Oxidoreductase

<h2 id="reactions">Reactions</h2>
<p>For example, an enzyme that catalyzed this reaction would be an oxidoreductase:
</p>
A– + B → A + B–
<p>In this example, A is the reductant (electron donor) and B is the oxidant (electron acceptor).
</p><p>In biochemical reactions, the <a href="/facts/Redox/Pyd5RVcj">redox</a> reactions are sometimes more difficult to see, such as this reaction from <a href="/facts/Glycolysis/a5ApxLoG">glycolysis</a>:
</p>
Pi + glyceraldehyde-3-phosphate + NAD+ → NADH + H+ + 1,3-bisphosphoglycerate
<p>In this reaction, NAD+ is the oxidant (electron acceptor), and <a href="/facts/Glyceraldehyde-3-phosphate/Wy3FMLzJ">glyceraldehyde-3-phosphate</a> is the reductant (electron donor).
</p>
<h2 id="nomenclature">Nomenclature</h2>
<p>Proper names of oxidoreductases are formed as "<i>donor:acceptor</i> oxidoreductase"; however, other names are much more common.
</p>
<ul><li>The common name is "<i>donor</i> <a href="/facts/Dehydrogenase/hX7eulAz">dehydrogenase</a>" when possible, such as glyceraldehyde-3-phosphate dehydrogenase for the second reaction above.</li>
<li>Common names are also sometimes formed as "<i>acceptor</i> reductase", such as NAD+ reductase.</li>
<li>"<i>Donor</i> <a href="/facts/Oxidase/MWIPq1cQ">oxidase</a>" is a special case where <a href="/facts/Dioxygen/UVNYnKUQ">O2</a> is the acceptor.</li></ul>
<h2 id="classification">Classification</h2>
<p>Oxidoreductases are classified as EC 1 in the <a href="/facts/Enzyme_Commission_number/Y5GNLRKX">EC number</a> classification of enzymes. Oxidoreductases can be further classified into 21 subclasses:
</p>
<ul><li>EC 1.1 includes oxidoreductases that act on the CH-OH group of donors (<a href="/facts/Alcohol_oxidoreductases/cSNSfgLp">alcohol oxidoreductases</a> such as <a href="/facts/Methanol_dehydrogenase/C5v9pluu">methanol dehydrogenase</a>)</li>
<li>EC 1.2 includes oxidoreductases that act on the <a href="/facts/Aldehyde/xSIRkW03">aldehyde</a> or oxo group of donors</li>
<li>EC 1.3 includes oxidoreductases that act on the CH-CH group of donors (<a href="/facts/CH-CH_oxidoreductases/IvtmlsvJ">CH-CH oxidoreductases</a>)</li>
<li>EC 1.4 includes oxidoreductases that act on the CH-NH2 group of donors (<a href="/facts/Amino_acid_oxidoreductases/cuMn86Uw">Amino acid oxidoreductases</a>, <a href="/facts/Monoamine_oxidase/4bJuxUFy">Monoamine oxidase</a>)</li>
<li>EC 1.5 includes oxidoreductases that act on CH-NH group of donors</li>
<li>EC 1.6 includes oxidoreductases that act on NADH or NADPH</li>
<li>EC 1.7 includes oxidoreductases that act on other nitrogenous compounds as donors</li>
<li>EC 1.8 includes oxidoreductases that act on a <a href="/facts/Sulfur/IK0amTfM">sulfur</a> group of donors</li>
<li>EC 1.9 includes oxidoreductases that act on a <a href="/facts/Heme/fRhyJAAb">heme</a> group of donors</li>
<li>EC 1.10 includes oxidoreductases that act on <a href="/facts/Benzenediol/LCm0bf1g">diphenols</a> and related substances as donors</li>
<li>EC 1.11 includes oxidoreductases that act on <a href="/facts/Peroxide/VMU8y4xB">peroxide</a> as an acceptor (<a href="/facts/Peroxidase/pEgHpmCV">peroxidases</a>)</li>
<li>EC 1.12 includes oxidoreductases that act on hydrogen as donors</li>
<li>EC 1.13 includes oxidoreductases that act on single donors with incorporation of molecular oxygen (<a href="/facts/Oxygenase/HCJvvLKP">oxygenases</a>)</li>
<li>EC 1.14 includes oxidoreductases that act on paired donors with incorporation of molecular oxygen</li>
<li>EC 1.15 includes oxidoreductases that act on <a href="/facts/Superoxide/2X2sQocn">superoxide</a> radicals as acceptors</li>
<li>EC 1.16 includes oxidoreductases that oxidize metal ions</li>
<li>EC 1.17 includes oxidoreductases that act on CH or CH2 groups</li>
<li>EC 1.18 includes oxidoreductases that act on iron-sulfur proteins as donors</li>
<li>EC 1.19 includes oxidoreductases that act on reduced <a href="/facts/Flavodoxin/N5zfv1vl">flavodoxin</a> as a donor</li>
<li>EC 1.20 includes oxidoreductases that act on <a href="/facts/Phosphorus/27xCeIqs">phosphorus</a> or <a href="/facts/Arsenic/k1c4f44D">arsenic</a> in donors</li>
<li>EC 1.21 includes oxidoreductases that act on X-H and Y-H to form an X-Y bond</li></ul>
<h2 id="see-also">See also</h2>
<ul><li><a href="/facts/Hydroxylase/AevYpR6L">Hydroxylase</a></li>
<li><a href="/facts/List_of_enzymes/w2RP6EwU">List of enzymes</a></li></ul>

<h2 id="external-links">External links</h2>
<ul><li> Media related to Oxidoreductases at Wikimedia Commons</li>
<li><a href="https://web.archive.org/web/20120716211126/http://www.chem.qmul.ac.uk/iubmb/enzyme/EC1/intro.html">EC 1 Introduction</a> from the Department of Chemistry at <a href="/facts/Queen_Mary%2c_University_of_London/j7FHapKf">Queen Mary, University of London</a></li></ul>

<h2 id="references">References</h2>

<ol>
<li id="fn:1"><p>Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 ed.). Wiley-Interscience. ISBN 0471205036. <a href="0471205036" target="_blank">0471205036</a> <a href="#fnref:1" class="footnote-back-ref">↩</a></p></li>
<li id="fn:2"><p>Nicholas C. Price; Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third ed.). USA: Oxford University Press. ISBN 019850229X. <a href="019850229X" target="_blank">019850229X</a> <a href="#fnref:2" class="footnote-back-ref">↩</a></p></li>
<li id="fn:3"><p>Superfamilies of single-pass transmembrane oxidoreductases in Membranome database <a href="http://membranome.org/protein_classes/9" target="_blank">http://membranome.org/protein_classes/9</a> <a href="#fnref:3" class="footnote-back-ref">↩</a></p></li>
</ol>

Oxidoreductase open-in-new

Oxidoreductase