Amine Oxidase (copper-containing)
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Amine Oxidase (copper-containing)
Amine oxidase (copper-containing) (AOC) ( and ; formerly ) is a family of amine oxidase enzymes which includes both primary-amine oxidase and diamine oxidase; these enzymes catalyze the oxidation of a wide range of biogenic amines including many neurotransmitters, histamine and xenobiotic amines. They act as a disulphide-linked homodimer. They catalyse the oxidation of primary amines to aldehydes, with the subsequent release of ammonia and hydrogen peroxide, which requires one copper ion per subunit and topaquinone as cofactor: :RCH2NH2 + H2O + O2 \rightleftharpoons RCHO + NH3 + H2O2 The 3 substrates of this enzyme are primary amines (RCH2NH2), H2O, and O2, whereas its 3 products are RCHO, NH3, and H2O2. Copper-containing amine oxidases are found in bacteria, fungi, plants and animals. In prokaryotes, the enzyme enables various amine substrates to be used as sources of carbon and nitrogen. This enzyme belongs to oxidoreductases, specifically those acting on the CH-NH2 ...
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Hansenula Polymorpha
''Ogataea polymorpha'' is a methylotrophic yeast with unusual characteristics. It is used as a protein factory for pharmaceuticals. ''Ogataea polymorpha'' belongs to a limited number of methylotrophic yeast species – yeasts that can grow on methanol. The range of methylotrophic yeasts includes ''Candida boidinii'', ''Pichia methanolica'', ''Pichia pastoris'' and ''Ogataea polymorpha''. ''O. polymorpha'' is taxonomically a species of the family Saccharomycetaceae. Strains Three ''O. polymorpha'' strains, identified in the 1950s, are known. They have unclear relationships and are of independent origins. They are found in soil samples, the gut of insects or in spoiled concentrated orange juice. They exhibit different features and are used in basic research and to recombinant protein production: *strain CBS4732 (CCY38-22-2; ATCC34438, NRRL-Y-5445) *strain DL-1 (NRRL-Y-7560; ATCC26012) *strain NCYC495 (CBS1976; ATAA14754, NRLL-Y-1798) Strains CBS4732 and NCYY495 can be mated wher ...
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Histidine Residue
Histidine (symbol His or H) is an essential amino acid that is used in the biosynthesis of proteins. It contains an α-amino group (which is in the protonated –NH3+ form under biological conditions), a carboxylic acid group (which is in the deprotonated –COO− form under biological conditions), and an imidazole side chain (which is partially protonated), classifying it as a positively charged amino acid at physiological pH. Initially thought essential only for infants, it has now been shown in longer-term studies to be essential for adults also. It is encoded by the codons CAU and CAC. Histidine was first isolated by Albrecht Kossel and Sven Gustaf Hedin in 1896. It is also a precursor to histamine, a vital inflammatory agent in immune responses. The acyl radical is histidyl. Properties of the imidazole side chain The conjugate acid (protonated form) of the imidazole side chain in histidine has a p''K''a of approximately 6.0. Thus, below a pH of 6, the imidazole ring is ...
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Topaquinone
Topaquinone (TPQ) is a redox cofactor derived from the amino acid tyrosine. Its name derives from 2,4,5-trihydroxyphenylalanine-quinone. Its structure was first identified in 1990.{{Cite journal, title = Structure and biogenesis of topaquinone and related cofactors , journal = Journal of Biological Inorganic Chemistry , date = Feb 1999, issn = 0949-8257, pmid = 10499097, pages = 1–11, volume = 4, issue = 1, first = D. M., last = Dooley, doi = 10.1007/s007750050283 , s2cid = 10104769 It is used by copper amine oxidases which contain a tyrosine residue near the active site. This residue catalyses its own transition, first to dopaquinone -Dopaquinone also known as ''o''-dopaquinone is a metabolite of L-DOPA (L-dihydroxyphenylalanine) and a precursor of melanin. Biosynthesis of melanin occurs in melanocytes, where tyrosine -Tyrosine or tyrosine (symbol Tyr or Y) or 4-hydroxy ... and then to topaquinone, in a Cu2+ dependent manner. References Cofactors Alpha-Amino aci ...
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Redox Cofactor
A cofactor is a non-protein chemical compound or metallic ion that is required for an enzyme's role as a catalyst (a catalyst is a substance that increases the rate of a chemical reaction). Cofactors can be considered "helper molecules" that assist in biochemical transformations. The rates at which these happen are characterized in an area of study called enzyme kinetics. Cofactors typically differ from ligands in that they often derive their function by remaining bound. Cofactors can be divided into two types: inorganic ions and complex organic molecules called coenzymes. Coenzymes are mostly derived from vitamins and other organic essential nutrients in small amounts. (Note that some scientists limit the use of the term "cofactor" for inorganic substances; both types are included here.) Coenzymes are further divided into two types. The first is called a "prosthetic group", which consists of a coenzyme that is tightly (or even covalently) and permanently bound to a protein. ...
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X-ray Crystallography
X-ray crystallography is the experimental science determining the atomic and molecular structure of a crystal, in which the crystalline structure causes a beam of incident X-rays to diffract into many specific directions. By measuring the angles and intensities of these diffracted beams, a crystallographer can produce a three-dimensional picture of the density of electrons within the crystal. From this electron density, the mean positions of the atoms in the crystal can be determined, as well as their chemical bonds, their crystallographic disorder, and various other information. Since many materials can form crystals—such as salts, metals, minerals, semiconductors, as well as various inorganic, organic, and biological molecules—X-ray crystallography has been fundamental in the development of many scientific fields. In its first decades of use, this method determined the size of atoms, the lengths and types of chemical bonds, and the atomic-scale differences among various mat ...
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Pyrroloquinoline Quinone
Pyrroloquinoline quinone (PQQ), also called methoxatin'','' is a redox cofactor and antioxidant. Produced by bacteria, it is found in soil and foods such as kiwifruit, as well as human breast milk. Enzymes using PQQ as a redox cofactor are called quinoproteins and play a variety of redox roles. Quinoprotein glucose dehydrogenase is used a glucose sensor in bacteria. PQQ stimulates growth in bacteria. Eukaryote targets, including mammalian lactate dehydrogenase, are of more interest to health. It is suggested that PQQ taken as a dietary supplement could promote mitochondrial biogenesis via this pathway as well as PGC-1α. History It was discovered by J.G. Hauge as the third redox cofactor after nicotinamide and flavin in bacteria (although he hypothesised that it was naphthoquinone). Anthony and Zatman also found the unknown redox cofactor in alcohol dehydrogenase. In 1979, Salisbury and colleagues as well as Duine and colleagues extracted this prosthetic group from methanol d ...
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Copper
Copper is a chemical element with the symbol Cu (from la, cuprum) and atomic number 29. It is a soft, malleable, and ductile metal with very high thermal and electrical conductivity. A freshly exposed surface of pure copper has a pinkish-orange color. Copper is used as a conductor of heat and electricity, as a building material, and as a constituent of various metal alloys, such as sterling silver used in jewelry, cupronickel used to make marine hardware and coins, and constantan used in strain gauges and thermocouples for temperature measurement. Copper is one of the few metals that can occur in nature in a directly usable metallic form ( native metals). This led to very early human use in several regions, from circa 8000 BC. Thousands of years later, it was the first metal to be smelted from sulfide ores, circa 5000 BC; the first metal to be cast into a shape in a mold, c. 4000 BC; and the first metal to be purposely alloyed with another metal, tin, to create ...
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Cofactor (biochemistry)
A cofactor is a non-protein chemical compound or metallic ion that is required for an enzyme's role as a catalyst (a catalyst is a substance that increases the rate of a chemical reaction). Cofactors can be considered "helper molecules" that assist in biochemical transformations. The rates at which these happen are characterized in an area of study called enzyme kinetics. Cofactors typically differ from ligands in that they often derive their function by remaining bound. Cofactors can be divided into two types: inorganic ions and complex organic molecules called coenzymes. Coenzymes are mostly derived from vitamins and other organic essential nutrients in small amounts. (Note that some scientists limit the use of the term "cofactor" for inorganic substances; both types are included here.) Coenzymes are further divided into two types. The first is called a "prosthetic group", which consists of a coenzyme that is tightly (or even covalently) and permanently bound to a protein. ...
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Alkaloid Biosynthesis Ii
Alkaloids are a class of basic, naturally occurring organic compounds that contain at least one nitrogen atom. This group also includes some related compounds with neutral and even weakly acidic properties. Some synthetic compounds of similar structure may also be termed alkaloids. In addition to carbon, hydrogen and nitrogen, alkaloids may also contain oxygen, sulfur and, more rarely, other elements such as chlorine, bromine, and phosphorus.Chemical Encyclopedia: alkaloids
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Alkaloids are produced by a large variety of organisms including , ,

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 it a polar molecule with a non-polar aromatic beta carbon substituent. It is essential in humans, meaning that the body cannot synthesize it and it must be obtained from the diet. Tryptophan is also a precursor to the neurotransmitter serotonin, the hormone melatonin, and vitamin B3. It is encoded by the codon UGG. Like other amino acids, tryptophan is a zwitterion at physiological pH where the amino group is protonated (–; pKa = 9.39) and the carboxylic acid is deprotonated ( –COO−; pKa = 2.38). Humans and many animals cannot synthesize tryptophan: they need to obtain it through their diet, making it an essential amino acid. Function Amino acids, including tryptophan, are used as building blocks in protein biosynthesis, and proteins are required to sustain life. Many anima ...
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