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Oxidoreductase

From Wikipedia, the free encyclopedia
Enzyme involved in redox reactions

Inbiochemistry, anoxidoreductase is anenzyme that catalyzes the transfer ofelectrons from one molecule, thereductant, also called theelectron donor, to another, theoxidant, also called theelectron acceptor. This group of enzymes usually utilizesNADP+ orNAD+ ascofactors.[1][2] Transmembrane oxidoreductases createelectron transport chains in bacteria,chloroplasts andmitochondria, including respiratory complexesI,II andIII. Some others can associate withbiological membranes asperipheral membrane proteins or be anchored to the membranes through a singletransmembrane helix.[3]

Reactions

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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, theredox reactions are sometimes more difficult to see, such as this reaction fromglycolysis:

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

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

Nomenclature

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Proper names of oxidoreductases are formed as "donor:acceptor oxidoreductase"; however, other names are much more common.[citation needed]

  • The common name is "donordehydrogenase" 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.
  • "Donoroxidase" is a special case whereO2 is the acceptor.

Classification

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Oxidoreductases are classified asEC 1 in theEC number classification of enzymes. Oxidoreductases can be further classified into 21 subclasses:

See also

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References

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  1. ^Eric J. Toone (2006).Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 ed.). Wiley-Interscience.ISBN 0471205036.
  2. ^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.
  3. ^Superfamilies of single-pass transmembrane oxidoreductases inMembranome database

External links

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1.1.1:NAD/NADP acceptor
1.1.2:cytochrome acceptor
1.1.3:oxygen acceptor
1.1.4:disulfide as acceptor
1.1.5:quinone/similar acceptor
1.1.99: other acceptors
Aldehyde/oxooxidoreductases (EC 1.2)
1.2.1:NAD orNADP
1.2.2:cytochrome
1.2.3:oxygen
1.2.4:disulfide
1.2.7:iron–sulfur protein
1.3.1:NAD/NADP acceptor
1.3.3:Oxygen acceptor
1.3.5:Quinone
1.3.99: Other acceptors
1.4.1:NAD/NADP acceptor
1.4.3:oxygen acceptor
1.4.4:disulfide acceptor
1.4.99: other acceptors
Oxidoreductases: CH-NH (EC 1.5)
1.5.1:NAD orNADP acceptor
1.5.3:oxygen acceptor
1.5.5:quinone acceptor
1.5.99
1.6.1:NAD/NADP
1.6.2:Heme
1.6.3:Oxygen
1.6.5:Quinone or similar
1.6.6:Nitrogenous group
1.6.99: other
Oxidoreductases: nitrogenous donor (EC 1.7)
1.7.1
1.7.2
1.7.3
1.7.7
1.7.99
Oxidoreductases: sulfur oxidoreductases (EC 1.8)
1.8.1:NAD orNADP
1.8.2:cytochrome
1.8.3:oxygen
1.8.4:disulfide
1.8.5:quinone
1.8.98: Other, known
1.8.99: Other
Oxidoreductases: Acting on aheme group of donors (EC 1.9)
1.9.3
1.9.6
1.9.99
1.10.1
1.10.2
1.10.3
1.10.99
Other
1.11.1.1-14
1.11.1.15 (peroxiredoxin)
Oxidoreductases: Acting onhydrogen as donor (EC 1.12)
1.12.1
1.12.2
1.12.5
1.12.7
1.10.98
1.10.99
1.13.11: two atoms of oxygen
1.13.12: one atom of oxygen
1.13.99: other
1.14.11:2-oxoglutarate
1.14.13:NADH orNADPH
1.14.14: reducedflavin orflavoprotein
1.14.15: reducediron–sulfur protein
1.14.16: reducedpteridine (BH4 dependent)
1.14.17: reducedascorbate
1.14.18-19: other
1.14.99 - miscellaneous
Otheroxidoreductases (EC 1.15–1.21)
1.15: Acting onsuperoxide as acceptor
1.16: Oxidizingmetal ions
1.17: Acting on CH or CH2 groups
1.18: Acting oniron–sulfur proteins as donors
1.19: Acting on reducedflavodoxin as donor
1.20: Acting onphosphorus orarsenic in donors
1.21: Acting on X-H and Y-H to form an X-Y bond
Activity
Regulation
Classification
Kinetics
Types
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