Showing Metabocard for biotin (BASm0002814)

Common NameBiotin
DescriptionBiotin is an enzyme co-factor present in minute amounts in every living cell. Biotin is also known as coenzyme R and vitamin H or B7. It occurs mainly bound to proteins or polypeptides and is abundant in liver, kidney, pancreas, yeast, and milk. Biotin has been recognized as an essential nutrient. Humans fulfill their biotin requirement through their diet through endogenous reutilization of biotin and perhaps through the capture of biotin generated in the intestinal flora. The utilization of biotin for covalent attachment to carboxylases and its reutilization through the release of carboxylase biotin after proteolytic degradation constitutes the 'biotin cycle'. Biotin deficiency is associated with neurological manifestations, skin rash, hair loss, and metabolic disturbances that are thought to relate to the various carboxylase deficiencies (metabolic ketoacidosis with lactic acidosis). It has also been suggested that biotin deficiency is associated with protein malnutrition, and that marginal biotin deficiency in pregnant women may be teratogenic. Biotin acts as a carboxyl carrier in carboxylation reactions. There are four biotin-dependent carboxylases in mammals: those of propionyl-CoA (PCC), 3-methylcrotonyl-CoA (MCC), pyruvate (PC), and acetyl-CoA carboxylases (isoforms ACC-1 and ACC-2). All but ACC-2 are mitochondrial enzymes. The biotin moiety is covalently bound to the epsilon amino group of a lysine residue in each of these carboxylases in a domain 60-80 amino acids long. The domain is structurally similar among carboxylases from bacteria to mammals. Evidence is emerging that biotin participates in processes other than classical carboxylation reactions. Specifically, novel roles for biotin in cell signalling, gene expression, and chromatin structure have been identified in recent years. Human cells accumulate biotin by using both the sodium-dependent multivitamin transporter and monocarboxylate transporter 1. These transporters and other biotin-binding proteins partition biotin to compartments involved in biotin signalling: cytoplasm, mitochondria, and nuclei. The activity of cell signals such as biotinyl-AMP, Sp1 and Sp3, nuclear factor (NF)-kappaB, and receptor tyrosine kinases depends on biotin supply. Consistent with a role for biotin and its catabolites in modulating these cell signals, greater than 2000 biotin-dependent genes have been identified in various human tissues. Many biotin-dependent gene products play roles in signal transduction and localize to the cell nucleus, consistent with a role for biotin in cell signalling. Posttranscriptional events related to ribosomal activity and protein folding may further contribute to the effects of biotin on gene expression. Finally, research has shown that biotinidase and holocarboxylase synthetase mediate covalent binding of biotin to histones (DNA-binding proteins), affecting chromatin structure; at least seven biotinylation sites have been identified in human histones. Biotinylation of histones appears to play a role in cell proliferation, gene silencing, and the cellular response to DNA repair. Roles for biotin in cell signalling and chromatin structure are consistent with the notion that biotin has a unique significance in cell biology (PMID: 15992684 , 16011464 ).
Structure
Molecular FormulaC10H16N2O3S
Average Mass244.31100
Monoisotopic Mass244.08816
IUPAC Name5-[(3aS,4S,6aR)-2-oxo-hexahydro-1H-thieno[3,4-d]imidazolidin-4-yl]pentanoic acid
Traditional NameBiotin
CAS Registry Number58-85-5
SMILESO=C([O-])CCCC[C@@H]1SC[C@@H]2NC(=O)N[C@@H]21
InChI IdentifierInChI=1S/C10H16N2O3S/c13-8(14)4-2-1-3-7-9-6(5-16-7)11-10(15)12-9/h6-7,9H,1-5H2,(H,13,14)(H2,11,12,15)/t6-,7-,9-/m0/s1
InChI KeyYBJHBAHKTGYVGT-ZKWXMUAHSA-N
CHEBI IDCHEBI:57586
HMDB IDHMDB0000030
Pathways
NameSMPDB/PathBank
Alanine, aspartate and glutamate metabolism
Nitrogen metabolism
Pyruvate metabolism
Valine, leucine and isoleucine degradation
Propanoate metabolism
Citric Acid Cycle
Biotin Metabolism
Glutamate Metabolism
Gluconeogenesis
2-Hydroxyglutric Aciduria (D And L Form)
2-Methyl-3-Hydroxybutryl CoA Dehydrogenase Deficiency
3-Hydroxy-3-Methylglutaryl-CoA Lyase Deficiency
3-Methylglutaconic Aciduria Type I
3-Methylglutaconic Aciduria Type III
3-Methylglutaconic Aciduria Type IV
Beta-Ketothiolase Deficiency
Biotinidase Deficiency
Leigh Syndrome
Malonic Aciduria
Maple Syrup Urine Disease
Methylmalonic Aciduria
Methylmalonic Aciduria Due to Cobalamin-Related Disorders
Pyruvate Dehydrogenase Complex Deficiency
Propionic Acidemia
3-Methylcrotonyl Coa Carboxylase Deficiency Type I
Isovaleric Aciduria
4-Hydroxybutyric Aciduria/Succinic Semialdehyde Dehydrogenase Deficiency
Lactic Acidemia
Pyruvate Decarboxylase E1 Component Deficiency (PDHE1 Deficiency)
Hyperinsulinism-Hyperammonemia Syndrome
Pyruvate Carboxylase Deficiency
Primary Hyperoxaluria Type I
Glycogen Storage Disease Type 1A (GSD1A) or Von Gierke Disease
Methylmalonate Semialdehyde Dehydrogenase Deficiency
Homocarnosinosis
Threonine and 2-Oxobutanoate Degradation
Fatty Acid Biosynthesis
Transfer of Acetyl Groups into Mitochondria
Malonyl-coa decarboxylase deficiency
3-hydroxyisobutyric acid dehydrogenase deficiency
3-hydroxyisobutyric aciduria
Isobutyryl-coa dehydrogenase deficiency
Isovaleric acidemia
Congenital lactic acidosis
Fumarase deficiency
Mitochondrial complex II deficiency
2-ketoglutarate dehydrogenase complex deficiency
Pyruvate dehydrogenase deficiency (E3)
Pyruvate dehydrogenase deficiency (E2)
Primary hyperoxaluria II, PH2
Pyruvate kinase deficiency
Phosphoenolpyruvate carboxykinase deficiency 1 (PEPCK1)
Fructose-1,6-diphosphatase deficiency
Triosephosphate isomerase
Multiple carboxylase deficiency, neonatal or early onset form
Succinic semialdehyde dehydrogenase deficiency
Glycogenosis, Type IB
Glycogenosis, Type IC
Glycogenosis, Type IA. Von gierke disease
Warburg Effect
Acylcarnitine 3-Hydroxydecanoylcarnitine
Acylcarnitine (7Z,9Z,12Z,15Z,18Z,21Z)-tetracosa-7,9,12,15,18,21-hexaenoylcarnitine
Acylcarnitine Pentacosanoylcarnitine
Acylcarnitine Hexacosanoylcarnitine
Acylcarnitine (17Z)-Hexacos-17-enoylcarnitine
Acylcarnitine (13Z,16Z)-Hexacosa-13,16-dienoylcarnitine
Acylcarnitine Heptacosanoylcarnitine
Acylcarnitine Octacosanoylcarnitine
Acylcarnitine Nonacosanoylcarnitine
Acylcarnitine (2S,3R)-3-Hydroxy-2-methylbutanoylcarnitine
The oncogenic action of 2-hydroxyglutarate
The Oncogenic Action of Succinate
The Oncogenic Action of Fumarate
Glutaminolysis and Cancer
The oncogenic action of L-2-hydroxyglutarate in Hydroxygluaricaciduria
The oncogenic action of D-2-hydroxyglutarate in Hydroxygluaricaciduria
StateSolid
Water Solubility1.22e+00 g/l
logP0.17
logS-2.30
pKa (Strongest Acidic)4.40
pKa (Strongest Basic)-1.86
Hydrogen Acceptor Count3
Hydrogen Donor Count3
Polar Surface Area78.43 Ų
Rotatable Bond Count5
Physiological Charge-1
Formal Charge0
Refractivity60.05 m³·mol⁻¹
Polarizability24.92

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