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    Pathway Description
      Biotin-Carboxyl Carrier Protein Assembly
Escherichia coli
            Category:
                Metabolite Pathway
                Sub-Category:
                Metabolic
            Created: 2015-10-09
          Last Updated: 2025-09-05
        
          The assembly of a biotin-carboxyl carrier protein starts with a biotin carboxyl carrier protein monomer interacting with an ATP, and a biotin through a biotin -acetyl-coa-carboxylase ligase resulting in the release of a hydrogen ion, an AMP, a diphosphate and a biotynylated BCCP monomer. The latter compound reacts spontaneously to create a biotinylated BCCP dimer. This compound in turn reacts with a hydrogen carbonate and an ATP driven biotin carboxylase resulting in the release of ADP, a hydrogen Ion , a phosphate and a carboxylated biotinylated BCCP dimer.
This complex can be degraded by reacting with water, an acetyl0CoA, and an ATP driven acetyl-CoA carboxyltransferase resulting in the release of a hydrogen ion, a phosphate, an ADP, a malonyl-CoA and a biotynylated BCCP dimer
        
      References
      
      Biotin-Carboxyl Carrier Protein Assembly References
Barber MC, Price NT, Travers MT: Structure and regulation of acetyl-CoA carboxylase genes of metazoa. Biochim Biophys Acta. 2005 Mar 21;1733(1):1-28. doi: 10.1016/j.bbalip.2004.12.001. Epub 2005 Jan 22.
                  Pubmed: 15749055
              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
              Li SJ, Cronan JE Jr: The genes encoding the two carboxyltransferase subunits of Escherichia coli acetyl-CoA carboxylase. J Biol Chem. 1992 Aug 25;267(24):16841-7.
                  Pubmed: 1355089
              Yamamoto Y, Miwa Y, Miyoshi K, Furuyama J, Ohmori H: The Escherichia coli ldcC gene encodes another lysine decarboxylase, probably a constitutive enzyme. Genes Genet Syst. 1997 Jun;72(3):167-72.
                  Pubmed: 9339543
              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
              Bognar AL, Osborne C, Shane B: Primary structure of the Escherichia coli folC gene and its folylpolyglutamate synthetase-dihydrofolate synthetase product and regulation of expression by an upstream gene. J Biol Chem. 1987 Sep 5;262(25):12337-43.
                  Pubmed: 3040739
              Nonet ML, Marvel CC, Tolan DR: The hisT-purF region of the Escherichia coli K-12 chromosome. Identification of additional genes of the hisT and purF operons. J Biol Chem. 1987 Sep 5;262(25):12209-17.
                  Pubmed: 3040734
              Yamamoto Y, Aiba H, Baba T, Hayashi K, Inada T, Isono K, Itoh T, Kimura S, Kitagawa M, Makino K, Miki T, Mitsuhashi N, Mizobuchi K, Mori H, Nakade S, Nakamura Y, Nashimoto H, Oshima T, Oyama S, Saito N, Sampei G, Satoh Y, Sivasundaram S, Tagami H, Horiuchi T, et al.: Construction of a contiguous 874-kb sequence of the Escherichia coli -K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features. DNA Res. 1997 Apr 28;4(2):91-113. doi: 10.1093/dnares/4.2.91.
                  Pubmed: 9205837
              Kondo H, Shiratsuchi K, Yoshimoto T, Masuda T, Kitazono A, Tsuru D, Anai M, Sekiguchi M, Tanabe T: Acetyl-CoA carboxylase from Escherichia coli: gene organization and nucleotide sequence of the biotin carboxylase subunit. Proc Natl Acad Sci U S A. 1991 Nov 1;88(21):9730-3. doi: 10.1073/pnas.88.21.9730.
                  Pubmed: 1682920
              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
              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
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