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Lysine 2,3-aminomutase
Lysine 2,3-aminomutase (KAM or LAM) () is a radical SAM enzyme that facilitates the conversion of the amino acid lysine to beta-lysine. It accomplishes this interconversion using three cofactors and a 5'- deoxyadenosyl radical formed in a S-Adenosyl methionine (SAM) activated radical reaction pathway. /sup> The generalized reaction is shown below: Structure Shown on the right is the three-dimensional structure of the Lysine 2,3-aminomutase protein. The structure was determined by X-ray crystallography to 2.1 Angstrom resolution and was seen to crystallize as a homotetramer. /sup> KAM was first purified and characterized in '' Clostridium subterminale'' for studies of Lysine metabolism. Cofactors Four key cofactors are required for the reaction catalyzed by the lysine 2,3-aminomutase enzyme. They are: * S-Adenosyl methionine (SAM): Helps generate the radical intermediate by borrowing an electron. * Pyridoxal phosphate (PLP): Responsible for binding of the amino acid duri ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Radical SAM
Radical SAM is a designation for a superfamily of enzymes that use a +_cluster.html" ;"title="Fe-4Ssup>+ cluster">Fe-4Ssup>+ cluster to reductively cleave ''S''-adenosyl-L-methionine (SAM) to generate a radical, usually a 5′-deoxyadenosyl radical (5'-dAdo), as a critical intermediate. These enzymes utilize this radical intermediate to perform diverse transformations, often to functionalize unactivated C-H bonds. Radical SAM enzymes are involved in cofactor biosynthesis, enzyme activation, peptide modification, post-transcriptional and post-translational modifications, metalloprotein cluster formation, tRNA modification, lipid metabolism, biosynthesis of antibiotics and natural products etc. The vast majority of known radical SAM enzymes belong to the radical SAM superfamily, and have a cysteine-rich motif that matches or resembles CxxxCxxC. rSAMs comprise the largest superfamily of metal-containing enzymes. History and mechanism As of 2001, 645 unique radical SAM enzymes ha ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Iron-sulfur Cluster
Iron–sulfur proteins (or iron–sulphur proteins in British spelling) are proteins characterized by the presence of iron–sulfur clusters containing sulfide-linked di-, tri-, and tetrairon centers in variable oxidation states. Iron–sulfur clusters are found in a variety of metalloproteins, such as the ferredoxins, as well as NADH dehydrogenase, hydrogenases, coenzyme Q – cytochrome c reductase, succinate – coenzyme Q reductase and nitrogenase. Iron–sulfur clusters are best known for their role in the oxidation-reduction reactions of electron transport in mitochondria and chloroplasts. Both Complex I and Complex II of oxidative phosphorylation have multiple Fe–S clusters. They have many other functions including catalysis as illustrated by aconitase, generation of radicals as illustrated by SAM-dependent enzymes, and as sulfur donors in the biosynthesis of lipoic acid and biotin. Additionally, some Fe–S proteins regulate gene expression. Fe–S proteins are ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Zinc
Zinc is a chemical element with the symbol Zn and atomic number 30. Zinc is a slightly brittle metal at room temperature and has a shiny-greyish appearance when oxidation is removed. It is the first element in group 12 (IIB) of the periodic table. In some respects, zinc is chemically similar to magnesium: both elements exhibit only one normal oxidation state (+2), and the Zn2+ and Mg2+ ions are of similar size.The elements are from different metal groups. See periodic table. Zinc is the 24th most abundant element in Earth's crust and has five stable isotopes. The most common zinc ore is sphalerite (zinc blende), a zinc sulfide mineral. The largest workable lodes are in Australia, Asia, and the United States. Zinc is refined by froth flotation of the ore, roasting, and final extraction using electricity ( electrowinning). Zinc is an essential trace element for humans, animals, plants and for microorganisms and is necessary for prenatal and postnatal development. It ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Pyridoxal Phosphate
Pyridoxal phosphate (PLP, pyridoxal 5'-phosphate, P5P), the active form of vitamin B6, is a coenzyme in a variety of enzymatic reactions. The International Union of Biochemistry and Molecular Biology has catalogued more than 140 PLP-dependent activities, corresponding to ~4% of all classified activities. The versatility of PLP arises from its ability to covalently bind the substrate, and then to act as an electrophilic catalyst, thereby stabilizing different types of carbanionic reaction intermediates. Role as a coenzyme PLP acts as a coenzyme in all transamination reactions, and in certain decarboxylation, deamination, and racemization reactions of amino acids. The aldehyde group of PLP forms a Schiff-base linkage (internal aldimine) with the ε-amino group of a specific lysine group of the aminotransferase enzyme. The α-amino group of the amino acid substrate displaces the ε-amino group of the active-site lysine residue in a process known as transaldimination. The resulting ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Pyridoxal-phosphate
Pyridoxal phosphate (PLP, pyridoxal 5'-phosphate, P5P), the active form of vitamin B6, is a coenzyme in a variety of enzymatic reactions. The International Union of Biochemistry and Molecular Biology has catalogued more than 140 PLP-dependent activities, corresponding to ~4% of all classified activities. The versatility of PLP arises from its ability to covalently bind the substrate, and then to act as an electrophilic catalyst, thereby stabilizing different types of carbanionic reaction intermediates. Role as a coenzyme PLP acts as a coenzyme in all transamination reactions, and in certain decarboxylation, deamination, and racemization reactions of amino acids. The aldehyde group of PLP forms a Schiff-base linkage (internal aldimine) with the ε-amino group of a specific lysine group of the aminotransferase enzyme. The α-amino group of the amino acid substrate displaces the ε-amino group of the active-site lysine residue in a process known as transaldimination. The resulting ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Clostridium
''Clostridium'' is a genus of anaerobic, Gram-positive bacteria. Species of ''Clostridium'' inhabit soils and the intestinal tract of animals, including humans. This genus includes several significant human pathogens, including the causative agents of botulism and tetanus. It also formerly included an important cause of diarrhea, ''Clostridioides difficile'', which was reclassified into the ''Clostridioides'' genus in 2016. History In the late 1700s, Germany experienced a number of outbreaks of an illness that seemed connected to eating certain sausages. In 1817, the German neurologist Justinus Kerner detected rod-shaped cells in his investigations into this so-called sausage poisoning. In 1897, the Belgian biology professor Emile van Ermengem published his finding of an endospore-forming organism he isolated from spoiled ham. Biologists classified van Ermengem's discovery along with other known gram-positive spore formers in the genus ''Bacillus''. This classification prese ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
KAM Labeled Reaction1
Kaam (Gurmukhi: ਕਾਮ ''Kāma'') in common usage, the term stands for 'excessive passion for sexual pleasure' and it is in this sense that it is considered to be an evil in Sikhism. In Sikhism it is believed that Kaam can be overcome by being satisfied with the current moment. All 5 thieves can be overcome with selfless service and remembrance of God (Simran). Sikh Guru teachings The Gurus rejected lust. Yet they recognized the four '' Purusarthas''—referred to in Gurbani as ''char Padaraths'', or the four human pursuits—as the Granth Sahib declares "Dharma, Artha, Kam and Moksha follow God's devotee like shadow" (SGGS 1320). However, in Sikhism, Kaam is not unrestricted gratification of carnal desires, but an impulse which needs to be kept under check like other impulses and passions. Unrestrained propensity towards Kam, especially sexual relationship outside the marital bond, is condemned in the strongest terms in Sikh codes of conduct as well as in the Scriptu ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Enzyme
Enzymes () are proteins that act as biological catalysts by accelerating chemical reactions. The molecules upon which enzymes may act are called substrates, and the enzyme converts the substrates into different molecules known as products. Almost all metabolic processes in the cell need enzyme catalysis in order to occur at rates fast enough to sustain life. Metabolic pathways depend upon enzymes to catalyze individual steps. The study of enzymes is called ''enzymology'' and the field of pseudoenzyme analysis recognizes that during evolution, some enzymes have lost the ability to carry out biological catalysis, which is often reflected in their amino acid sequences and unusual 'pseudocatalytic' properties. Enzymes are known to catalyze more than 5,000 biochemical reaction types. Other biocatalysts are catalytic RNA molecules, called ribozymes. Enzymes' specificity comes from their unique three-dimensional structures. Like all catalysts, enzymes increase the reaction ra ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
S-Adenosyl Methionine
''S''-Adenosyl methionine (SAM), also known under the commercial names of SAMe, SAM-e, or AdoMet, is a common cosubstrate involved in methyl group transfers, transsulfuration, and aminopropylation. Although these anabolic reactions occur throughout the body, most SAM is produced and consumed in the liver. More than 40 methyl transfers from SAM are known, to various substrates such as nucleic acids, proteins, lipids and secondary metabolites. It is made from adenosine triphosphate (ATP) and methionine by methionine adenosyltransferase. SAM was first discovered by Giulio Cantoni in 1952. In bacteria, SAM is bound by the SAM riboswitch, which regulates genes involved in methionine or cysteine biosynthesis. In eukaryotic cells, SAM serves as a regulator of a variety of processes including DNA, tRNA, and rRNA methylation; immune response; amino acid metabolism; transsulfuration; and more. In plants, SAM is crucial to the biosynthesis of ethylene, an important plant hormone and sig ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Deoxyadenosyl
A deoxyadenosyl radical is a free radical that is structurally related to adenosine by removal of a 5′-hydroxy group from adenosine. This radical occurs in nature as a reactive intermediate. It is generated by radical SAM enzymes and by some varieties of vitamin B12. The deoxyadenosyl radical abstracts hydrogen atoms from substrates, causing rearrangements and other post transcriptional modification Transcriptional modification or co-transcriptional modification is a set of biological processes common to most eukaryotic cells by which an RNA primary transcript is chemically altered following transcription from a gene to produce a mature, func ...s required for biosynthesis.{{cite journal, authors=Broderick, J. B.; Duffus, B. R.; Duschene, K. S.; Shepard, E. M. , title=Radical ''S''-Adenosylmethionine Enzymes, journal=Chemical Reviews, year=2014, volume=114, issue=8, pages=4229–4317, doi= 10.1021/cr4004709, pmid=24476342, pmc=4002137 References Enzymes Free radicals ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
