Thermodynamics of reactions of nicotinamide adenine dinucleotide and nicotinamide adenine dinucleotide phosphate. 1993

R A Alberty
Chemistry Department, Massachusetts Institute of Technology, Cambridge 02139.

The thermodynamics of six reactions of nicotinamide adenine dinucleotide and nicotinamide adenine dinucleotide phosphate is discussed both from the viewpoint of the chemical equations and the biochemical equations for these reactions. Tables of the standard enthalpies of formation and standard Gibbs energies of formation of species are presented and are used to calculate standard enthalpies of reaction, standard Gibbs energies of reaction, and equilibrium constants K of chemical reactions at 25 degrees C, 1 bar, and ionic strengths of 0, 0.1, and 0.25 M. These tables are used to calculate standard transformed enthalpies of formation and standard transformed Gibbs energies of formation of reactants, standard transformed enthalpies of reaction, standard transformed Gibbs energies of reaction, and apparent equilibrium constants K' of biochemical reactions at 25 degrees C, 1 bar, pH 7, and ionic strengths of 0, 0.1, and 0.25 M. Since these reactions do not involve pK's of acid groups in the vicinity of pH 7, these reactions produce exactly 0, 1, or 2 mol of H+ per mole of reaction. The calculations are compared with experimental values.

UI MeSH Term Description Entries
D007700 Kinetics The rate dynamics in chemical or physical systems.
D009243 NAD A coenzyme composed of ribosylnicotinamide 5'-diphosphate coupled to adenosine 5'-phosphate by pyrophosphate linkage. It is found widely in nature and is involved in numerous enzymatic reactions in which it serves as an electron carrier by being alternately oxidized (NAD+) and reduced (NADH). (Dorland, 27th ed) Coenzyme I,DPN,Diphosphopyridine Nucleotide,Nadide,Nicotinamide-Adenine Dinucleotide,Dihydronicotinamide Adenine Dinucleotide,NADH,Adenine Dinucleotide, Dihydronicotinamide,Dinucleotide, Dihydronicotinamide Adenine,Dinucleotide, Nicotinamide-Adenine,Nicotinamide Adenine Dinucleotide,Nucleotide, Diphosphopyridine
D009249 NADP Nicotinamide adenine dinucleotide phosphate. A coenzyme composed of ribosylnicotinamide 5'-phosphate (NMN) coupled by pyrophosphate linkage to the 5'-phosphate adenosine 2',5'-bisphosphate. It serves as an electron carrier in a number of reactions, being alternately oxidized (NADP+) and reduced (NADPH). (Dorland, 27th ed) Coenzyme II,Nicotinamide-Adenine Dinucleotide Phosphate,Triphosphopyridine Nucleotide,NADPH,Dinucleotide Phosphate, Nicotinamide-Adenine,Nicotinamide Adenine Dinucleotide Phosphate,Nucleotide, Triphosphopyridine,Phosphate, Nicotinamide-Adenine Dinucleotide
D009250 NADP Transhydrogenases Enzymes that catalyze the reversible reduction of NAD by NADPH to yield NADP and NADH. This reaction permits the utilization of the reducing properties of NADPH by the respiratory chain and in the reverse direction it allows the reduction of NADP for biosynthetic purposes. NADP Transhydrogenase,Pyridine Nucleotide Transhydrogenase,Energy-Linked Transhydrogenase,NAD Transhydrogenase,NADPH NAD Transhydrogenase,NADPH Transferase,Nicotinamide Nucleotide Transhydrogenase,Energy Linked Transhydrogenase,NAD Transhydrogenase, NADPH,Nucleotide Transhydrogenase, Nicotinamide,Nucleotide Transhydrogenase, Pyridine,Transferase, NADPH,Transhydrogenase, Energy-Linked,Transhydrogenase, NAD,Transhydrogenase, NADP,Transhydrogenase, NADPH NAD,Transhydrogenase, Nicotinamide Nucleotide,Transhydrogenase, Pyridine Nucleotide,Transhydrogenases, NADP
D010088 Oxidoreductases The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possible; as an alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor. (Enzyme Nomenclature, 1992, p9) Dehydrogenases,Oxidases,Oxidoreductase,Reductases,Dehydrogenase,Oxidase,Reductase
D000426 Alcohol Dehydrogenase A zinc-containing enzyme which oxidizes primary and secondary alcohols or hemiacetals in the presence of NAD. In alcoholic fermentation, it catalyzes the final step of reducing an aldehyde to an alcohol in the presence of NADH and hydrogen. Alcohol Dehydrogenase (NAD+),Alcohol Dehydrogenase I,Alcohol Dehydrogenase II,Alcohol-NAD+ Oxidoreductase,Yeast Alcohol Dehydrogenase,Alcohol Dehydrogenase, Yeast,Alcohol NAD+ Oxidoreductase,Dehydrogenase, Alcohol,Dehydrogenase, Yeast Alcohol,Oxidoreductase, Alcohol-NAD+
D000444 Aldehyde Dehydrogenase An enzyme that oxidizes an aldehyde in the presence of NAD+ and water to an acid and NADH. This enzyme was formerly classified as EC 1.1.1.70. D-Glucuronolactone Dehydrogenase,Aldehyde Dehydrogenase (NAD(+)),Aldehyde Dehydrogenase E1,Aldehyde Dehydrogenase E2,Aldehyde-NAD Oxidoreductase,Aldehyde NAD Oxidoreductase,D Glucuronolactone Dehydrogenase,Dehydrogenase, Aldehyde,Dehydrogenase, D-Glucuronolactone
D000594 Amino Acid Oxidoreductases A class of enzymes that catalyze oxidation-reduction reactions of amino acids. Acid Oxidoreductases, Amino,Oxidoreductases, Amino Acid
D013816 Thermodynamics A rigorously mathematical analysis of energy relationships (heat, work, temperature, and equilibrium). It describes systems whose states are determined by thermal parameters, such as temperature, in addition to mechanical and electromagnetic parameters. (From Hawley's Condensed Chemical Dictionary, 12th ed) Thermodynamic
D050788 Alanine Dehydrogenase An NAD-dependent enzyme that catalyzes the reversible DEAMINATION of L-ALANINE to PYRUVATE and AMMONIA. The enzyme is needed for growth when ALANINE is the sole CARBON or NITROGEN source. It may also play a role in CELL WALL synthesis because L-ALANINE is an important constituent of the PEPTIDOGLYCAN layer. L-Alanine Dehydrogenase,Dehydrogenase, Alanine,Dehydrogenase, L-Alanine,L Alanine Dehydrogenase

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