Clinical Name Uses

Biotin Necessary for metabolism Also known as Vitamin H Has been linked tangentially as a treatment for baldness

Soluble(Fat or Water) Water

Foods this Vitamin is liver Found In kidneys egg yolk

Biotin, also known as Vitamin H or Coenzyme R[2], is a water-soluble B-complex vitamin (vitamin B7). It is composed of a ureido (tetrahydroimidizalone) ring fused with a tetrahydrothiophene ring. A valeric acid substituent is attached to one of the carbon atoms of the tetrahydrothiophene ring. Biotin is a coenzyme in the synthesis of fatty acids, isoleucine, and valine, and it plays a role in gluconeogenesis General overview
Biotin is necessary for cell growth, the production of fatty acids, and the metabolism of fats and amino acids. It plays a role in the citric acid cycle, which is the process by which biochemical energy is generated during aerobic respiration. Biotin not only assists in various metabolic reactions but also helps to transfer carbon dioxide. Biotin may also be helpful in maintaining a steady blood sugar level.[3] Biotin is often recommended for strengthening hair and nails.[citation needed] As a consequence, it is found in many cosmetics and health products for the hair and skin, though it cannot be absorbed through the hair or skin it self.[citation needed]

Biosynthesis
The Empirical formula of Biotin is (C10 H16 O3 N2 S). Biotin has an unusual structure. It has two side rings fused together. The two side rings are imidazole and thiophene. Biotin is a heterocyclic S-containing (mono-)carboxylic acid. Biotin is made from two precursors, alanine and pimeloyl-CoA via three enzymes. 8-Amino-7-oxopelargonic acid synthase is a pyridoxal 5'-phosphate enzyme. The pimeloyl-CoA, could be produced by a modified fatty acid pathway involving a malonyl thioester as the starter. 7,8-Diaminopelargonic acid (DAPA) aminotransferase, is unusual in using S-adenosylmethionine (AdoMet) as the NH2

donor. Dethiobiotin synthethase catalyzes the formation of the ureido ring via a DAPA carbamate activated with ATP. Biotin synthase reductively cleaves AdoMet into a deoxyadenosyl radical -- a first radical formed on dethiobiotin is trapped by the sulfur donor, which was found to be the iron-sulfur (Fe-S) center contained in the enzyme.[6]

Cofactor biochemistry
D-(+)-Biotin is a cofactor responsible for carbon dioxide transfer

in several carboxylase

enzymes:

Acetyl-CoA carboxylase alpha Acetyl-CoA carboxylase beta Methylcrotonyl-CoA carboxylase Propionyl-CoA carboxylase Pyruvate carboxylase

It is important in fatty acid synthesis, branched-chain amino acid catabolism, and gluconeogenesis. Biotin covalently attaches to the epsilon-amino group of specific lysine residues in these carboxylases. This biotinylation reaction requires ATP and is catalyzed by holocarboxylase synthetase.[7] The attachment of biotin to various chemical sites can be used as an important laboratory technique to study various processes including protein localization, protein interactions, DNA transcription, and replication. Biotinidase itself is known to be able to biotinylate histone proteins,[8] but little biotin is found naturally attached to chromatin. Biotin binds very tightly to the tetrameric protein avidin (also streptavidin and neutravidin), with a dissociation constant Kd in the order of 1015, which is one of the strongest known protein-ligand interactions, approaching the covalent bond in strength.[9] This is often used in different biotechnological applications. Until 2005, very harsh conditions were thought to be required to break the biotin-streptavidin bond.[10]
citation needed]

Sources of biotin
Biotin is consumed from a wide range of food sources in the diet, however there are few particularly rich sources. Foods with a relatively high biotin content include Swiss chard, raw egg yolk (however, the consumption of egg whites with egg yolks minimizes the effectiveness of egg yolk's biotin in one's body), liver, some vegetables[citation needed][vague], and peanuts. The dietary biotin intake in Western populations has been estimated to be 35 to 70 g/d (143287 nmol/d).[11] Biotin is also available from supplements. The synthetic process developed by Leo Sternbach and Moses Wolf Goldberg in the 1940s uses fumaric acid as a starting material.

Factors that affect biotin requirements

The frequency of marginal biotin status is not known, but the incidence of low circulating biotin levels in alcoholics has been found to be much greater than in the general population. Also, relatively low levels of biotin have been reported in the urine or plasma of patients that have had partial gastrectomy or that have other causes of achlorhydria, burn patients, epileptics, elderly individuals, and athletes.[14] Pregnancy and lactation may be associated with an increased demand for biotin. In pregnancy, this may be due to a possible acceleration of biotin catabolism, whereas, in lactation, the higher demand has yet to be elucidated. Recent studies have shown that marginal biotin deficiency can be present in human gestation, as evidenced by increased urinary excretion of 3-hydroxyisovaleric acid, decreased urinary excretion of biotin and bisnorbiotin, and decreased plasma concentration of biotin. Additionally, smoking may further accelerate biotin catabolism in women.[15]

[edit] Deficiency
Biotin deficiency is rare because, in general, intestinal bacteria produce biotin in excess of the body's daily requirements. Biotin deficiency is relatively rare and mild, and can be addressed with supplementation. Such deficiency can be caused by the consumption of raw egg whites (eating two or more uncooked egg whites daily for several months has caused biotin deficiency that is serious enough to produce symptoms [1]), which contain high levels of the protein avidin, which binds biotin strongly. Symptoms of biotin deficiency include: Hair loss (alopecia) Conjunctivitis Dermatitis in the form of a scaly red rash around the eyes, nose, mouth, and genital area. Neurological symptoms in adults such as depression, lethargy, hallucination, and numbness and tingling of the extremities

Biotin[1]

IUPAC name[hide] 5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4yl]pentanoic acid Other names[hide] Vitamin B7; Vitamin H; Coenzyme R; Biopeiderm

CAS number PubChem ChemSpider UNII DrugBank KEGG ChEBI ChEMBL ATC code Jmol-3D images
[show]

Identifiers 58-85-5 171548 149962 6SO6U10H04 DB00121 D00029 CHEBI:15956 CHEMBL857 A11HA05 Image 1 Image 2 SMILES

InChI
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Molecular formula Molar mass Appearance Melting point Solubility in water

Properties C10H16N2O3S 244.31 g mol1 White crystalline needles 232-233 C 22 mg/100 mL (verify) (what is: / ?) Except where noted otherwise, data are given for materials in their standard state (at 25 C, 100 kPa) Infobox references