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The 37 pages that link to Nicotinamide adenine dinucleotide, each with the reason it gives.
NucleotideRelated: Its structure includes an adenine nucleotide joined to another nucleotide-like unit.
Cellular respirationRelated: Respiratory pathways load NADH with electrons that feed the electron transport chain.
GlycolysisRelated: Glycolysis reduces NAD+ to NADH while oxidizing a sugar intermediate.
MetabolismRelated: This electron carrier links oxidation reactions to energy-producing pathways.
ATPCompared with: NADH chiefly transfers reducing power, unlike ATP’s widespread role in energy coupling.
Lactic acid fermentationRelated: Fermentation depends on recycling NADH back to NAD⁺.
Citric acid cycleRelated: Several cycle reactions transfer electrons from carbon intermediates to NAD⁺.
Alcoholic fermentationRelated: Its oxidized form, NAD⁺, must be replenished for glycolysis to continue.
Beta oxidationRelated: A later oxidation step reduces NAD⁺ to NADH in every round.
Lactate dehydrogenaseRelated: Its oxidized and reduced forms, NAD⁺ and NADH, are interconverted in the enzyme’s reaction.
NADPHCompared with: Unlike NADP+, it lacks the phosphate that distinguishes NADPH's coenzyme family.
Flavin adenine dinucleotideCompared with: NAD usually diffuses between enzymes, whereas FAD often remains tightly bound to one enzyme.
DNA ligaseCompared with: Some bacterial DNA ligases use NAD+ rather than ATP as their adenyl-group source.
NADHCompared with: NADH’s electron-donating capacity depends on its conversion back to NAD+.
AdenineBroader topic: Its name and structure include an adenine-bearing nucleotide unit.
Alcohol dehydrogenaseRelated: NAD⁺ accepts a hydride during many alcohol dehydrogenase reactions.
PellagraRelated: Niacin supplies precursors for NAD, whose depletion impairs energy metabolism in pellagra.
CoenzymeBroader topic: Its NAD⁺ and NADH forms illustrate how coenzymes shuttle electrons.
Pyruvate dehydrogenase complexRelated: The complex reduces NAD+ to NADH during acetyl-CoA formation.
RiboflavinCompared with: NAD and FAD both transfer electrons, but their structures and enzyme roles differ.
Hydride transferBroader topic: NADH transfers hydride equivalents in numerous enzyme-catalyzed redox reactions.
MalateRelated: Malate dehydrogenase couples malate conversion to the NADH/NAD⁺ redox pair.
NicotinamideBroader topic: Nicotinamide supplies the vitamin-derived ring in this central metabolic coenzyme.
Nicotinamide adenine dinucleotide phosphateNarrower topic: NADP is structurally derived from NAD by addition of a phosphate group.
Microbial metabolismRelated: NADH and its oxidized form shuttle electrons between metabolic reactions.
Nicotinic acidBroader topic: NAD is the central active product that makes vitamin B3 indispensable to cells.
Arthur HardenRelated: The fermentative enzyme systems Harden studied belong to the broader history of coenzyme research.
Corynebacterium diphtheriaeRelated: Diphtheria toxin uses NAD to transfer ADP-ribose onto elongation factor 2.
B vitaminsRelated: Niacin supplies the molecular building block for NAD.
Hans KrebsRelated: Cycle reactions capture electrons in NADH for later energy production.
Vitamin B3Broader topic: Vitamin B3 supplies building blocks for this central coenzyme.
Flavin mononucleotideCompared with: NAD usually carries two electrons together, unlike FMN’s ability to support single-electron steps.
Hans von Euler-ChelpinRelated: Its coenzyme role in fermentation belongs to the enzyme chemistry Euler-Chelpin helped clarify.
Pyruvic acidRelated: NADH supplies reducing power for converting pyruvate to lactate.
Alec ToddBroader topic: Todd’s research helped establish the structure of this nucleotide-containing coenzyme.
Enzymes and CoenzymesBroader topic: It illustrates how a coenzyme carries electrons between enzyme-catalyzed reactions.
Otto Heinrich WarburgRelated: Warburg studied how coenzymes participate in enzyme-catalyzed oxidation.