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Family Report for: Bacterial_lip_FamI.6

Bacterial_lip_FamI.6



Relationship
Block L
Parent Family : Bacterial_lipase

Comment
This family correspond to family I.6 of the classification of Arpigny and Jaeger (1999). These lipases differ from other bacterial lipases. They present high phospholipase A1 activity. The substrate-binding cavity contains two large hydrophobic acyl chain-binding pockets and a shallow and more polar third pocket that is capable of binding either a (short) fatty acid or a phospholipid head-group.

Database
Sequences
Interpro
|
PIRSF
|
Pdoc
|
PFam
|
Prints
|
Prosite
|
no EC number



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

References
    Title: Structural basis of phospholipase activity of Staphylococcus hyicus lipase
    Tiesinga JJ, van Pouderoyen G, Nardini M, Ransac S, Dijkstra BW
    Ref: Journal of Molecular Biology, 371:447, 2007 : PubMed

            

    Title: Lipases for biotechnology
    Jaeger KE, Eggert T
    Ref: Curr Opin Biotechnol, 13:390, 2002 : PubMed

            

    Title: Bacterial lipolytic enzymes: classification and properties
    Arpigny JL, Jaeger KE
    Ref: Biochemical Journal, 343:177, 1999 : PubMed

            

Other Papers


Structure scheme for Bacterial_lip_FamI.6

Structures in Bacterial_lip_FamI.6 family (4)

Genes Proteins in Bacterial_lip_FamI.6 family (13)

No fragments
Substrates of some enzymes in the Bacterial_lip_FamI.6 family (1)

Inhibitors of some enzymes in the Bacterial_lip_FamI.6 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.
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