Oxidoreductase

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Overview

Oxidoreductase is an enzyme that catalyzes the transfer of electrons from one molecule (the reductant, also called the hydrogen acceptor or electron donor) to another (the oxidant, also called the hydrogen donor or electron acceptor). For example, an enzyme that catalyzed this reaction would be an oxidoreductase:

A + B → A + B

In this example, A is the reductant (electron donor) and B is the oxidant (electron acceptor).

In biochemical reactions, the redox reactions are sometimes more difficult to see, such as this reaction from glycolysis:

Pi + glyceraldehyde-3-phosphate + NAD+ → NADH + H+ + 1,3-bisphosphoglycerate

In this reaction, NAD+ is the oxidant (electron acceptor), and glyceraldehyde-3-phosphate is the reductant (electron donor).

Nomenclature

Proper names of oxidoreductases are formed as "donor:acceptor oxidoreductase." However, other names are much more common. The common name is "donor dehydrogenase" when possible, such as glyceraldehyde-3-phosphate dehydrogenase for the second reaction above. Common names are also sometimes formed as "acceptor reductase", such as NAD+ reductase. "Donor oxidase" is a special case where O2 is the acceptor.

Classification

Oxidoreductases are classified as EC 1 in the EC number classification of enzymes. Oxidoreductases can be further classified into 22 subclasses:

  • EC 1.1 includes oxidoreductases that act on the CH-OH group of donors (alcohol oxidoreductases)
  • EC 1.2 includes oxidoreductases that act on the aldehyde or oxo group of donors
  • EC 1.3 includes oxidoreductases that act on the CH-CH group of donors (CH-CH oxidoreductases)
  • EC 1.4 includes oxidoreductases that act on the CH-NH2 group of donors (Amino acid oxidoreductases, Monoamine oxidase)
  • EC 1.5 includes oxidoreductases that act on CH-NH group of donors
  • EC 1.6 includes oxidoreductases that act on NADH or NADPH
  • EC 1.7 includes oxidoreductases that act on other nitrogenous compounds as donors
  • EC 1.8 includes oxidoreductases that act on a sulfur group of donors
  • EC 1.9 includes oxidoreductases that act on a heme group of donors
  • EC 1.10 includes oxidoreductases that act on diphenols and related substances as donors
  • EC 1.11 includes oxidoreductases that act on peroxide as an acceptor (peroxidases)
  • EC 1.12 includes oxidoreductases that act on hydrogen as donors
  • EC 1.13 includes oxidoreductases that act on single donors with incorporation of molecular oxygen (oxygenases)
  • EC 1.14 includes oxidoreductases that act on paired donors with incorporation of molecular oxygen
  • EC 1.15 includes oxidoreductases that act on superoxide radicals as acceptors
  • EC 1.16 includes oxidoreductases that oxidize metal ions
  • EC 1.17 includes oxidoreductases that act on CH or CH2 groups
  • EC 1.18 includes oxidoreductases that act on iron-sulfur proteins as donors
  • EC 1.19 includes oxidoreductases that act on reduced flavodoxin as a donor
  • EC 1.20 includes oxidoreductases that act on phosphorus or arsenic in donors
  • EC 1.21 includes oxidoreductases that act on X-H and Y-H to form an X-Y bond
  • EC 1.97 includes other oxidoreductases

See also

External link

  • EC 1 Introduction from the Department of Chemistry at Queen Mary, University of London
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bg:Оксидоредуктаза ca:Oxidoreductasa cs:Oxidoreduktasa de:Oxidoreduktasenfr:Oxydo-réductase it:Ossidoreduttasi ja:酸化還元酵素

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Acknowledgement and Attribution Regarding Sources of Content

Some of the initial content on this page may be incorporated in part from copyleft sources in the public domain including wikis such as Wikipedia and AskDrWiki. Drug information for patients came from the The National Library of Medicine. Infectious disease information may have come from the Centers for Disease Control (CDC). Differential Diagnoses are drawn from clinicians as well as an amalgamation of 3 sources: 1.The Disease Database; 2. Kahan, Scott, Smith, Ellen G. In A Page: Signs and Symptoms. Malden, Massachusetts: Blackwell Publishing, 2004:3; 3. Sailer, Christian, Wasner, Susanne. Differential Diagnosis Pocket. Hermosa Beach, CA: Borm Bruckmeir Publishing LLC, 2002:7 .

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