|
Flavin-containing Amine Oxidoreductase
Flavin-containing amine oxidoreductases are a family of various amine oxidases, including maize polyamine oxidase (PAO), L-amino acid oxidases (LAO) and various flavin containing monoamine oxidases (MAO). The aligned region includes the flavin binding site of these enzymes. In vertebrates, MAO plays an important role in regulating the intracellular levels of amines via their oxidation; these include various neurotransmitters, neurotoxins and trace amines. In lower eukaryotes such as aspergillus and in bacteria the main role of amine oxidases is to provide a source of ammonium. PAOs in plants, bacteria and protozoa oxidise spermidine and spermine to an aminobutyral, diaminopropane and hydrogen peroxide and are involved in the catabolism of polyamines. Other members of this family include tryptophan 2-monooxygenase, putrescine oxidase, corticosteroid-binding proteins, and antibacterial glycoproteins. Human proteins containing this domain AOF1; AOF2; IL4I1; ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Amine Oxidase
An amine oxidase is an enzyme that catalyzes the oxidative cleavage of alkylamines into aldehydes and ammonia Ammonia is an inorganic compound of nitrogen and hydrogen with the formula . A stable binary hydride, and the simplest pnictogen hydride, ammonia is a colourless gas with a distinct pungent smell. Biologically, it is a common nitrogenous was ...: :RCH2NH2 + H2O + O2 \rightleftharpoons RCHO + NH3 + H2O2 Amine oxidases are divided into two subfamilies based on the cofactor they contain: References External links * {{oxidoreductase-stub EC 1.4.3 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Tryptophan 2-monooxygenase
In enzymology, a tryptophan 2-monooxygenase () is an enzyme that catalyzes the chemical reaction :L-tryptophan + O2 \rightleftharpoons (indol-3-yl)acetamide + CO2 + H2O Thus, the two substrates of this enzyme are L-tryptophan and O2, and its 3 products are (indol-3-yl)acetamide, CO2, and H2O. This enzyme belongs to the family of oxidoreductases, specifically those acting on single donors with O2 as oxidant and incorporation of two atoms of oxygen into the substrate (oxygenases). The oxygen incorporated need not be derived from O with incorporation of one atom of oxygen (internal monooxygenases o internal mixed-function oxidases). The systematic name of this enzyme class is L-tryptophan:oxygen 2-oxidoreductase (decarboxylating). This enzyme participates in tryptophan metabolism Tryptophan (symbol Trp or W) is an α-amino acid that is used in the biosynthesis of proteins. Tryptophan contains an α-amino group, an α-carboxylic acid group, and a side chain indole, making ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
SMOX
Spermine oxidase is an enzyme that in humans is encoded by the ''SMOX'' gene. Function The product of this gene is the polyamine oxidase A polyamine oxidase (PAO) is an enzymatic flavoprotein that oxidizes a carbon-nitrogen bond in a secondary amino group of a polyamine donor, using molecular oxygen as an acceptor. The generalized PAO reaction converts three substrates (water, oxy .... This enzyme potentially represents a new class of catabolic enzymes in the mammalian polyamine metabolic pathway capable of the efficient oxidation of polyamines. More than five transcript variants encoding four active isoenzymes have been identified for this gene, however, not all variants have been fully described. The characterized isoenzymes have distinctive biochemical characteristics and substrate specificities, suggesting the existence of additional levels of complexity in polyamine catabolism. References Further reading * * * * * * * * {{gene-20-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
PPOX
Protoporphyrinogen oxidase or protox is an enzyme that in humans is encoded by the ''PPOX'' gene. Protoporphyrinogen oxidase is responsible for the seventh step in biosynthesis of protoporphyrin IX. This porphyrin is the precursor to hemoglobin, the oxygen carrier in animals, and chlorophyll, the dye in plants. The enzyme catalyzes the dehydrogenation (removal of hydrogen atoms) of protoporphyrinogen IX (the product of the sixth step in the production of heme) to form protoporphyrin IX. One additional enzyme must modify protoporphyrin IX before it becomes heme. Inhibition of this enzyme is a strategy used in certain herbicides. Gene The PPOX gene is located on the long (q) arm of chromosome 1 at position 22, from base pair 157,949,266 to base pair 157,954,082. Function This gene encodes the penultimate enzyme of heme biosynthesis, which catalyzes the 6-electron oxidation of protoporphyrinogen IX to form protoporphyrin IX. This protein is a flavoprotein associated with th ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
PAOX
Peroxisomal N(1)-acetyl-spermine/spermidine oxidase is an enzyme that in humans is encoded by the ''PAOX'' gene In biology, the word gene (from , ; "...Wilhelm Johannsen coined the word gene to describe the Mendelian units of heredity..." meaning ''generation'' or ''birth'' or ''gender'') can have several different meanings. The Mendelian gene is a ba .... References Further reading * * * * * * * {{gene-10-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
MAOB
Monoamine oxidase B, also known as MAOB, is an enzyme that in humans is encoded by the ''MAOB'' gene. The protein encoded by this gene belongs to the flavin monoamine oxidase family. It is an enzyme located in the outer mitochondrial membrane. It catalyzes the oxidative deamination of biogenic and xenobiotic amines and plays an important role in the catabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues (such as dopamine). This protein preferentially degrades benzylamine and phenethylamine. Similarly to monoamine oxidase A (MAOA), it also degrades dopamine hough some new research contradicts this, suggesting that MAOB does ''not'' directly degrade dopamine, but is responsible for GABA synthesis Structure Monoamine oxidase B has a hydrophobic bipartite elongated cavity that (for the "open" conformation) occupies a combined volume close to 700 Å3. hMAO-A has a single cavity that exhibits a rounder shape and is larger in volume than ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
MAOA
Monoamine oxidase A, also known as MAO-A, is an enzyme that in humans is encoded by the ''MAOA'' gene. This gene is one of two neighboring gene family members that encode mitochondrial enzymes which catalyze the oxidative deamination of amines, such as dopamine, norepinephrine, and serotonin. A mutation of this gene results in Brunner syndrome. This gene has also been associated with a variety of other psychiatric disorders, including antisocial behavior. Alternatively spliced transcript variants encoding multiple isoforms have been observed. Structures Gene Monoamine oxidase A, also known as MAO-A, is an enzyme that in humans is encoded by the ''MAOA'' gene. The promoter of ''MAOA'' contains conserved binding sites for Sp1, GATA2, and TBP. This gene is adjacent to a related gene (''MAOB'') on the opposite strand of the X chromosome. In humans, there is a 30-base repeat sequence repeated several different numbers of times in the promoter region of MAO-A. There are 2R ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
AOF2
Lysine-specific histone demethylase 1A (LSD1) also known as lysine (K)-specific demethylase 1A (KDM1A) is a protein in humans that is encoded by the KDM1A gene. LSD1 is a flavin-dependent monoamine oxidase, which can demethylate mono- and di-methylated lysines, specifically histone 3, lysines 4 and 9 (H3K4 and H3K9). This enzyme can have roles critical in embryogenesis and tissue-specific differentiation, as well as oocyte growth. KDM1A was the first histone demethylase to be discovered though more than 30 have been described. Structure This gene encodes a nuclear protein containing a SWIRM domain, a FAD-binding motif, and an amine oxidase domain. This protein is a component of several histone deacetylase complexes, though it silences genes by functioning as a histone demethylase. Function LSD1 (lysine-specific demethylase 1), also known as KDM1, is the first of several protein lysine demethylases discovered. Through a FAD-dependent oxidative reaction, LSD1 specifically ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
AOF1
Lysine (K)-specific demethylase 1B is a protein that in humans is encoded by the KDM1B gene. Function Flavin-dependent histone demethylases, such as KDM1B, regulate histone lysine methylation, an epigenetic mark that regulates gene expression and chromatin Chromatin is a complex of DNA and protein found in eukaryotic cells. The primary function is to package long DNA molecules into more compact, denser structures. This prevents the strands from becoming tangled and also plays important roles in r ... function. References Further reading * * * * {{gene-6-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Corticosteroid
Corticosteroids are a class of steroid hormones that are produced in the adrenal cortex of vertebrates, as well as the synthetic analogues of these hormones. Two main classes of corticosteroids, glucocorticoids and mineralocorticoids, are involved in a wide range of physiological processes, including stress response, immune response, and regulation of inflammation, carbohydrate metabolism, protein catabolism, blood electrolyte levels, and behavior. Some common naturally occurring steroid hormones are cortisol (), corticosterone (), cortisone () and aldosterone (). (Note that cortisone and aldosterone are isomers.) The main corticosteroids produced by the adrenal cortex are cortisol and aldosterone. Classes * Glucocorticoids such as cortisol affect carbohydrate, fat, and protein metabolism, and have anti-inflammatory, immunosuppressive, anti-proliferative, and vasoconstrictive effects. Anti-inflammatory effects are mediated by blocking the action of inflammatory medi ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Putrescine Oxidase
In enzymology, a putrescine oxidase () is an enzyme that catalyzes the chemical reaction :putrescine + O2 + H2O \rightleftharpoons 4-aminobutanal + NH3 + H2O2 The 3 substrates of this enzyme are putrescine, O2, and H2O, whereas its 3 products are 4-aminobutanal, NH3, and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with oxygen as acceptor. The systematic name of this enzyme class is putrescine:oxygen oxidoreductase (deaminating). This enzyme participates in urea cycle and metabolism of amino groups. It employs one cofactor, FAD A fad or trend is any form of collective behavior that develops within a culture, a generation or social group in which a group of people enthusiastically follow an impulse for a short period. Fads are objects or behaviors that achieve short- .... References * * EC 1.4.3 Flavoproteins Enzymes of unknown structure {{1.4-enzyme-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
