The aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain is an evolutionary conserved protein domain.
Aldehyde oxidase (EC1.2.3.1) catalyzes the conversion of an aldehyde in the presence of oxygen and water to an acid and hydrogen peroxide. The enzyme is a homodimer, and requires FAD, molybdenum and two 2FE-2S clusters as cofactors. Xanthine dehydrogenase (EC1.1.1.204) catalyzes the hydrogenation of xanthine to urate, and also requires FAD, molybdenum and two 2FE-2S clusters as cofactors. This activity is often found in a bifunctional enzyme with xanthine oxidase (EC1.1.3.22) activity too. The enzyme can be converted from the dehydrogenase form to the oxidase form irreversibly by proteolysis or reversibly through oxidation of sulfhydryl groups.
Romão MJ, Archer M, Moura I, Moura JJ, LeGall J, Engh R, Schneider M, Hof P, Huber R (November 1995). "Crystal structure of the xanthine oxidase-related aldehyde oxido-reductase from D. gigas". Science. 270 (5239): 1170–6. doi:10.1126/science.270.5239.1170. PMID7502041. S2CID34922450.
A dehydrogenase (also called DH or DHase in the literature) is an enzyme belonging to the group of oxidoreductases that oxidizes a substrate by reducing an electron acceptor, usually NAD+/NADP+ or a flavin coenzyme such as FAD or FMN. They also catalyze the reverse reaction, for instance alcohol dehydrogenase not only oxidizes ethanol to acetaldehyde in animals but also produces ethanol from acetaldehyde in yeast.
Flavin is the common name for a group of organic compounds based on pteridine, formed by the tricyclic heterocycle isoalloxazine. The biochemical source is the vitamin riboflavin. The flavin moiety is often attached with an adenosine diphosphate to form flavin adenine dinucleotide (FAD), and, in other circumstances, is found as flavin mononucleotide, a phosphorylated form of riboflavin. It is in one or the other of these forms that flavin is present as a prosthetic group in flavoproteins.
Xanthine oxidase is a form of xanthine oxidoreductase, a type of enzyme that generates reactive oxygen species. These enzymes catalyze the oxidation of hypoxanthine to xanthine and can further catalyze the oxidation of xanthine to uric acid. These enzymes play an important role in the catabolism of purines in some species, including humans.
In biochemistry, flavin adenine dinucleotide (FAD) is a redox-active coenzyme associated with various proteins, which is involved with several enzymatic reactions in metabolism. A flavoprotein is a protein that contains a flavin group, which may be in the form of FAD or flavin mononucleotide (FMN). Many flavoproteins are known: components of the succinate dehydrogenase complex, α-ketoglutarate dehydrogenase, and a component of the pyruvate dehydrogenase complex.
Molybdopterins are a class of cofactors found in most molybdenum-containing and all tungsten-containing enzymes. Synonyms for molybdopterin are: MPT and pyranopterin-dithiolate. The nomenclature for this biomolecule can be confusing: Molybdopterin per se contains no molybdenum; rather, this is the name of the ligand that will bind the active metal. After molybdopterin is eventually complexed with molybdenum, the complete ligand is usually called molybdenum cofactor.
Aldehyde oxidase (AO) is a metabolizing enzyme, located in the cytosolic compartment of tissues in many organisms. AO catalyzes the oxidation of aldehydes into carboxylic acid, and in addition, catalyzes the hydroxylation of some heterocycles. It can also catalyze the oxidation of both cytochrome P450 (CYP450) and monoamine oxidase (MAO) intermediate products. AO plays an important role in the metabolism of several drugs.
Xanthine dehydrogenase, also known as XDH, is a protein that, in humans, is encoded by the XDH gene.
In enzymology, a malate oxidase (EC 1.1.3.3) is an enzyme that catalyzes the chemical reaction
In enzymology, an aldehyde dehydrogenase (FAD-independent) (EC 1.2.99.7) is an enzyme that catalyzes the chemical reaction
In enzymology, carbon monoxide dehydrogenase (CODH) (EC 1.2.7.4) is an enzyme that catalyzes the chemical reaction
In enzymology, a carbon-monoxide dehydrogenase (cytochrome b-561) (EC 1.2.2.4) is an enzyme that catalyzes the chemical reaction
In enzymology, a pyruvate dehydrogenase (cytochrome) (EC 1.2.2.2) is an enzyme that catalyzes the chemical reaction
Arsenate reductase (azurin) (EC 1.20.9.1) is an enzyme that catalyzes the chemical reaction
Molybdenum cofactor deficiency is a rare human disease in which the absence of molybdopterin – and consequently its molybdenum complex, commonly called molybdenum cofactor – leads to accumulation of toxic levels of sulphite and neurological damage. Usually this leads to death within months of birth, due to the lack of active sulfite oxidase. Furthermore, a mutational block in molybdenum cofactor biosynthesis causes absence of enzyme activity of xanthine dehydrogenase/oxidase and aldehyde oxidase.
Cyclic pyranopterin monophosphate (cPMP) is an experimental treatment for molybdenum cofactor deficiency type A, which was developed by José Santamaría-Araujo and Guenter Schwarz at the German universities TU Braunschweig and the University of Cologne.
Molybdopterin synthase (EC 2.8.1.12, MPT synthase) is an enzyme required to synthesize molybdopterin (MPT) from precursor Z (now known as cyclic pyranopterin monophosphate). Molydopterin is subsequently complexed with molybdenum to form molybdenum cofactor (MoCo). MPT synthase catalyses the following chemical reaction:
Aldehyde oxidase 1 is an enzyme that in humans is encoded by the AOX1 gene.
Molybdenum cofactor sulfurtransferase (EC 2.8.1.9, molybdenum cofactor sulfurase, ABA3, HMCS, MoCo sulfurase, MoCo sulfurtransferase) is an enzyme with systematic name L-cysteine:molybdenum cofactor sulfurtransferase. This enzyme catalyses the following chemical reaction
In enzymology, an aldehyde ferredoxin oxidoreductase (EC 1.2.7.5) is an enzyme that catalyzes the chemical reaction
In enzymology, a formylmethanofuran dehydrogenase (EC 1.2.99.5) is an enzyme that catalyzes the chemical reaction:
This page is based on this Wikipedia article Text is available under the CC BY-SA 4.0 license; additional terms may apply. Images, videos and audio are available under their respective licenses.
