Go to basket

Tree Display

AceDB Schema

XML Display


Family Report for: BioH


Family BioH
Block X
Parent Family : Abhydrolase_6

Pimelyl-[acyl-carrier protein] methyl ester esterase: BioH family previously included in AlphaBeta_hydrolase family. The structure of ecoli-bioh by Sanishvili et al pdb:1M33 allowed description of function of this family. This CoA-binding enzyme is required for the production of pimeloyl-coenzyme A, the substrate of the BioF protein early in the biosynthesis of biotin. Its exact function is unknown. Members of this family are restricted to the proteobacteria. BioH shows carboxylesterase activity with a preference for short chain fatty acid esters (acyl chain length of up to 6 carbons). It also displays a weak thioesterase activity. Biotin synthesis necessitate the fatty acid synthetic pathway: Malonyl-thioester is methylated by BioC, which allows recognition of this atypical substrate by the fatty acid synthetic enzymes. The malonyl-thioester methyl ester enters fatty acid synthesis as the primer and undergoes two reiterations of the fatty acid elongation cycle to give pimeloyl-acyl carrier protein (ACP) methyl ester, which is hydrolyzed to pimeloyl-ACP and methanol by BioH. In Pseudomonas aeruginosa the bioH gene is within a biotin synthesis operon and its transcription is coregulated with the other biotin operon genes. In Escherichia coli the gene is not located within a biotin synthetic operon and its transcription is not coregulated with the other biotin synthesis genes (Cao et al. 2017). In Francisella BioJ is the enzyme of the biotin biosynthesis pathway that determines the chain length of the biotin valeryl side-chain. It is the functionnal equivalent of BioH although it shows low homology to BioH (belongs to hormone sensitive lipase family)( Feng et al. 2014). In Haemophilus influenzae it is another family Duf_452 which plays the role (Shi et al. 2016). In Helicobacter it is another alpha/beta hydrolase BioV (Bi et al. 2016)

IPR010076 (BioH Pimelyl-[acyl-carrier protein] methyl ester esterase)
no EC number

Peptide in
Nucleotide in
Alignment with Multalin
|Text only/graphic display
Seed alignment with MAFFT
|No colour/coloured with Mview
Alignment with MAFFT
|No colour/coloured with Mview
|Graphical display, obtained with the dnd file produced by Clustalw

4 more
    Title: A Francisella virulence factor catalyses an essential reaction of biotin synthesis
    Feng Y, Napier BA, Manandhar M, Henke SK, Weiss DS, Cronan JE
    Ref: Molecular Microbiology, 91:300, 2014 : PubMed


    Title: Biotin synthesis begins by hijacking the fatty acid synthetic pathway.
    Lin S, Hanson RE, Cronan JE
    Ref: Nat Chemical Biology, 6:682, 2010 : PubMed


    Title: Integrating structure, bioinformatics, and enzymology to discover function: BioH, a new carboxylesterase from Escherichia coli
    Sanishvili R, Yakunin AF, Laskowski RA, Skarina T, Evdokimova E, Doherty-Kirby A, Lajoie GA, Thornton JM, Arrowsmith CH and Edwards AM <2 more author(s)>
    Ref: Journal of Biological Chemistry, 278:26039, 2003 : PubMed


Other Papers

No structure scheme yet for this family

Structures in BioH family (4)

Genes Proteins in BioH family (220)

Fragments of genes in BioH family (2)

Substrates of some enzymes in the BioH family (7)

Inhibitors of some enzymes in the BioH family (2)

Send your questions or comments to :
Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
For technical information about these pages see:
ESTHER Home Page and ACEDB Home Page
AcePerl Lincoln Stein Home Page

Acknowledgements and disclaimer