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Histidine

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histidine (hĭs`tĭdēn), organic compound, one of the 22 α-amino acids amino acid , any one of a class of simple organic compounds containing carbon, hydrogen, oxygen, nitrogen, and in certain cases sulfur. These compounds are the building blocks of proteins.
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 commonly found in animal proteins. Only the l-stereoisomer appears in mammalian protein. Histidine is the direct precursor of histamine histamine , organic compound derived in the body from the amino acid histidine by the removal of a carboxyl group (COOH). Although found in many plant and animal tissues, histamine is specifically important in human physiology because it is one of the chemicals
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; it is also an important source of carbon atoms in the synthesis of purines purine, type of organic base found in the nucleotides and nucleic acids of plant and animal tissue. The German chemist Emil Fischer did much of the basic work on purines and introduced the term into the chemical literature in the early 20th cent.
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. The imidazole group on the side chain of histidine can act as both an acid and a base, i.e., it can both donate and accept protons under some conditions. This turns out to be an important property when histidine is incorporated into proteins protein, any of the group of highly complex organic compounds found in all living cells and comprising the most abundant class of all biological molecules. Protein comprises approximately 50% of cellular dry weight.
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, particularly when it becomes a part of the primary structure of some enzymes enzyme, biological catalyst. The term enzyme comes from zymosis, the Greek word for fermentation, a process accomplished by yeast cells and long known to the brewing industry, which occupied the attention of many 19th-century chemists.
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. It is thought that the side chain of this amino acid acts as a general acid and base as it participates in the catalytic functions of chymotrypsin chymotrypsin , proteolytic, or protein-digesting, enzyme active in the mammalian intestinal tract. It catalyzes the hydrolysis of proteins, degrading them into smaller molecules called peptides. Peptides are further split into free amino acids.
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, as well as those of a number of enzymes dealing with the metabolism of carbohydrates, proteins, and nucleic acids. It has even been implicated in the workings of cocoonase, the enzyme that allows adult silk moths to escape from their cocoons. Histidine is considered to be an essential amino acid for infants (it must be supplied in the diet); experiments with adults indicate that they can go for at least short periods without dietary intake of this amino acid. It was isolated from protein in 1896; its structure was confirmed by chemical synthesis in 1911.

histidine

One of the essential amino acids, first isolated in 1896. It occurs abundantly in hemoglobin and can be isolated from blood cells. It is used in medicine and biochemical research and as a dietary supplement and feed additive.


histidine [′his·tə‚dēn]
(biochemistry)
C6H9O2N3A crystalline basic amino acid present in large amounts in hemoglobin and resulting from the hydrolysis of most proteins.

Histidine 

(α-amino-β-imidazole-propionic acid):

an amino acid with basic characteristics, essential in many animals; the human body is capable of limited synthesis of histidine. It is one of the ingredients of the active centers of many enzymes, in particular of ribonuclease and transketolase. The initial stage of the enzymatic destruction of histidine in the body is the splitting off of ammonia, with the formation of urocanic acid, which is discharged in the urine. The deamination of histidine is an irreversible reaction and is catalyzed by the enzyme histidine ammonia lyase (histidine-a-deaminase), which is found in the liver of animals and in bacteria. Histidine deficiency leads to many metabolic disturbances, including inhibition of hemoglobin synthesis. Histidine is a precursor of the specific dipeptides of the skeletal musculature—carnosine and anserine. Decarboxylation of histidine leads to the formation of the biologically active amine histamine; this process is catalyzed by histidine decarboxylase, an enzyme belonging to the class of lyases. This enzyme acts only on the L-isomer (natural form) of histidine. The reaction is reversibly inhibited by the respiratory inhibitors cyanide, hydroxylamine, and semicarbazide.

A. A. BOLDYREV and E. V. PETUSHKOVA



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It's very important for the newborn to get vital nutrients such as good fats (DHA and EPA) for brain development, immune system protectors, digestible protein, the amino acids argenine and histidine plus many others as soon as possible to start the process of total body development.
If the EPR spectra of Cu(II)-bound H86A frataxin loses the signal for histidine coordination, this will indicate the location of one potential iron binding site.
Bogoch called them "Replikins," and they are strictly defined by the concentration of lysine and histidine residues and the spacing between them.
 
 
 
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