN) in the culture supernatants. The percentages of labeled NA, NAM, and NAD + were calculated from the peak areas of each compound. The percentages of labeled Trp and Asp were calculated based on their respective concentrations of added labeled compounds and the unlabeled concentrations originally present in the MRS broth. ( G ) NMN concentrations in the supernatants of MRS broth cultures of L. reuteri JCM 1112 T supplemented with 5,000 ng/mL of NAD + (7.5 µmol/L), NAM (41 µmol/L), or NA (41 µmol/L). The data are expressed as fold changes in NMN production relative to the unsupplemented MRS broth culture (Control). The cultivation time was 12 h. The bars represent the mean values, and the error bars indicate the standard deviation calculated from triplicates. One-way ANOVA showed a significant treatment effect ( F (3,8) = 570, P < 0.0001). Dunnett’s test was then performed using unsupplemented MRS broth culture as the control; *** P < 0.001 versus control; ns = not significant.
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    Production pathway and precursors of NMN in <t>L.</t> <t>reuteri</t> JCM 1112 T . ( A ) Putative NMN production pathway in bacteria ( , ). FtNadE: NMN synthase of Francisella tularensis ; MazG: nucleoside triphosphate pyrophosphohydrolase; NadC: quinolinate phosphoribosyl transferase; NadD: NAMN adenylyl transferase; NadE: NAD⁺ synthetase; <t>NadV:</t> NAM phosphoribosyl transferase (NAMPT); NudE: NADH hydrolase; PncA: nicotinamidase; PncB: nicotinic acid phosphoribosyl transferase; UshA: UDP-sugar hydrolase. Dotted lines from Asp and Trp to quinolinic acid represent multiple reactions. ( B–F ) Production of labeled NMN by L. reuteri JCM 1112 T in MRS broth supplemented with 13 C 6 -NA ( B ), 13 C 6 -NAM ( C ), 13 C 5 -NAD + ( D ), 13 C 4 - 15 N-Asp ( E ), or 13 C - 15 N 2 -Trp ( F ). The cultivation time was 12 h. The blank bars represent the percentages of labeled compounds (with respect to the total of labeled and unlabeled compounds) at the start of cultivation. The gray bars represent the percentages of labeled NMN (with respect to the total of labeled and unlabeled NMN) in the culture supernatants. The percentages of labeled NA, NAM, and NAD + were calculated from the peak areas of each compound. The percentages of labeled Trp and Asp were calculated based on their respective concentrations of added labeled compounds and the unlabeled concentrations originally present in the MRS broth. ( G ) NMN concentrations in the supernatants of MRS broth cultures of L. reuteri JCM 1112 T supplemented with 5,000 ng/mL of NAD + (7.5 µmol/L), NAM (41 µmol/L), or NA (41 µmol/L). The data are expressed as fold changes in NMN production relative to the unsupplemented MRS broth culture (Control). The cultivation time was 12 h. The bars represent the mean values, and the error bars indicate the standard deviation calculated from triplicates. One-way ANOVA showed a significant treatment effect ( F (3,8) = 570, P < 0.0001). Dunnett’s test was then performed using unsupplemented MRS broth culture as the control; *** P < 0.001 versus control; ns = not significant.
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    Image Search Results


    Production pathway and precursors of NMN in L. reuteri JCM 1112 T . ( A ) Putative NMN production pathway in bacteria ( , ). FtNadE: NMN synthase of Francisella tularensis ; MazG: nucleoside triphosphate pyrophosphohydrolase; NadC: quinolinate phosphoribosyl transferase; NadD: NAMN adenylyl transferase; NadE: NAD⁺ synthetase; NadV: NAM phosphoribosyl transferase (NAMPT); NudE: NADH hydrolase; PncA: nicotinamidase; PncB: nicotinic acid phosphoribosyl transferase; UshA: UDP-sugar hydrolase. Dotted lines from Asp and Trp to quinolinic acid represent multiple reactions. ( B–F ) Production of labeled NMN by L. reuteri JCM 1112 T in MRS broth supplemented with 13 C 6 -NA ( B ), 13 C 6 -NAM ( C ), 13 C 5 -NAD + ( D ), 13 C 4 - 15 N-Asp ( E ), or 13 C - 15 N 2 -Trp ( F ). The cultivation time was 12 h. The blank bars represent the percentages of labeled compounds (with respect to the total of labeled and unlabeled compounds) at the start of cultivation. The gray bars represent the percentages of labeled NMN (with respect to the total of labeled and unlabeled NMN) in the culture supernatants. The percentages of labeled NA, NAM, and NAD + were calculated from the peak areas of each compound. The percentages of labeled Trp and Asp were calculated based on their respective concentrations of added labeled compounds and the unlabeled concentrations originally present in the MRS broth. ( G ) NMN concentrations in the supernatants of MRS broth cultures of L. reuteri JCM 1112 T supplemented with 5,000 ng/mL of NAD + (7.5 µmol/L), NAM (41 µmol/L), or NA (41 µmol/L). The data are expressed as fold changes in NMN production relative to the unsupplemented MRS broth culture (Control). The cultivation time was 12 h. The bars represent the mean values, and the error bars indicate the standard deviation calculated from triplicates. One-way ANOVA showed a significant treatment effect ( F (3,8) = 570, P < 0.0001). Dunnett’s test was then performed using unsupplemented MRS broth culture as the control; *** P < 0.001 versus control; ns = not significant.

    Journal: Microbiology Spectrum

    Article Title: Nicotinamide mononucleotide production by non-recombinant Limosilactobacillus reuteri and nicotinamide adenine dinucleotide synthesizing lactic acid bacteria

    doi: 10.1128/spectrum.00333-25

    Figure Lengend Snippet: Production pathway and precursors of NMN in L. reuteri JCM 1112 T . ( A ) Putative NMN production pathway in bacteria ( , ). FtNadE: NMN synthase of Francisella tularensis ; MazG: nucleoside triphosphate pyrophosphohydrolase; NadC: quinolinate phosphoribosyl transferase; NadD: NAMN adenylyl transferase; NadE: NAD⁺ synthetase; NadV: NAM phosphoribosyl transferase (NAMPT); NudE: NADH hydrolase; PncA: nicotinamidase; PncB: nicotinic acid phosphoribosyl transferase; UshA: UDP-sugar hydrolase. Dotted lines from Asp and Trp to quinolinic acid represent multiple reactions. ( B–F ) Production of labeled NMN by L. reuteri JCM 1112 T in MRS broth supplemented with 13 C 6 -NA ( B ), 13 C 6 -NAM ( C ), 13 C 5 -NAD + ( D ), 13 C 4 - 15 N-Asp ( E ), or 13 C - 15 N 2 -Trp ( F ). The cultivation time was 12 h. The blank bars represent the percentages of labeled compounds (with respect to the total of labeled and unlabeled compounds) at the start of cultivation. The gray bars represent the percentages of labeled NMN (with respect to the total of labeled and unlabeled NMN) in the culture supernatants. The percentages of labeled NA, NAM, and NAD + were calculated from the peak areas of each compound. The percentages of labeled Trp and Asp were calculated based on their respective concentrations of added labeled compounds and the unlabeled concentrations originally present in the MRS broth. ( G ) NMN concentrations in the supernatants of MRS broth cultures of L. reuteri JCM 1112 T supplemented with 5,000 ng/mL of NAD + (7.5 µmol/L), NAM (41 µmol/L), or NA (41 µmol/L). The data are expressed as fold changes in NMN production relative to the unsupplemented MRS broth culture (Control). The cultivation time was 12 h. The bars represent the mean values, and the error bars indicate the standard deviation calculated from triplicates. One-way ANOVA showed a significant treatment effect ( F (3,8) = 570, P < 0.0001). Dunnett’s test was then performed using unsupplemented MRS broth culture as the control; *** P < 0.001 versus control; ns = not significant.

    Article Snippet: We could not identify the nadV gene in the L. reuteri genome by a search using L. reuteri and nadV as keywords in the database of the National Center for Biotechnology Information (NCBI Gene, https://www.ncbi.nlm.nih.gov/gene , accessed November 2024).

    Techniques: Bacteria, Labeling, Control, Standard Deviation