Chemicals and Drugs

Formate Dehydrogenases

Flavoproteins that catalyze reversibly the reduction of carbon dioxide to formate. Many compounds can act as acceptors, but the only physiologically active acceptor is NAD. The enzymes are active in the fermentation of sugars and other compounds to carbon dioxide and are the key enzymes in obtaining energy when bacteria are grown on formate as the main carbon source. They have been purified from bovine blood. EC 1.2.1.2.

National Library of MedicineMedical Subject Headings2026

Structured Summary

Abstract

Flavoproteins that catalyze reversibly the reduction of carbon dioxide to formate. Many compounds can act as acceptors, but the only physiologically active acceptor is NAD. The enzymes are active in the fermentation of sugars and other compounds to carbon dioxide and are the key enzymes in obtaining energy when bacteria are grown on formate as the main carbon source. They have been purified from bovine blood. EC 1.2.1.2.

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Synonyms

8 entry terms
  • Formate Dehydrogenase
  • Formate Hydrogenlyases
  • NAD-Formate Dehydrogenase
  • Dehydrogenase, Formate
  • Dehydrogenase, NAD-Formate
  • Dehydrogenases, Formate
  • Hydrogenlyases, Formate
  • NAD Formate Dehydrogenase

MeSH Record

Aspects Covered

29 allowable subheadings

Indexed with the subheadings administration & dosage, adverse effects, analysis, antagonists & inhibitors, biosynthesis, blood, cerebrospinal fluid, chemical synthesis, chemistry, classification, deficiency, drug effects, economics, genetics, history, immunology, isolation & purification, metabolism, pharmacokinetics, pharmacology, physiology, poisoning, radiation effects, standards, supply & distribution, therapeutic use, toxicity, ultrastructure, urine.

MeSH Record

History Note

91(80); was see under ALDEHYDE OXIDOREDUCTASES 1980-90

MeSH Record

Previous Indexing

  • Aldehyde Oxidoreductases (1973-1979)
  • Formates (1966-1967)
  • Formic Acids (1968-1979)
  • Oxidoreductases (1966-1972)

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References

  1. National Library of Medicine. Formate Dehydrogenases. Medical Subject Headings (MeSH). 2026. Unique ID D005560. http://id.nlm.nih.gov/mesh/2026/D005560
  2. Formate Dehydrogenases. In: Wikipedia. https://en.wikipedia.org/wiki/Formate_dehydrogenase
  3. Formate Dehydrogenases. In: Wikidata. https://www.wikidata.org/wiki/Q1147563