Oxidoreductases

A dehydrogenase (also called DH or DHase in the literature) is an enzyme belonging to the group of oxidoreductases that oxidizes a substrate by a reduction reaction that removes one or more hydrogens from a substrate to an electron acceptor, usually NAD+/NADP+ or a flavin coenzyme such as FAD or FMN.

Flavin mononucleotide (FMN), or riboflavin-5′-phosphate, is a biomolecule produced from riboflavin (vitamin B2) by the enzyme riboflavin kinase and functions as prosthetic group of various oxidoreductases including NADH dehydrogenase as well as cofactor in biological blue-light photo receptors.

Luciferase is a generic term for the class of oxidative enzymes that produce bioluminescence, and is distinct from a photoprotein.

Superoxide dismutase (SOD, EC 1.15.1.1) is an enzyme that alternately catalyzes the dismutation (or partitioning) of the superoxide (O2−) radical into either ordinary molecular oxygen (O2) or hydrogen peroxide (H2O2).

An oxidase is an enzyme that catalyzes an oxidation-reduction reaction, especially one involving dioxygen (O2) as the electron acceptor.

The enzyme urate oxidase (UO), or uricase or factor-independent urate hydroxylase, absent in humans, catalyzes the oxidation of uric acid to 5-hydroxyisourate: Uric acid + O2 + H2O → 5-hydroxyisourate + H2O2 → allantoin + CO2

Methane monooxygenase, or MMO, is an enzyme capable of oxidizing the C-H bond in methane as well as other alkanes.

In molecular biology, TauD refers to a protein domain that in many enteric bacteria is used to break down taurine (2-aminoethanesulphonic acid) as a source of sulphur under stress conditions.

Dioxygenases are oxidoreductase enzymes.

DMSO reductase is a molybdenum-containing enzyme that catalyzes reduction of dimethyl sulfoxide (DMSO) to dimethyl sulfide (DMS).

The flavin-containing monooxygenase (FMO) protein family specializes in the oxidation of xeno-substrates in order to facilitate the excretion of these compounds from living organisms.

In enzymology, a 1-pyrroline-5-carboxylate dehydrogenase (EC 1.2.1.88) is an enzyme that catalyzes the chemical reaction (S)-1-pyrroline-5-carboxylate + NAD+ + 2 H2O L-glutamate + NADH + H+ The three substrates of this enzyme are (S)-1-pyrroline-5-carboxylate, NAD+, and H2O, whereas its three products are glutamate, NADH, and H+.

Octopine dehydrogenase (N2-(D-1-carboxyethyl)-L-arginine:NAD+ oxidoreductase, OcDH, ODH) is a dehydrogenase enzyme in the opine dehydrogenase family that helps maintain redox balance under anaerobic conditions.

Vinylphenol reductase is an enzyme that catalyses the reaction : 4-vinylphenol + NAD+ + 3 H+ ⇔ 4-ethylphenol + NADH It is found in Brettanomyces bruxellensis, a yeast responsible of the presence of ethyl phenols in wine formed from p-coumaric acid.