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Prosthetic Groups
A prosthetic group is the non-amino acid component that is part of the structure of the heteroproteins or conjugated proteins, being tightly linked to the apoprotein. Not to be confused with the cosubstrate that binds to the enzyme apoenzyme (either a holoprotein or heteroprotein) by non-covalent binding a non-protein (non-amino acid) This is a component of a conjugated protein that is required for the protein's biological activity. The prosthetic group may be organic (such as a vitamin, sugar, RNA, phosphate or lipid) or inorganic (such as a metal ion). Prosthetic groups are bound tightly to proteins and may even be attached through a covalent bond. They often play an important role in enzyme catalysis. A protein without its prosthetic group is called an apoprotein, while a protein combined with its prosthetic group is called a holoprotein. A non-covalently bound prosthetic group cannot generally be removed from the holoprotein without denaturating the protein. Thus, the ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Conjugated Protein
A conjugated protein is a protein that functions in interaction with other (non-polypeptide) chemical groups attached by covalent bonding or weak interactions. Many proteins contain only amino acids and no other chemical groups, and they are called simple proteins. However, other kind of proteins yield, on hydrolysis, some other chemical component in addition to amino acids and they are called conjugated proteins. The non-amino part of a conjugated protein is usually called its prosthetic group. Most prosthetic groups are formed from vitamins. Conjugated proteins are classified on the basis of the chemical nature of their prosthetic groups. Examples Some examples of conjugated proteins are lipoproteins, glycoproteins, Nucleoproteins, phosphoproteins, hemoproteins, flavoproteins, metalloproteins, phytochromes, cytochromes, opsins, and chromoproteins. Hemoglobin contains the prosthetic group known as heme. Each heme group contains an iron ion (Fe2+) which forms a co-ordinate bo ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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 classified 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. (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, therefore, permanently) bound to a ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Carbonic Anhydrase
The carbonic anhydrases (or carbonate dehydratases) () form a family of enzymes that catalyst, catalyze the interconversion between carbon dioxide and water and the Dissociation (chemistry), dissociated ions of carbonic acid (i.e. bicarbonate and hydrogen ions). The active site of most carbonic anhydrases contains a zinc ion. They are therefore classified as metalloprotein, metalloenzymes. The enzyme maintains Acid–base homeostasis, acid-base balance and helps transport carbon dioxide. Carbonic anhydrase helps maintain acid–base homeostasis, regulate pH, and fluid balance. Depending on its location, the role of the enzyme changes slightly. For example, carbonic anhydrase produces acid in the stomach lining. In the kidney, the control of bicarbonate ions influences the water content of the cell. The control of bicarbonate ions also influences the water content in the eyes. Inhibitors of carbonic anhydrase are used to treat glaucoma, the excessive build-up of water in the eyes ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Zinc
Zinc is a chemical element; it has symbol Zn and atomic number 30. It 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. 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 is the second most abundant trace metal in humans after iron, an import ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cytochrome C Oxidase
The enzyme cytochrome c oxidase or Complex IV (was , now reclassified as a translocasEC 7.1.1.9 is a large transmembrane protein complex found in bacteria, archaea, and the mitochondria of eukaryotes. It is the last enzyme in the Cellular respiration, respiratory electron transport chain of cell (biology), cells located in the membrane. It receives an electron from each of four cytochrome c molecules and transfers them to one oxygen molecule and four protons, producing two molecules of water. In addition to binding the four protons from the inner aqueous phase, it transports another four protons across the membrane, increasing the transmembrane difference of proton electrochemical potential, which the ATP synthase then uses to synthesize Adenosine triphosphate, ATP. Structure The complex The complex is a large integral membrane protein composed of several Cofactor (biochemistry)#Metal ions, metal prosthetic sites and 13 protein subunits in mammals. In mammals, ten subunits a ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Iron
Iron is a chemical element; it has symbol Fe () and atomic number 26. It is a metal that belongs to the first transition series and group 8 of the periodic table. It is, by mass, the most common element on Earth, forming much of Earth's outer and inner core. It is the fourth most abundant element in the Earth's crust, being mainly deposited by meteorites in its metallic state. Extracting usable metal from iron ores requires kilns or furnaces capable of reaching , about 500 °C (900 °F) higher than that required to smelt copper. Humans started to master that process in Eurasia during the 2nd millennium BC and the use of iron tools and weapons began to displace copper alloys – in some regions, only around 1200 BC. That event is considered the transition from the Bronze Age to the Iron Age. In the modern world, iron alloys, such as steel, stainless steel, cast iron and special steels, are by far the most common industrial metals, due to their mechan ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Transition Metal
In chemistry, a transition metal (or transition element) is a chemical element in the d-block of the periodic table (groups 3 to 12), though the elements of group 12 (and less often group 3) are sometimes excluded. The lanthanide and actinide elements (the f-block) are called inner transition metals and are sometimes considered to be transition metals as well. They are lustrous metals with good electrical and thermal conductivity. Most (with the exception of group 11 and group 12) are hard and strong, and have high melting and boiling temperatures. They form compounds in any of two or more different oxidation states and bind to a variety of ligands to form coordination complexes that are often coloured. They form many useful alloys and are often employed as catalysts in elemental form or in compounds such as coordination complexes and oxides. Most are strongly paramagnetic because of their unpaired d electrons, as are many of their compounds. All of the elements that are ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Biotin
Biotin (also known as vitamin B7 or vitamin H) is one of the B vitamins. It is involved in a wide range of metabolic processes, both in humans and in other organisms, primarily related to the utilization of fats, carbohydrates, and amino acids. The name ''biotin'', borrowed from the German , derives from the Ancient Greek word (; 'life') and the suffix "-in" (a suffix used in chemistry usually to indicate 'forming'). Biotin appears as a white, needle-like crystalline solid. Chemical description Biotin is classified as a heterocyclic compound, with a sulfur-containing tetrahydrothiophene ring fused to a ureido group. A C5-carboxylic acid side chain is appended to the former ring. The ureido ring, containing the −N−CO−N− group, serves as the carbon dioxide carrier in carboxylation reactions. Biotin is a coenzyme for five carboxylase enzymes, which are involved in the catabolism of amino acids and fatty acids, synthesis of fatty acids, and gluconeogenesis. Biotinylat ... [...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 result ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Thiamine Pyrophosphate
Thiamine pyrophosphate (TPP or ThPP), or thiamine diphosphate (ThDP), or cocarboxylase is a thiamine (vitamin B1) derivative which is produced by the enzyme thiamine diphosphokinase. Thiamine pyrophosphate is a cofactor that is present in all living systems, in which it catalyzes several biochemical reactions. Thiamine pyrophosphate is synthesized in the cytosol and is required in the cytosol for the activity of transketolase and in the mitochondria for the activity of pyruvate-, oxoglutarate- and branched chain keto acid dehydrogenases. To date, the yeast ThPP carrier (Tpc1p) the human Tpc and the ''Drosophila melanogaster'' have been identified as being responsible for the mitochondrial transport of ThPP and ThMP. It was first discovered as an essential nutrient (vitamin) in humans through its link with the peripheral nervous system disease beriberi, which results from a deficiency of thiamine in the diet. TPP works as a coenzyme in many enzymatic reactions, such as: * Pyru ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Hemoglobin
Hemoglobin (haemoglobin, Hb or Hgb) is a protein containing iron that facilitates the transportation of oxygen in red blood cells. Almost all vertebrates contain hemoglobin, with the sole exception of the fish family Channichthyidae. Hemoglobin in the blood carries oxygen from the respiratory organs (lungs or gills) to the other tissues of the body, where it releases the oxygen to enable aerobic respiration which powers an animal's metabolism. A healthy human has 12to 20grams of hemoglobin in every 100mL of blood. Hemoglobin is a metalloprotein, a chromoprotein, and a globulin. In mammals, hemoglobin makes up about 96% of a red blood cell's dry matter, dry weight (excluding water), and around 35% of the total weight (including water). Hemoglobin has an oxygen-binding capacity of 1.34mL of O2 per gram, which increases the total blood oxygen capacity seventy-fold compared to dissolved oxygen in blood plasma alone. The mammalian hemoglobin molecule can bind and transport up to four ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Heme
Heme (American English), or haem (Commonwealth English, both pronounced /Help:IPA/English, hi:m/ ), is a ring-shaped iron-containing molecule that commonly serves as a Ligand (biochemistry), ligand of various proteins, more notably as a Prosthetic group, component of hemoglobin, which is necessary to bind oxygen in the bloodstream. It is composed of four pyrrole rings with 2 Vinyl group, vinyl and 2 propionic acid side chains. Heme is biosynthesized in both the bone marrow and the liver. Heme plays a critical role in multiple different redox reactions in mammals, due to its ability to carry the oxygen molecule. Reactions include oxidative metabolism (cytochrome c oxidase, succinate dehydrogenase), xenobiotic detoxification via cytochrome P450 pathways (including Drug metabolism, metabolism of some drugs), gas sensing (Guanylate cyclase, guanyl cyclases, nitric oxide synthase), and microRNA processing (DGCR8). Heme is a coordination complex "consisting of an iron ion coordinated ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
