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Record Information
Version3.6
Creation Date2005-11-16 15:48:42 UTC
Update Date2014-10-09 18:45:30 UTC
HMDB IDHMDB00030
Secondary Accession NumbersNone
Metabolite Identification
Common NameBiotin
DescriptionBiotin is an enzyme co-factor present in minute amounts in every living cell. Biotin is also known as vitamin H or B7 or coenzyme R. 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. Our biotin requirement is fulfilled in part through diet, through endogenous reutilization of biotin and perhaps through 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. 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 Lys 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 signaling, 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 signaling: 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 signaling. Posttranscriptional events related to ribosomal activity and protein folding may further contribute to 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 signaling and chromatin structure are consistent with the notion that biotin has a unique significance in cell biology. (PMID: 15992684 , 16011464 ).
Structure
Thumb
Synonyms
  1. (+)-Biotin
  2. (+)-cis-Hexahydro-2-oxo-1H-thieno[3,4]imidazole-4-valerate
  3. (+)-cis-Hexahydro-2-oxo-1H-thieno[3,4]imidazole-4-valeric acid
  4. (3aS,4S,6aR)-Hexahydro-2-oxo-1H-thieno[3,4-D]imidazole-4-valerate
  5. (3aS,4S,6aR)-Hexahydro-2-oxo-1H-thieno[3,4-D]imidazole-4-valeric acid
  6. -(+)-biotin
  7. 1swk
  8. 1swn
  9. 1swr
  10. 5-(2-Oxohexahydro-1H-thieno[3,4-D]imidazol-4-yl)pentanoate
  11. 5-(2-Oxohexahydro-1H-thieno[3,4-D]imidazol-4-yl)pentanoic acid
  12. Biodermatin
  13. Bioepiderm
  14. Bios h
  15. Bios II
  16. Biotin
  17. cis-(+)-Tetrahydro-2-oxothieno[3,4]imidazoline-4-valerate
  18. cis-(+)-Tetrahydro-2-oxothieno[3,4]imidazoline-4-valeric acid
  19. cis-Hexahydro-2-oxo-1H-thieno(3,4)imidazole-4-valeric acid
  20. cis-Tetrahydro-2-oxothieno(3,4-D)imidazoline-4-valeric acid
  21. Coenzyme R
  22. D(+)-Biotin
  23. D-(+)-Biotin
  24. D-Biotin
  25. D-Biotin factor S
  26. delta-(+)-Biotin
  27. delta-Biotin
  28. delta-Biotin factor S
  29. Factor S
  30. Factor S (vitamin)
  31. Hexahydro-2-oxo-1H-thieno(3,4-D)imidazole-4-pentanoate
  32. Hexahydro-2-oxo-1H-thieno(3,4-D)imidazole-4-pentanoic acid
  33. Hexahydro-2-oxo-[3aS-(3aa,4b,6aa)]-1H-Thieno[3,4-D]imidazole-4-pentanoate
  34. Hexahydro-2-oxo-[3aS-(3aa,4b,6aa)]-1H-Thieno[3,4-D]imidazole-4-pentanoic acid
  35. Hexahydro-2-oxo-[3as-(3alpha,4beta,6alpha)]-1H-Thieno[3,4-D]imidazole-4-pentanoate
  36. Hexahydro-2-oxo-[3as-(3alpha,4beta,6alpha)]-1H-Thieno[3,4-D]imidazole-4-pentanoic acid
  37. Lutavit H2
  38. Meribin
  39. Rovimix H 2
  40. Vitamin B7
  41. Vitamin H
  42. Vitamin-h
Chemical FormulaC10H16N2O3S
Average Molecular Weight244.311
Monoisotopic Molecular Weight244.088163078
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
SMILES
[H][C@]12CS[C@@H](CCCCC(O)=O)[C@@]1([H])NC(=O)N2
InChI Identifier
InChI=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
Chemical Taxonomy
KingdomOrganic Compounds
Super ClassAliphatic Heteropolycyclic Compounds
ClassThienoimidazolidines
Sub ClassBiotin and Derivatives
Other Descriptors
  • Aliphatic Heteropolycyclic Compounds
  • Heterocyclic Fatty Acids
  • Thia Fatty Acids
Substituents
  • Carboxylic Acid
  • Imidazolidine
  • Imidazolidinone
  • Thioether
  • Thiolane
  • Urea
Direct ParentBiotin and Derivatives
Ontology
StatusDetected and Quantified
Origin
  • Food
Biofunction
  • Component of Biotin metabolism
  • Essential vitamins
Application
  • .
Cellular locations
  • Cytoplasm
  • Extracellular
  • Mitochondria
  • Nucleus
Physical Properties
StateSolid
Experimental Properties
PropertyValueReference
Melting Point232 °CNot Available
Boiling PointNot AvailableNot Available
Water Solubility0.22 mg/mL at 25 °CNot Available
LogPNot AvailableNot Available
Predicted Properties
PropertyValueSource
Water Solubility1.22 g/LALOGPS
logP0.17ALOGPS
logP0.32ChemAxon
logS-2.3ALOGPS
pKa (Strongest Acidic)4.4ChemAxon
pKa (Strongest Basic)-1.9ChemAxon
Physiological Charge-1ChemAxon
Hydrogen Acceptor Count3ChemAxon
Hydrogen Donor Count3ChemAxon
Polar Surface Area78.43ChemAxon
Rotatable Bond Count5ChemAxon
Refractivity60.05ChemAxon
Polarizability24.92ChemAxon
Spectra
SpectraGC-MSLC-MS1D NMR2D NMR
Biological Properties
Cellular Locations
  • Cytoplasm
  • Extracellular
  • Mitochondria
  • Nucleus
Biofluid Locations
  • Blood
  • Cerebrospinal Fluid (CSF)
  • Saliva
  • Urine
Tissue Location
  • All Tissues
  • Prostate
Pathways
NameSMPDB LinkKEGG Link
Biotin MetabolismSMP00066map00780
Normal Concentrations
BiofluidStatusValueAgeSexConditionReferenceDetails
BloodDetected and Quantified0.0034 (0.002 - 0.0051) uMNewborn (0-30 days old)BothNormal
    • Geigy Scientific ...
details
BloodDetected and Quantified0.0016 (0.0009 - 0.0028) uMChildren (1-13 years old)Not SpecifiedNormal
    • Geigy Scientific ...
details
BloodDetected and Quantified0.0024 (0.0008 - 0.0041) uMAdult (>18 years old)FemaleNormal
    • Geigy Scientific ...
details
BloodDetected and Quantified0.00127 +/- 0.00067 uMAdult (>18 years old)BothNormal details
Cerebrospinal Fluid (CSF)Detected and Quantified0.000557 +/- 0.000307 uMAdult (>18 years old)Not SpecifiedNormal details
Cerebrospinal Fluid (CSF)Detected and Quantified0.0005 +/- 0.0002 uMAdult (>18 years old)Not SpecifiedNormal details
SalivaDetected and Quantified0.071 +/- 0.041 uMAdult (>18 years old)BothNormal
    • Dame, ZT. et al. ...
details
UrineDetected and Quantified0.014 (0.002-0.044) umol/mmol creatinineChildren (1-13 years old)BothNormal
    • Geigy Scientific ...
details
UrineDetected and Quantified0.049 +/- 0.035 umol/mmol creatinineAdult (>18 years old)BothNormal details
UrineDetected and Quantified0.023 (0.013-0.032) umol/mmol creatinineAdult (>18 years old)BothNormal details
Abnormal Concentrations
BiofluidStatusValueAgeSexConditionReferenceDetails
Cerebrospinal Fluid (CSF)Detected and Quantified0.08198 (0.00033-0.421) uMNot SpecifiedNot SpecifiedAcute lymphoblastic leukemia details
Cerebrospinal Fluid (CSF)Detected and Quantified0.16 uMNot SpecifiedNot SpecifiedBronchopulmonary dysplasia details
Cerebrospinal Fluid (CSF)Detected and Quantified0.00039 uMNot SpecifiedNot SpecifiedBurkitt's lymphoma details
Cerebrospinal Fluid (CSF)Detected and Quantified0.000447 +/- 0.000217 uMNot SpecifiedNot SpecifiedDementia details
Cerebrospinal Fluid (CSF)Detected and Quantified0.000336 +/- 8.603e-05 uMNot SpecifiedNot SpecifiedEpilepsy details
Cerebrospinal Fluid (CSF)Detected and Quantified0.0229 uMNot SpecifiedNot SpecifiedHead injury details
Cerebrospinal Fluid (CSF)Detected and Quantified0.0273 (0.0247-0.0299) uMNot SpecifiedNot SpecifiedLymphoblastic lymphoma details
Cerebrospinal Fluid (CSF)Detected and Quantified0.000459 +/- 9.0000e-05 uMNot SpecifiedNot SpecifiedMotor neuron disease (MND) details
Cerebrospinal Fluid (CSF)Detected and Quantified0.000324 +/- 0.000107 uMNot SpecifiedNot SpecifiedMultiple sclerosis details
Cerebrospinal Fluid (CSF)Detected and Quantified0.000692 +/- 0.000602 uMNot SpecifiedNot SpecifiedPolyneuropathy details
Cerebrospinal Fluid (CSF)Detected and Quantified0.000438 +/- 0.000156 uMNot SpecifiedNot SpecifiedVascular encephalopathies details
Associated Disorders and Diseases
Disease ReferencesNone
Associated OMIM IDsNone
DrugBank IDDB00121
DrugBank Metabolite IDNot Available
Phenol Explorer Compound IDNot Available
Phenol Explorer Metabolite IDNot Available
FoodDB IDFDB014510
KNApSAcK IDC00000756
Chemspider ID149962
KEGG Compound IDC00120
BioCyc IDBIOTIN
BiGG ID33931
Wikipedia LinkBiotin
NuGOwiki LinkHMDB00030
Metagene LinkHMDB00030
METLIN ID243
PubChem Compound171548
PDB IDBTN
ChEBI ID15956
References
Synthesis ReferenceCorey, E. J.; Mehrotra, Mukund M. A simple and enantioselective synthesis of (+)-biotin. Tetrahedron Letters (1988), 29(1), 57-60.
Material Safety Data Sheet (MSDS)Download (PDF)
General References
  1. Sreekumar A, Poisson LM, Rajendiran TM, Khan AP, Cao Q, Yu J, Laxman B, Mehra R, Lonigro RJ, Li Y, Nyati MK, Ahsan A, Kalyana-Sundaram S, Han B, Cao X, Byun J, Omenn GS, Ghosh D, Pennathur S, Alexander DC, Berger A, Shuster JR, Wei JT, Varambally S, Beecher C, Chinnaiyan AM: Metabolomic profiles delineate potential role for sarcosine in prostate cancer progression. Nature. 2009 Feb 12;457(7231):910-4. Pubmed: 19212411
  2. Thuy LP, Belmont J, Nyhan WL: Prenatal diagnosis and treatment of holocarboxylase synthetase deficiency. Prenat Diagn. 1999 Feb;19(2):108-12. Pubmed: 10215065
  3. Zempleni J, McCormick DB, Mock DM: Identification of biotin sulfone, bisnorbiotin methyl ketone, and tetranorbiotin-l-sulfoxide in human urine. Am J Clin Nutr. 1997 Feb;65(2):508-11. Pubmed: 9022537
  4. Bussolati G, Gugliotta P, Volante M, Pace M, Papotti M: Retrieved endogenous biotin: a novel marker and a potential pitfall in diagnostic immunohistochemistry. Histopathology. 1997 Nov;31(5):400-7. Pubmed: 9416479
  5. Mock DM, Stadler DD, Stratton SL, Mock NI: Biotin status assessed longitudinally in pregnant women. J Nutr. 1997 May;127(5):710-6. Pubmed: 9164991
  6. Thuy LP, Sweetman L, Nyhan WL: A new immunochemical assay for biotin. Clin Chim Acta. 1991 Oct 31;202(3):191-7. Pubmed: 1814646
  7. Limat A, Suormala T, Hunziker T, Waelti ER, Braathen LR, Baumgartner R: Proliferation and differentiation of cultured human follicular keratinocytes are not influenced by biotin. Arch Dermatol Res. 1996;288(1):31-8. Pubmed: 8750932
  8. Bigham SL, Ballard JD, Giles KD, Clelland CS, Jeffcoat R, Griffin KS, Farley TD, Bushman DR, Wright JR: Synthesis and possible applications of biotin-linked copper clusters. Physiol Chem Phys Med NMR. 1990;22(2):63-72. Pubmed: 2100006
  9. Mock DM, Stadler DD: Conflicting indicators of biotin status from a cross-sectional study of normal pregnancy. J Am Coll Nutr. 1997 Jun;16(3):252-7. Pubmed: 9176832
  10. Bingham JP, Bian S, Tan ZY, Takacs Z, Moczydlowski E: Synthesis of a biotin derivative of iberiotoxin: binding interactions with streptavidin and the BK Ca2+-activated K+ channel expressed in a human cell line. Bioconjug Chem. 2006 May-Jun;17(3):689-99. Pubmed: 16704206
  11. Mock DM: Biotin status: which are valid indicators and how do we know? J Nutr. 1999 Feb;129(2S Suppl):498S-503S. Pubmed: 10064317
  12. Mock DM, Dyken ME: Biotin catabolism is accelerated in adults receiving long-term therapy with anticonvulsants. Neurology. 1997 Nov;49(5):1444-7. Pubmed: 9371938
  13. Mock DM, Nyalala JO, Raguseo RM: A direct streptavidin-binding assay does not accurately quantitate biotin in human urine. J Nutr. 2001 Aug;131(8):2208-14. Pubmed: 11481419
  14. Mardach R, Zempleni J, Wolf B, Cannon MJ, Jennings ML, Cress S, Boylan J, Roth S, Cederbaum S, Mock DM: Biotin dependency due to a defect in biotin transport. J Clin Invest. 2002 Jun;109(12):1617-23. Pubmed: 12070309
  15. Mock DM, Heird GM: Urinary biotin analogs increase in humans during chronic supplementation: the analogs are biotin metabolites. Am J Physiol. 1997 Jan;272(1 Pt 1):E83-5. Pubmed: 9038855
  16. Fujimoto W, Inaoki M, Fukui T, Inoue Y, Kuhara T: Biotin deficiency in an infant fed with amino acid formula. J Dermatol. 2005 Apr;32(4):256-61. Pubmed: 15863846
  17. Schenker S, Hu ZQ, Johnson RF, Yang Y, Frosto T, Elliott BD, Henderson GI, Mock DM: Human placental biotin transport: normal characteristics and effect of ethanol. Alcohol Clin Exp Res. 1993 Jun;17(3):566-75. Pubmed: 8333586
  18. Mock NI, Malik MI, Stumbo PJ, Bishop WP, Mock DM: Increased urinary excretion of 3-hydroxyisovaleric acid and decreased urinary excretion of biotin are sensitive early indicators of decreased biotin status in experimental biotin deficiency. Am J Clin Nutr. 1997 Apr;65(4):951-8. Pubmed: 9094878
  19. Grafe F, Wohlrab W, Neubert RH, Brandsch M: Transport of biotin in human keratinocytes. J Invest Dermatol. 2003 Mar;120(3):428-33. Pubmed: 12603856
  20. Gravel RA, Narang MA: Molecular genetics of biotin metabolism: old vitamin, new science. J Nutr Biochem. 2005 Jul;16(7):428-31. Pubmed: 15992684
  21. Zempleni J: Uptake, localization, and noncarboxylase roles of biotin. Annu Rev Nutr. 2005;25:175-96. Pubmed: 16011464
  22. Holmberg A, Blomstergren A, Nord O, Lukacs M, Lundeberg J, Uhlen M: The biotin-streptavidin interaction can be reversibly broken using water at elevated temperatures. Electrophoresis. 2005 Feb;26(3):501-10. Pubmed: 15690449

Enzymes

General function:
Involved in acetyl-CoA carboxylase activity
Specific function:
ACC-beta may be involved in the provision of malonyl-CoA or in the regulation of fatty acid oxidation, rather than fatty acid biosynthesis. Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase.
Gene Name:
ACACB
Uniprot ID:
O00763
Molecular weight:
276538.575
References
  1. Liu Y, Zalameda L, Kim KW, Wang M, McCarter JD: Discovery of acetyl-coenzyme A carboxylase 2 inhibitors: comparison of a fluorescence intensity-based phosphate assay and a fluorescence polarization-based ADP Assay for high-throughput screening. Assay Drug Dev Technol. 2007 Apr;5(2):225-35. Pubmed: 17477831
General function:
Involved in catalytic activity
Specific function:
Pyruvate carboxylase catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second. Catalyzes in a tissue specific manner, the initial reactions of glucose (liver, kidney) and lipid (adipose tissue, liver, brain) synthesis from pyruvate.
Gene Name:
PC
Uniprot ID:
P11498
Molecular weight:
129632.565
References
  1. Liu L, Li Y, Zhu Y, Du G, Chen J: Redistribution of carbon flux in Torulopsis glabrata by altering vitamin and calcium level. Metab Eng. 2007 Jan;9(1):21-9. Epub 2006 Aug 12. Pubmed: 17008113
  2. Ferreira G, Weiss WP: Effect of biotin on activity and gene expression of biotin-dependent carboxylases in the liver of dairy cows. J Dairy Sci. 2007 Mar;90(3):1460-6. Pubmed: 17297119
  3. Jitrapakdee S, Surinya KH, Adina-Zada A, Polyak SW, Stojkoski C, Smyth R, Booker GW, Cleland WW, Attwood PV, Wallace JC: Conserved Glu40 and Glu433 of the biotin carboxylase domain of yeast pyruvate carboxylase I isoenzyme are essential for the association of tetramers. Int J Biochem Cell Biol. 2007;39(11):2120-34. Epub 2007 Jun 27. Pubmed: 17659996
  4. Jitrapakdee S, Adina-Zada A, Besant PG, Surinya KH, Cleland WW, Wallace JC, Attwood PV: Differential regulation of the yeast isozymes of pyruvate carboxylase and the locus of action of acetyl CoA. Int J Biochem Cell Biol. 2007;39(6):1211-23. Epub 2007 Mar 30. Pubmed: 17478118
  5. Ozimek PZ, Klompmaker SH, Visser N, Veenhuis M, van der Klei IJ: The transcarboxylase domain of pyruvate carboxylase is essential for assembly of the peroxisomal flavoenzyme alcohol oxidase. FEMS Yeast Res. 2007 Oct;7(7):1082-92. Epub 2007 Feb 20. Pubmed: 17316367
General function:
Involved in acetyl-CoA carboxylase activity
Specific function:
Catalyzes the rate-limiting reaction in the biogenesis of long-chain fatty acids. Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase.
Gene Name:
ACACA
Uniprot ID:
Q13085
Molecular weight:
269997.01
References
  1. Bilder P, Lightle S, Bainbridge G, Ohren J, Finzel B, Sun F, Holley S, Al-Kassim L, Spessard C, Melnick M, Newcomer M, Waldrop GL: The structure of the carboxyltransferase component of acetyl-coA carboxylase reveals a zinc-binding motif unique to the bacterial enzyme. Biochemistry. 2006 Feb 14;45(6):1712-22. Pubmed: 16460018
  2. Brownsey RW, Boone AN, Elliott JE, Kulpa JE, Lee WM: Regulation of acetyl-CoA carboxylase. Biochem Soc Trans. 2006 Apr;34(Pt 2):223-7. Pubmed: 16545081
  3. Aoki H, Kimura K, Igarashi K, Takenaka A: Soy protein suppresses gene expression of acetyl-coA carboxylase alpha from promoter PI in rat liver. Biosci Biotechnol Biochem. 2006 Apr;70(4):843-9. Pubmed: 16636450
  4. Santoro N, Brtva T, Roest SV, Siegel K, Waldrop GL: A high-throughput screening assay for the carboxyltransferase subunit of acetyl-CoA carboxylase. Anal Biochem. 2006 Jul 1;354(1):70-7. Epub 2006 May 3. Pubmed: 16707089
  5. Leonard E, Lim KH, Saw PN, Koffas MA: Engineering central metabolic pathways for high-level flavonoid production in Escherichia coli. Appl Environ Microbiol. 2007 Jun;73(12):3877-86. Epub 2007 Apr 27. Pubmed: 17468269
General function:
Involved in ligase activity
Specific function:
Not Available
Gene Name:
PCCB
Uniprot ID:
P05166
Molecular weight:
58215.13
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. Pubmed: 17139284
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. Pubmed: 17016423
  3. Vlasova TI, Stratton SL, Wells AM, Mock NI, Mock DM: Biotin deficiency reduces expression of SLC19A3, a potential biotin transporter, in leukocytes from human blood. J Nutr. 2005 Jan;135(1):42-7. Pubmed: 15623830
  4. Cherbonnel-Lasserre CL, Linares-Cruz G, Rigaut JP, Sabatier L, Dutrillaux B: Strong decrease in biotin content may correlate with metabolic alterations in colorectal adenocarcinoma. Int J Cancer. 1997 Sep 4;72(5):768-75. Pubmed: 9311592
  5. Ishii M, Chuakrut S, Arai H, Igarashi Y: Occurrence, biochemistry and possible biotechnological application of the 3-hydroxypropionate cycle. Appl Microbiol Biotechnol. 2004 Jun;64(5):605-10. Epub 2004 Feb 28. Pubmed: 14997352
General function:
Involved in catalytic activity
Specific function:
Not Available
Gene Name:
PCCA
Uniprot ID:
P05165
Molecular weight:
80058.295
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. Pubmed: 17139284
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. Pubmed: 17016423
  3. Clavero S, Martinez MA, Perez B, Perez-Cerda C, Ugarte M, Desviat LR: Functional characterization of PCCA mutations causing propionic acidemia. Biochim Biophys Acta. 2002 Nov 20;1588(2):119-25. Pubmed: 12385775
  4. Cherbonnel-Lasserre CL, Linares-Cruz G, Rigaut JP, Sabatier L, Dutrillaux B: Strong decrease in biotin content may correlate with metabolic alterations in colorectal adenocarcinoma. Int J Cancer. 1997 Sep 4;72(5):768-75. Pubmed: 9311592
  5. Vlasova TI, Stratton SL, Wells AM, Mock NI, Mock DM: Biotin deficiency reduces expression of SLC19A3, a potential biotin transporter, in leukocytes from human blood. J Nutr. 2005 Jan;135(1):42-7. Pubmed: 15623830
General function:
Involved in ligase activity
Specific function:
Not Available
Gene Name:
MCCC2
Uniprot ID:
Q9HCC0
Molecular weight:
61332.65
References
  1. Santoro N, Brtva T, Roest SV, Siegel K, Waldrop GL: A high-throughput screening assay for the carboxyltransferase subunit of acetyl-CoA carboxylase. Anal Biochem. 2006 Jul 1;354(1):70-7. Epub 2006 May 3. Pubmed: 16707089
  2. de Queiroz MS, Waldrop GL: Modeling and numerical simulation of biotin carboxylase kinetics: implications for half-sites reactivity. J Theor Biol. 2007 May 7;246(1):167-75. Epub 2006 Dec 28. Pubmed: 17266990
  3. Ludke A, Kramer R, Burkovski A, Schluesener D, Poetsch A: A proteomic study of Corynebacterium glutamicum AAA+ protease FtsH. BMC Microbiol. 2007 Jan 25;7:6. Pubmed: 17254330
  4. Jitrapakdee S, Surinya KH, Adina-Zada A, Polyak SW, Stojkoski C, Smyth R, Booker GW, Cleland WW, Attwood PV, Wallace JC: Conserved Glu40 and Glu433 of the biotin carboxylase domain of yeast pyruvate carboxylase I isoenzyme are essential for the association of tetramers. Int J Biochem Cell Biol. 2007;39(11):2120-34. Epub 2007 Jun 27. Pubmed: 17659996
General function:
Involved in biotin-[acetyl-CoA-carboxylase] ligase activity
Specific function:
Post-translational modification of specific protein by attachment of biotin. Acts on various carboxylases such as acetyl-CoA-carboxylase, pyruvate carboxylase, propionyl CoA carboxylase, and 3-methylcrotonyl CoA carboxylase.
Gene Name:
HLCS
Uniprot ID:
P50747
Molecular weight:
80759.345
Reactions
Adenosine triphosphate + Biotin + apo-[methylmalonyl-CoA:pyruvate carboxytransferase] → Adenosine monophosphate + Pyrophosphate + [methylmalonyl-CoA:pyruvate carboxytransferase]details
Adenosine triphosphate + Biotin + apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)] → Adenosine monophosphate + Pyrophosphate + [propionyl-CoA:carbon-dioxide ligase (ADP-forming)]details
Adenosine triphosphate + Biotin + apo-[3-methylcrotonoyl-CoA:carbon-dioxide ligase (ADP-forming)] → Adenosine monophosphate + Pyrophosphate + [3-methylcrotonoyl-CoA:carbon-dioxide ligase (ADP-forming)]details
Adenosine triphosphate + Biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)] → Adenosine monophosphate + Pyrophosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]details
Adenosine triphosphate + Biotin → Pyrophosphate + Biotinyl-5'-AMPdetails
References
  1. Velazquez-Arellano A: From an inborn error patient to a search for regulatory meaning: a biotin conducted voyage. Mol Genet Metab. 2006 Mar;87(3):194-7. Epub 2005 Dec 15. Pubmed: 16359899
  2. Hassan YI, Zempleni J: Epigenetic regulation of chromatin structure and gene function by biotin. J Nutr. 2006 Jul;136(7):1763-5. Pubmed: 16772434
  3. Camporeale G, Giordano E, Rendina R, Zempleni J, Eissenberg JC: Drosophila melanogaster holocarboxylase synthetase is a chromosomal protein required for normal histone biotinylation, gene transcription patterns, lifespan, and heat tolerance. J Nutr. 2006 Nov;136(11):2735-42. Pubmed: 17056793
General function:
Involved in catalytic activity
Specific function:
Not Available
Gene Name:
MCCC1
Uniprot ID:
Q96RQ3
Molecular weight:
80472.45
References
  1. Friebel D, von der Hagen M, Baumgartner ER, Fowler B, Hahn G, Feyh P, Heubner G, Baumgartner MR, Hoffmann GF: The first case of 3-methylcrotonyl-CoA carboxylase (MCC) deficiency responsive to biotin. Neuropediatrics. 2006 Apr;37(2):72-8. Pubmed: 16773504
General function:
Involved in hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
Specific function:
Catalytic release of biotin from biocytin, the product of biotin-dependent carboxylases degradation.
Gene Name:
BTD
Uniprot ID:
P43251
Molecular weight:
61132.43
Reactions
Biotin amide + Water → Biotin + Ammoniadetails
Biocytin + Water → Biotin + L-Lysinedetails
General function:
Involved in monooxygenase activity
Specific function:
Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. Participates in the metabolism of an as-yet-unknown biologically active molecule that is a participant in eye development.
Gene Name:
CYP1B1
Uniprot ID:
Q16678
Molecular weight:
60845.33
References
  1. Preissner S, Kroll K, Dunkel M, Senger C, Goldsobel G, Kuzman D, Guenther S, Winnenburg R, Schroeder M, Preissner R: SuperCYP: a comprehensive database on Cytochrome P450 enzymes including a tool for analysis of CYP-drug interactions. Nucleic Acids Res. 2010 Jan;38(Database issue):D237-43. Epub 2009 Nov 24. Pubmed: 19934256
General function:
Involved in transporter activity
Specific function:
Transports pantothenate, biotin and lipoate in the presence of sodium.
Gene Name:
SLC5A6
Uniprot ID:
Q9Y289
Molecular weight:
68641.27
References
  1. Luo S, Kansara VS, Zhu X, Mandava NK, Pal D, Mitra AK: Functional characterization of sodium-dependent multivitamin transporter in MDCK-MDR1 cells and its utilization as a target for drug delivery. Mol Pharm. 2006 May-Jun;3(3):329-39. Pubmed: 16749865
  2. Janoria KG, Hariharan S, Paturi D, Pal D, Mitra AK: Biotin uptake by rabbit corneal epithelial cells: role of sodium-dependent multivitamin transporter (SMVT). Curr Eye Res. 2006 Oct;31(10):797-809. Pubmed: 17038304
  3. Reidling JC, Said HM: Regulation of the human biotin transporter hSMVT promoter by KLF-4 and AP-2: confirmation of promoter activity in vivo. Am J Physiol Cell Physiol. 2007 Apr;292(4):C1305-12. Epub 2006 Nov 29. Pubmed: 17135299
  4. Camporeale G, Zempleni J, Eissenberg JC: Susceptibility to heat stress and aberrant gene expression patterns in holocarboxylase synthetase-deficient Drosophila melanogaster are caused by decreased biotinylation of histones, not of carboxylases. J Nutr. 2007 Apr;137(4):885-9. Pubmed: 17374649
General function:
Involved in catalytic activity
Specific function:
Not Available
Gene Name:
DKFZp686B20267
Uniprot ID:
Q68D27
Molecular weight:
63966.5