Loading Pathway...
Error: Pathway image not found.
Hide
Pathway Description
Operon: Biotin Biosynthesis
Escherichia coli
Category:
Protein Pathway
Sub-Categories:
Gene Regulatory
Cellular Response
Created: 2015-10-26
Last Updated: 2025-01-30
The BioBFCD operon in E. coli contains four genes involved in the biosynthesis of biotin, a molecule important for various metabolic functions in the cell. The operon can be inactivated by the ginding of bifunctional protein BirA when it interacts with the biotin carboxyl carrier protein of acetyl-CoA carboxylase (AccB). This complex forms when AccB is in high concentrations, due to high levels of biotin already in the cell.
The first gene in the operon, bioB, encodes biotin synthase, and enzyme that catalyzes conversion of dethiobiotin into biotin.
The second gene, bioF, encodes 8-amino-7-oxononanoate synthase. This protein is an enzyme that condenses pimeloyl-[ACP] and L-alanine to form 8-amino-7-oxononanoate. This is later used in biotin biosynthesis.
The third gene, bioC, encodes malonyl-[ACP] methyltransferase, a protein that methylates malonyl-thioester to its ester form as a part of biotin biosynthesis.
The final gene, bioD, encodes dethiobiotin synthetase. This enzyme forms dethiobiotin, the direct precursor to biotin, by adding a carbon dioxide molecule into 7,8-diaminononanoate, which ends up forming a ring structure. Dethiobiotin is then acted upon by biotin synthase, forming biotin.
References
Operon: Biotin Biosynthesis References
Abdel-Hamid AM, Cronan JE: Coordinate expression of the acetyl coenzyme A carboxylase genes, accB and accC, is necessary for normal regulation of biotin synthesis in Escherichia coli. J Bacteriol. 2007 Jan;189(2):369-76. doi: 10.1128/JB.01373-06. Epub 2006 Oct 20.
Pubmed: 17056747
Cronan JE Jr: The E. coli bio operon: transcriptional repression by an essential protein modification enzyme. Cell. 1989 Aug 11;58(3):427-9.
Pubmed: 2667763
Sanyal I, Cohen G, Flint DH: Biotin synthase: purification, characterization as a [2Fe-2S]cluster protein, and in vitro activity of the Escherichia coli bioB gene product. Biochemistry. 1994 Mar 29;33(12):3625-31. doi: 10.1021/bi00178a020.
Pubmed: 8142361
Lotierzo M, Raux E, Tse Sum Bui B, Goasdoue N, Libot F, Florentin D, Warren MJ, Marquet A: Biotin synthase mechanism: mutagenesis of the YNHNLD conserved motif. Biochemistry. 2006 Oct 10;45(40):12274-81. doi: 10.1021/bi060662m.
Pubmed: 17014080
Otsuka AJ, Buoncristiani MR, Howard PK, Flamm J, Johnson C, Yamamoto R, Uchida K, Cook C, Ruppert J, Matsuzaki J: The Escherichia coli biotin biosynthetic enzyme sequences predicted from the nucleotide sequence of the bio operon. J Biol Chem. 1988 Dec 25;263(36):19577-85.
Pubmed: 3058702
Alexeev D, Alexeeva M, Baxter RL, Campopiano DJ, Webster SP, Sawyer L: The crystal structure of 8-amino-7-oxononanoate synthase: a bacterial PLP-dependent, acyl-CoA-condensing enzyme. J Mol Biol. 1998 Nov 27;284(2):401-19. doi: 10.1006/jmbi.1998.2086.
Pubmed: 9813126
Alexeev D, Baxter RL, Campopiano DJ, Kerbarh O, Sawyer L, Tomczyk N, Watt R, Webster SP: Suicide inhibition of alpha-oxamine synthases: structures of the covalent adducts of 8-amino-7-oxononanoate synthase with trifluoroalanine. Org Biomol Chem. 2006 Apr 7;4(7):1209-12. doi: 10.1039/b517922j. Epub 2006 Mar 1.
Pubmed: 16557306
Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. doi: 10.1126/science.277.5331.1453.
Pubmed: 9278503
Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. doi: 10.1038/msb4100049. Epub 2006 Feb 21.
Pubmed: 16738553
Alexeev D, Bury SM, Boys CW, Turner MA, Sawyer L, Ramsey AJ, Baxter HC, Baxter RL: Sequence and crystallization of Escherichia coli dethiobiotin synthetase, the penultimate enzyme of biotin biosynthesis. J Mol Biol. 1994 Jan 14;235(2):774-6. doi: 10.1006/jmbi.1994.1030.
Pubmed: 8289297
Howard PK, Shaw J, Otsuka AJ: Nucleotide sequence of the birA gene encoding the biotin operon repressor and biotin holoenzyme synthetase functions of Escherichia coli. Gene. 1985;35(3):321-31. doi: 10.1016/0378-1119(85)90011-3.
Pubmed: 3899863
Buoncristiani MR, Howard PK, Otsuka AJ: DNA-binding and enzymatic domains of the bifunctional biotin operon repressor (BirA) of Escherichia coli. Gene. 1986;44(2-3):255-61. doi: 10.1016/0378-1119(86)90189-7.
Pubmed: 3536662
Blattner FR, Burland V, Plunkett G 3rd, Sofia HJ, Daniels DL: Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes. Nucleic Acids Res. 1993 Nov 25;21(23):5408-17. doi: 10.1093/nar/21.23.5408.
Pubmed: 8265357
Muramatsu S, Mizuno T: Nucleotide sequence of the fabE gene and flanking regions containing a bent DNA sequence of Escherichia coli. Nucleic Acids Res. 1989 May 25;17(10):3982. doi: 10.1093/nar/17.10.3982.
Pubmed: 2660106
Alix JH: A rapid procedure for cloning genes from lambda libraries by complementation of E. coli defective mutants: application to the fabE region of the E. coli chromosome. DNA. 1989 Dec;8(10):779-89. doi: 10.1089/dna.1989.8.779.
Pubmed: 2575489
Li SJ, Cronan JE Jr: The gene encoding the biotin carboxylase subunit of Escherichia coli acetyl-CoA carboxylase. J Biol Chem. 1992 Jan 15;267(2):855-63.
Pubmed: 1370469
Highlighted elements will appear in red.
Highlight Compounds
No Compounds Present
Highlight Proteins
Enter relative concentration values (without units). Elements will be highlighted in a color gradient where red = lowest concentration and green = highest concentration. For the best results, view the pathway in Black and White.
Visualize Compound Data
No Compounds Present
Visualize Protein Data
Downloads
Settings