isoprenoid

Vitamin K denotes a group of 2-methilo-naphthoquinone derivatives. They are human vitamins, lipophilic (i.e., soluble in lipids) and therefore hydrophobic (i.e., insoluble in water). They are needed for the posttranslational modification of certain proteins, mostly required for blood coagulation. Normally it is produced by bacteria in the intestines, and dietary deficiency is extremely rare unless the intestines are heavily damaged. Vitamin K - Chemical structure. Vitamin K is a group name for a numb ...

Including:

• Vitamin K - Chemical structure
• Vitamin K - Physiology
• Vitamin K - Role in disease
• Vitamin K - History
• Vitamin K - Discovery
• Vitamin K - Gla-proteins

Read more here: » Vitamin K: Encyclopedia - Vitamin K

Coenzyme Q (CoQ), also known as ubiquinone or ubiquinol, is a biologically active quinone with an isoprenoid side chain, related in structure to vitamin K and vitamin E. Coenzyme Q - History. Coenzyme Q was first discovered in 1957 by professor F. L. Crane and colleagues at the University of Wisconsin Enzyme Institute. In 1958, its chemical structure was reported by Dr. D.E. Wolf and a research group at Merck Laboratories led by Dr. Karl Folkers. Coenzyme Q - Chemi ...

Including:

• Coenzyme Q - History
• Coenzyme Q - Chemical properties
• Coenzyme Q - Biochemical role
• Coenzyme Q - Supplementation
• Coenzyme Q - Synthesis and Its Inhibition by Statins

Read more here: » Coenzyme Q: Encyclopedia - Coenzyme Q

Vitamin K is a group name for a number of related compounds, which have in common a methylated naphthoquinone ring structure, and which vary in the aliphatic side chain attached at the 3-position (see figure 1). Phylloquinone (also known as vitamin K1) invariably contains in its side chain four isoprenoid residues, one of which is unsaturated. Menaquinones have side chains composed of a variable number of unsaturated isoprenoid residues; generally they are designated as MK ...

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Vitamin K, Vitamin K - Chemical structure, Vitamin K - Physiology, Vitamin K - Role in disease, Vitamin K - History, Vitamin K - Discovery, Vitamin K - Gla-proteins

Read more here: » Vitamin K: Encyclopedia II - Vitamin K - Chemical structure

Details of heme synthesis can be found in the article on porphyrin. The enzymatic process that produces heme is properly called porphyrin synthesis, as all the intermediates are tetrapyrroles that are chemically classified are porphyrins. The process is highly conserved across biology. In humans, this pathway serves almost exclusively to form heme. In other species, it also produces similar substance ...

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Heme, Heme - Types, Heme - Function, Heme - Synthesis, Heme - Genes

Read more here: » Heme: Encyclopedia II - Heme - Synthesis

Because of its ability to transfer electrons and therefore act as an antioxidant, Coenzyme Q has become a fashionable dietary supplement. Young people are able to make Q10 from the lower numbered ubiquinones such as Q6 or Q8. The sick and elderly may not be able to make enough. Q10 thus becomes a vitamin later in life and in illness. Supplementation of Coenzyme Q10 has been found to have a beneficial effect on the condition of some sufferers of migraines, and is a common component of the "mito cocktail" used to treat mitochondr ...

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Coenzyme Q, Coenzyme Q - History, Coenzyme Q - Chemical properties, Coenzyme Q - Biochemical role, Coenzyme Q - Supplementation, Coenzyme Q - Synthesis and Its Inhibition by Statins

Read more here: » Coenzyme Q: Encyclopedia II - Coenzyme Q - Supplementation

Archaea are similar to other prokaryotes in most aspects of cell structure and metabolism. However, their genetic transcription and translation — the two central processes in molecular biology — do not show the typical bacterial features, but are extremely similar to those of eukaryotes. For instance, archaean translation uses eukaryotic initiation and elongation factors, and their transcription ...

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Archaea, Archaea - History, Archaea - Archaea Bacteria and Eukaryotes, Archaea - Habitats, Archaea - Form, Archaea - Evolution and classification

Read more here: » Archaea: Encyclopedia II - Archaea - Archaea Bacteria and Eukaryotes

Vitamin K is involved in the carboxylation of certain glutamate residues in proteins to form gamma-carboxyglutamate residues (abbreviated Gla-residues). Gla-residues are usually involved in binding calcium. The Gla-residues are essential for the biological activity of all known Gla-proteins. At this time fewer than 12 human Gla-proteins have been discovered, and they play key roles in the regulation of three physiological processes: blood coagulation (prothrombin (factor II), factors VII, IX, X, protein C, protein S and protein Z) bone meta ...

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Vitamin K, Vitamin K - Chemical structure, Vitamin K - Physiology, Vitamin K - Role in disease, Vitamin K - History, Vitamin K - Discovery, Vitamin K - Gla-proteins

Read more here: » Vitamin K: Encyclopedia II - Vitamin K - Physiology

The main function of heme is the retention of O2 and delivering it for enzymatic reactions. The iron atom of every heme group can bind one molecule of O2. As the main site of oxidation in the cell is the mitochondrion, many heme-containing enzymes are located there, and part of the heme synthesis (see below) takes place there. Hemoglobin is not an enzyme, but a transporter. It binds oxygen in the pulmonary vasculature, where the pH is high and the pCO2 is low, and releases it in the tissues, where the ...

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Heme, Heme - Types, Heme - Function, Heme - Synthesis, Heme - Genes

Read more here: » Heme: Encyclopedia II - Heme - Function

There are three biologically important kinds of heme. The most common type is heme b; the others are heme a and heme c. Heme b is not covalently bound to the containing protein (known as apoprotein) in which it is found. It is the most abundant heme: both hemoglobin and myoglobin are examples of proteins that contain heme b. Heme a differs from heme b in that a methyl side chain is oxidized into a formyl group, and one of the vinyl side chains has been replaced by an isoprenoid chain. ...

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Heme, Heme - Types, Heme - Function, Heme - Synthesis, Heme - Genes

Read more here: » Heme: Encyclopedia II - Heme - Types

The oxidized structure of CoQ, or Q, is given here: The various kinds of Coenzyme Q can be distinguished by the number of isoprenoid side chains they have. The most common CoQ in human mitochondria is Q10. The image above has three isoprenoid units and would be called Q3. If Coenzyme Q is reduced by one equivalent, the following structure results, a ubisemiquinone, and is denoted QH. Note the free radical on one of the ring oxygens. If Coenzyme Q is reduced by two equivalents, the compound becomes a ubi ...

See also:

Coenzyme Q, Coenzyme Q - History, Coenzyme Q - Chemical properties, Coenzyme Q - Biochemical role, Coenzyme Q - Supplementation, Coenzyme Q - Synthesis and Its Inhibition by Statins

Read more here: » Coenzyme Q: Encyclopedia II - Coenzyme Q - Chemical properties