Page last updated: 2024-08-17

nad and propionaldehyde

nad has been researched along with propionaldehyde in 26 studies

Research

Studies (26)

TimeframeStudies, this research(%)All Research%
pre-19908 (30.77)18.7374
1990's8 (30.77)18.2507
2000's3 (11.54)29.6817
2010's6 (23.08)24.3611
2020's1 (3.85)2.80

Authors

AuthorsStudies
Blackwell, LF; Buckley, PD; Hill, JP; Kingston, RL; Sime, RM1
Abriola, DP; Blatter, EE; Pietruszko, R1
Blackwell, LF; Buckley, PD; Hill, JP; Motion, RL2
Marselos, M; Vasiliou, V1
Marselos, M; Michalopoulos, G; Strom, SC1
Blackwell, LF; Buckley, PD; Hardman, MJ; MacGibbon, AK; Motion, RL1
Bennett, AF; Blackwell, LF; Buckley, PD; Deady, LW1
Bennett, AF; Blackwell, LF; Buckley, PD2
Blackwell, LF; Buckley, PD; Motion, RL1
Bennett, AF; Blackwell, LF; Buckley, PD; Crow, KE; Deady, LW1
Dickinson, FM; Hart, GJ1
Bennett, AF; Blackwell, LF; Buckley, PD; Hill, JP; Motion, RL1
Anderson, BM; Leskovac, V; Stancić, B; Trivić, S; Zeremski, J1
Hwang, S; Kim, CK; Kim, SJ; Kim, Y; Kim, YC1
Allali-Hassani, A; Weiner, H1
Barber, AR; Pamment, NB; Vriesekoop, F1
Deerfield, DW; Hempel, J; Wymore, T1
Baek, JO; Heo, SY; Hong, WK; Kim, CH; Kim, DH; Luo, LH; Oh, BR; Seo, JW1
Huang, HC; Huang, ST; Lin, CM; Lin, HY; Wang, KL1
Branlant, G; Stines-Chaumeil, C; Talfournier, F1
Asiimwe, T; Kothe, E; Krause, K; Schlunk, I1
Hatti-Kaul, R; Linares-Pastén, JA; Sabet-Azad, R; Sardari, RR; Torkelson, L1
Bobik, TA; Chowdhury, C1
Chowdhury, NP; Moon, J; Müller, V1

Other Studies

26 other study(ies) available for nad and propionaldehyde

ArticleYear
Activation of aldehyde dehydrogenase at physiological temperatures.
    Biochemical pharmacology, 1992, Dec-15, Volume: 44, Issue:12

    Topics: Aldehyde Dehydrogenase; Aldehydes; Animals; Body Temperature; Cytosol; Enzyme Activation; Liver; NAD; Sheep

1992
Aldehyde dehydrogenase. Covalent intermediate in aldehyde dehydrogenation and ester hydrolysis.
    The Biochemical journal, 1992, Mar-01, Volume: 282 ( Pt 2)

    Topics: Alcohol Dehydrogenase; Aldehydes; Amino Acid Sequence; Catalysis; Chloral Hydrate; Chromatography, Liquid; Cinnamates; Esters; Humans; Hydrolysis; Imidazoles; Isoenzymes; Kinetics; Molecular Sequence Data; NAD; Nitrophenols; Substrate Specificity

1992
Steady-state and pre-steady-state kinetics of propionaldehyde oxidation by sheep liver cytosolic aldehyde dehydrogenase at pH 5.2. Evidence that the release of NADH remains rate-limiting in the enzyme mechanism at acid pH values.
    Biochemistry, 1991, Feb-05, Volume: 30, Issue:5

    Topics: Aldehyde Dehydrogenase; Aldehydes; Animals; Cytosol; Hydrogen-Ion Concentration; In Vitro Techniques; Kinetics; Liver; NAD; Osmolar Concentration; Sheep; Spectrometry, Fluorescence

1991
Effect of various chemicals on the aldehyde dehydrogenase activity of the rat liver cytosol.
    Chemico-biological interactions, 1991, Volume: 79, Issue:1

    Topics: Aldehyde Dehydrogenase; Aldehydes; Amines; Animals; Benzaldehydes; Carcinogens; Cytosol; Liver; NAD; NADP; Nitrosamines; Oxidation-Reduction; Polycyclic Compounds; Rats; Rats, Inbred Strains; Structure-Activity Relationship

1991
Effect of phenobarbital and 3-methylcholanthrene on aldehyde dehydrogenase activity in cultures of HepG2 cells and normal human hepatocytes.
    Chemico-biological interactions, 1987, Volume: 62, Issue:1

    Topics: Aldehyde Dehydrogenase; Aldehydes; Benzaldehydes; Carcinoma, Hepatocellular; Cells, Cultured; Liver; Liver Neoplasms; Methylcholanthrene; NAD; Neoplasm Proteins; Phenobarbital; Substrate Specificity

1987
Evidence that the slow conformation change controlling NADH release from the enzyme is rate-limiting during the oxidation of propionaldehyde by aldehyde dehydrogenase.
    The Biochemical journal, 1987, Mar-15, Volume: 242, Issue:3

    Topics: Aldehyde Dehydrogenase; Aldehydes; Binding Sites; Catalysis; Hydrogen-Ion Concentration; Kinetics; Macromolecular Substances; NAD; Oxidation-Reduction; Protein Conformation

1987
Kinetics of inhibition and hysteresis of sheep liver cytoplasmic aldehyde dehydrogenase with glyoxylic acid: further evidence relating to the two-site model for aldehyde oxidation.
    Archives of biochemistry and biophysics, 1985, Volume: 243, Issue:2

    Topics: Aldehyde Dehydrogenase; Aldehydes; Animals; Binding Sites; Cytoplasm; Glyoxylates; Hydrogen-Ion Concentration; Kinetics; Liver; Models, Chemical; NAD; Oxidation-Reduction; Sheep; Spectrometry, Fluorescence

1985
Proton release during the pre-steady-state oxidation of aldehydes by aldehyde dehydrogenase. Evidence for a rate-limiting conformational change.
    Biochemistry, 1982, Aug-31, Volume: 21, Issue:18

    Topics: Acetaldehyde; Aldehyde Dehydrogenase; Aldehyde Oxidoreductases; Aldehydes; Benzaldehydes; Hydrogen-Ion Concentration; Kinetics; NAD; Oxidation-Reduction; Protein Conformation; Protons; Spectrophotometry

1982
Activating effect of p-(chloromercuri)benzoate on the cytoplasmic aldehyde dehydrogenase from sheep liver.
    Biochemistry, 1984, Dec-18, Volume: 23, Issue:26

    Topics: Aldehyde Dehydrogenase; Aldehydes; Animals; Chloromercuribenzoates; Cytoplasm; Enzyme Activation; In Vitro Techniques; Kinetics; Liver; NAD; p-Chloromercuribenzoic Acid; Sheep

1984
Relationship between the mechanisms of the esterase and dehydrogenase activities of the cytoplasmic aldehyde dehydrogenase from sheep liver. An alternative view.
    Biochemistry, 1983, Aug-02, Volume: 22, Issue:16

    Topics: Aldehyde Dehydrogenase; Aldehyde Oxidoreductases; Aldehydes; Animals; Binding, Competitive; Chloral Hydrate; Esterases; Kinetics; Ligands; Liver; NAD; Sheep

1983
A two-site model for the esterase and dehydrogenase activities of sheep liver aldehyde dehydrogenase.
    Pharmacology, biochemistry, and behavior, 1983, Volume: 18 Suppl 1

    Topics: Aldehyde Dehydrogenase; Aldehyde Oxidoreductases; Aldehydes; Animals; Esterases; Glyoxylates; Hydrogen-Ion Concentration; Liver; NAD; Sheep; Substrate Specificity

1983
Kinetic properties of highly purified preparations of sheep liver cytoplasmic aldehyde dehydrogenase.
    The Biochemical journal, 1982, Jun-01, Volume: 203, Issue:3

    Topics: Aldehyde Dehydrogenase; Aldehyde Oxidoreductases; Aldehydes; Animals; Cytoplasm; Kinetics; Liver; NAD; Oxidation-Reduction; Sheep; Spectrometry, Fluorescence; Spectrophotometry

1982
The effect of p-(chloromercuri)benzoate modification of cytosolic aldehyde dehydrogenase from sheep liver. Evidence for a second aldehyde binding site.
    Archives of biochemistry and biophysics, 1994, Volume: 310, Issue:1

    Topics: Aldehyde Dehydrogenase; Aldehydes; Animals; Chloromercuribenzoates; Enzyme Activation; Fluorescence; Liver; Molecular Weight; NAD; p-Chloromercuribenzoic Acid; Protein Conformation; Sheep

1994
Is the single site binding model for aldehyde dehydrogenase an oversimplification? The one-site, two-site debate revisited.
    Advances in experimental medicine and biology, 1993, Volume: 328

    Topics: Aldehyde Dehydrogenase; Aldehydes; Animals; Binding Sites; Chloromercuribenzoates; Cytosol; Disulfiram; Fluorescence; In Vitro Techniques; Kinetics; Liver; Models, Chemical; NAD; Protons; Sheep

1993
Influence of Tris(hydroxymethyl)aminomethane on kinetic mechanism of yeast alcohol dehydrogenase.
    Journal of enzyme inhibition, 1998, Volume: 13, Issue:1

    Topics: 1-Propanol; Acetaldehyde; Acridines; Alcohol Dehydrogenase; Aldehydes; Buffers; Enzyme Inhibitors; Kinetics; NAD; Oxidation-Reduction; Phosphates; Potassium Compounds; Saccharomyces cerevisiae; Tromethamine

1998
The phnIJ genes encoding acetaldehyde dehydrogenase (acylating) and 4-hydroxy-2-oxovalerate aldolase in Pseudomonas sp. DJ77 and their evolutionary implications.
    Biochemical and biophysical research communications, 1999, Mar-24, Volume: 256, Issue:3

    Topics: Acetaldehyde; Aldehyde Oxidoreductases; Aldehydes; Amino Acid Sequence; Base Sequence; Blotting, Southern; Cloning, Molecular; Coenzyme A; Evolution, Molecular; Genes, Bacterial; Molecular Sequence Data; NAD; Open Reading Frames; Operon; Oxo-Acid-Lyases; Phenanthrenes; Phylogeny; Pseudomonas; Recombinant Proteins; Sequence Homology, Amino Acid

1999
Interaction of human aldehyde dehydrogenase with aromatic substrates and ligands.
    Chemico-biological interactions, 2001, Jan-30, Volume: 130-132, Issue:1-3

    Topics: Aldehyde Dehydrogenase; Aldehyde Dehydrogenase 1 Family; Aldehydes; Benzaldehydes; Binding Sites; Catalytic Domain; Chloramphenicol; Chromatography, Affinity; Enzyme Activation; Enzyme Inhibitors; Humans; In Vitro Techniques; Isoenzymes; Kinetics; Ligands; NAD; Retinal Dehydrogenase; Substrate Specificity

2001
Acetaldehyde mediates growth stimulation of ethanol-stressed Saccharomyces cerevisiae: evidence of a redox-driven mechanism.
    Biotechnology letters, 2007, Volume: 29, Issue:7

    Topics: Acetaldehyde; Aldehydes; Electrons; Ethanol; Glucose; NAD; Oxidation-Reduction; Saccharomyces cerevisiae; Time Factors

2007
Mechanistic implications of the cysteine-nicotinamide adduct in aldehyde dehydrogenase based on quantum mechanical/molecular mechanical simulations.
    Biochemistry, 2007, Aug-21, Volume: 46, Issue:33

    Topics: Aldehyde Dehydrogenase; Aldehyde Dehydrogenase, Mitochondrial; Aldehydes; Computer Simulation; Cysteine; Humans; NAD; Niacinamide; Protein Conformation; Protons; Quantum Theory

2007
Identification and characterization of the propanediol utilization protein PduP of Lactobacillus reuteri for 3-hydroxypropionic acid production from glycerol.
    Applied microbiology and biotechnology, 2011, Volume: 89, Issue:3

    Topics: Aldehydes; Bacterial Proteins; Cloning, Molecular; Coenzymes; Enzymes; Gene Expression; Glycerol; Kinetics; Klebsiella pneumoniae; Lactic Acid; Limosilactobacillus reuteri; NAD; NADP; Recombinant Proteins; Substrate Specificity

2011
Development of a sensitive long-wavelength fluorogenic probe for nitroreductase: a new fluorimetric indictor for analyte determination by dehydrogenase-coupled biosensors.
    Biosensors & bioelectronics, 2011, Apr-15, Volume: 26, Issue:8

    Topics: 3-Hydroxybutyric Acid; Aldehyde Dehydrogenase; Aldehydes; Biosensing Techniques; Fluorescence; Fluorescent Dyes; Fluorometry; Hydroxybutyrate Dehydrogenase; NAD; Nitro Compounds; Nitroreductases

2011
Methylmalonate-semialdehyde dehydrogenase from Bacillus subtilis: substrate specificity and coenzyme A binding.
    The Journal of biological chemistry, 2011, Jun-24, Volume: 286, Issue:25

    Topics: Aldehydes; Amino Acid Sequence; Amino Acid Substitution; Animals; Bacillus subtilis; Biocatalysis; Coenzyme A; Enzyme Stability; Esterification; Humans; Kinetics; Methylmalonate-Semialdehyde Dehydrogenase (Acylating); Methylmalonic Acid; Molecular Sequence Data; Mutation; NAD; Protein Binding; Rats; Substrate Specificity

2011
Modulation of ethanol stress tolerance by aldehyde dehydrogenase in the mycorrhizal fungus Tricholoma vaccinum.
    Mycorrhiza, 2012, Volume: 22, Issue:6

    Topics: Aldehyde Dehydrogenase; Aldehydes; Amino Acid Motifs; Amino Acid Sequence; Base Sequence; Ethanol; Evolution, Molecular; Fungal Proteins; Gene Expression Regulation, Fungal; Kinetics; Molecular Sequence Data; Mycelium; Mycorrhizae; NAD; NADP; Phylogeny; Recombinant Fusion Proteins; Stress, Physiological; Substrate Specificity; Tricholoma; Up-Regulation

2012
Coenzyme A-acylating propionaldehyde dehydrogenase (PduP) from Lactobacillus reuteri: kinetic characterization and molecular modeling.
    Enzyme and microbial technology, 2013, Sep-10, Volume: 53, Issue:4

    Topics: Aldehyde Dehydrogenase; Aldehyde Oxidoreductases; Aldehydes; Amino Acid Sequence; Bacterial Proteins; Binding Sites; Cloning, Molecular; Coenzyme A; Computer Simulation; Genes, Bacterial; Kinetics; Limosilactobacillus reuteri; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; NAD; Protein Conformation; Recombinant Proteins; Sequence Homology, Amino Acid

2013
Engineering the PduT shell protein to modify the permeability of the 1,2-propanediol microcompartment of
    Microbiology (Reading, England), 2019, Volume: 165, Issue:12

    Topics: Aldehydes; Bacterial Proteins; Culture Media; Models, Biological; Models, Molecular; Mutagenesis, Site-Directed; Mutation; NAD; Organelles; Permeability; Propylene Glycol; Salmonella

2019
Adh4, an alcohol dehydrogenase controls alcohol formation within bacterial microcompartments in the acetogenic bacterium Acetobacterium woodii.
    Environmental microbiology, 2021, Volume: 23, Issue:1

    Topics: 1-Propanol; Acetaldehyde; Acetates; Acetobacterium; Alcohol Dehydrogenase; Aldehydes; Bacterial Proteins; Carbon Dioxide; Ethanol; Genome, Bacterial; NAD; Oxidation-Reduction

2021