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Novel transmembrane lipases of alpha/beta hydrolase fold
Author(s) -
Lazniewski Michal,
Steczkiewicz Kamil,
Knizewski Lukasz,
Wawer Iwona,
Ginalski Krzysztof
Publication year - 2011
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2011.02.016
Subject(s) - biochemistry , biology , transmembrane domain , transmembrane protein , enzyme , hydrolase , lipid metabolism , peptide sequence , amino acid , computational biology , gene , receptor
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.