EC 3.1.1.85 - Pimeloyl-[acyl-carrier protein] methyl ester esterase

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IntEnz Enzyme Nomenclature
EC 3.1.1.85

Names

Accepted name:
pimeloyl-[acyl-carrier protein] methyl ester esterase
Other name:
BioH
Systematic name:
pimeloyl-[acyl-carrier protein] methyl ester hydrolase

Reaction

Comments:

Involved in biotin biosynthesis in Gram-negative bacteria. The enzyme exhibits carboxylesterase activity, particularly toward substrates with short acyl chains [1,2]. Even though the enzyme can interact with coenzyme A thioesters [3], the in vivo role of the enzyme is to hydrolyse the methyl ester of pimeloyl-[acyl carrier protein], terminating the part of the biotin biosynthesis pathway that is catalysed by the fatty acid elongation enzymes [4].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot: (106) [show] [UniProt]

References

  1. Sanishvili, R., Yakunin, A. F., Laskowski, R. A., Skarina, T., Evdokimova, E., Doherty-Kirby, A., Lajoie, G. A., Thornton, J. M., Arrowsmith, C. H., Savchenko, A., Joachimiak, A., Edwards, A. M.
    Integrating structure, bioinformatics, and enzymology to discover function: BioH, a new carboxylesterase from Escherichia coli.
    J. Biol. Chem. 278 : 26039-26045 (2003). [PMID: 12732651]
  2. Lemoine, Y., Wach, A., Jeltsch, J. M.
    To be free or not: the fate of pimelate in Bacillus sphaericus and in Escherichia coli.
    Mol. Microbiol. 19 : 645-647 (1996). [PMID: 8830257]
  3. Tomczyk, N. H., Nettleship, J. E., Baxter, R. L., Crichton, H. J., Webster, S. P., Campopiano, D. J.
    Purification and characterisation of the BIOH protein from the biotin biosynthetic pathway.
    FEBS Lett. 513 : 299-304 (2002). [PMID: 11904168]
  4. Lin, S., Hanson, R. E., Cronan, J. E.
    Biotin synthesis begins by hijacking the fatty acid synthetic pathway.
    Nat. Chem. Biol. 6 : 682-688 (2010). [PMID: 20693992]

[EC 3.1.1.85 created 2011]