| Title : Novel transmembrane lipases of alpha\/beta hydrolase fold - Lazniewski_2011_FEBS.Lett_585_870 |
| Author(s) : Lazniewski M , Steczkiewicz K , Knizewski L , Wawer I , Ginalski K |
| Ref : FEBS Letters , 585 :870 , 2011 |
| Abstract : Processing of exogenous glycerol esters is an initial step in energy derivation for many bacterial cells. Lipid-rich environments settled by a variety of organisms exert strong evolutionary pressure for establishing enzymatic pathways involved in lipid metabolism. However, a certain number of enzymes involved in this process remain unknown since they do not share detectable sequence similarity with any known protein domains. Using distant homology detection and fold recognition we predict that bacterial transmembrane proteins belonging to the uncharacterized domain of unknown function 2319 (DUF2319) family possess the alpha/beta hydrolase fold domain together with the catalytic triad critical for hydrolysis. A detailed analysis of sequence/structure features and genomic context indicates that DUF2319 proteins may be involved in lipid metabolism. Therefore, these enzymes are likely to serve as extracellular lipases. |
| ESTHER : Lazniewski_2011_FEBS.Lett_585_870 |
| PubMedSearch : Lazniewski_2011_FEBS.Lett_585_870 |
| PubMedID: 21333648 |
Lazniewski M, Steczkiewicz K, Knizewski L, Wawer I, Ginalski K (2011)
Novel transmembrane lipases of alpha\/beta hydrolase fold
FEBS Letters
585 :870
Lazniewski M, Steczkiewicz K, Knizewski L, Wawer I, Ginalski K (2011)
FEBS Letters
585 :870