Amino acid oxidoreductases

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Amino acid oxidoreductases are oxidoreductases, a type of enzyme, that act upon amino acids.

They constitute the majority of enzymes classified under EC number 1.4, with most of the remainder being monoamine oxidases.

The Enzyme Commission number is a numerical classification scheme for enzymes, based on the chemical reactions they catalyze. As a system of enzyme nomenclature, every EC number is associated with a recommended name for the respective enzyme.

Monoamine oxidase enzyme

Monoamine oxidases (MAO) are a family of enzymes that catalyze the oxidation of monoamines, employing oxygen to clip off their amine group. They are found bound to the outer membrane of mitochondria in most cell types of the body. The first such enzyme was discovered in 1928 by Mary Bernheim in the liver and was named tyramine oxidase. The MAOs belong to the protein family of flavin-containing amine oxidoreductases.

Examples include:

Medical Subject Headings (MeSH) is a comprehensive controlled vocabulary for the purpose of indexing journal articles and books in the life sciences. It serves as a thesaurus that facilitates searching. Created and updated by the United States National Library of Medicine (NLM), it is used by the MEDLINE/PubMed article database and by NLM's catalog of book holdings. MeSH is also used by ClinicalTrials.gov registry to classify which diseases are studied by trials registered in ClinicalTrials.


Related Research Articles

In biochemistry, an oxidoreductase is an enzyme that catalyzes the transfer of electrons from one molecule, the reductant, also called the electron donor, to another, the oxidant, also called the electron acceptor. This group of enzymes usually utilizes NADP or NAD+ as cofactors. Transmembrane oxidoreductases create electron transport chains in bacteria, chloroplasts and mitochondria, including respiratory complexes I, II and III. Some others can associate with biological membranes as peripheral membrane proteins or be anchored to the membranes through a single transmembrane helix.

L-xylulose reductase enzyme

Dicarbonyl/L-xylulose reductase, also known as carbonyl reductase II, is an enzyme that in human is encoded by the DCXR gene located on chromosome 17.

Penitrem A chemical compound

Penitrem A (tremortin) is an indole-diterpenoid mycotoxin produced by certain species of Aspergillus, Claviceps, and Penicillium, which can be found growing on various plant species such as ryegrass. Penitrem A is one of many secondary metabolites following the synthesis of paxilline in Penicillium crostosum. Penitrem A poisoning in humans and animals usually occurs through the consumption of contaminated foods by mycotoxin-producing species, which is then distributed through the body by the bloodstream. It bypasses the blood-brain barrier to exert its toxicological effects on the central nervous system. In humans, penitrem A poisoning has been associated with severe tremors, hyperthermia, nausea/vomiting, diplopia, and bloody diarrhea. In animals, symptoms of penitrem A poisoning has been associated with symptoms ranging from tremors, seizures, and hyperthermia to ataxia and nystagmus.

(R,R)-butanediol dehydrogenase class of enzymes

In enzymology, a (R,R)-butanediol dehydrogenase (EC 1.1.1.4) is an enzyme that catalyzes the chemical reaction

Isovaleryl-CoA dehydrogenase class of enzymes

In enzymology, an isovaleryl-CoA dehydrogenase is an enzyme that catalyzes the chemical reaction

In enzymology, a tryptophan alpha,beta-oxidase (EC 1.3.3.10) is an enzyme that catalyzes the chemical reaction

Beta-cyclopiazonate dehydrogenase class of enzymes

Beta-cyclopiazonate dehydrogenase is an enzyme that catalyzes the chemical reaction

In enzymology, a thiamine oxidase (EC 1.1.3.23) is an enzyme that catalyzes the chemical reaction

Aspartate-semialdehyde dehydrogenase class of enzymes

In enzymology, an aspartate-semialdehyde dehydrogenase is an enzyme that is very important in the biosynthesis of amino acids in prokaryotes, fungi, and some higher plants. It forms an early branch point in the metabolic pathway forming lysine, methionine, leucine and isoleucine from aspartate. This pathway also produces diaminopimelate which plays an essential role in bacterial cell wall formation. There is particular interest in ASADH as disabling this enzyme proves fatal to the organism giving rise to the possibility of a new class of antibiotics, fungicides, and herbicides aimed at inhibiting it.

3-hydroxyanthranilate 3,4-dioxygenase enzyme

In enzymology, a 3-hydroxyanthranilate 3,4-dioxygenase (EC 1.13.11.6) is an enzyme that catalyzes the chemical reaction

In enzymology, an indole 2,3-dioxygenase (EC 1.13.11.17) is an enzyme that catalyzes the chemical reaction

In enzymology, a 2,4-diaminopentanoate dehydrogenase (EC 1.4.1.12) is an enzyme that catalyzes the chemical reaction

In enzymology, a L-amino-acid dehydrogenase (EC 1.4.1.5) is an enzyme that catalyzes the chemical reaction

In enzymology, an L-amino acid oxidase (LAAO) (EC 1.4.3.2) is an enzyme that catalyzes the chemical reaction

In enzymology, a N-methyl-L-amino-acid oxidase (EC 1.5.3.2) is an enzyme that catalyzes the chemical reaction

In enzymology, an opine dehydrogenase (EC 1.5.1.28) is an enzyme that catalyzes the chemical reaction

FAD dependent oxidoreductase family class of enzymes

In molecular biology, the FAD dependent oxidoreductase family of proteins is a family of FAD dependent oxidoreductases. Members of this family include Glycerol-3-phosphate dehydrogenase EC 1.1.99.5, Sarcosine oxidase beta subunit EC 1.5.3.1, D-amino-acid dehydrogenase EC 1.4.99.1, D-aspartate oxidase EC 1.4.3.1.

D-amino acid dehydrogenase (quinone) (EC 1.4.5.1, DadA) is an enzyme with systematic name D-amino acid:quinone oxidoreductase (deaminating). This enzyme catalyses the following chemical reaction

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Aldehyde ferredoxin oxidoreductase class of enzymes

In enzymology, an aldehyde ferredoxin oxidoreductase (EC 1.2.7.5) is an enzyme that catalyzes the chemical reaction