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Importance of a repetitive nine‐residue sequence motif for intracellular stability and functional structure of a family I.3 lipase
Author(s) -
Angkawidjaja Clement,
Paul Aditya,
Koga Yuichi,
Takano Kazufumi,
Kanaya Shigenori
Publication year - 2005
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.2005.07.041
Subject(s) - intracellular , lipase , mutant , residue (chemistry) , secretion , biochemistry , extracellular , biology , chemistry , enzyme , microbiology and biotechnology , gene
PML5 is a functional derivative of a family I.3 lipase from Pseudomonas sp. MIS38 and contains five repeats of a nine‐residue sequence motif. Two aspartate residues within the second and third repetitive sequences of PML5 were replaced by Ala. The secretion level, intracellular accumulation level, and stability of the resultant mutant protein were greatly reduced as compared to those of PML5. In addition, this mutant protein was inactive and did not bind Ca 2+ ion. We propose that the repetitive sequences of PML5 form a β‐roll structure in the cells and thereby contribute to the intracellular stability and secretion efficiency of the protein.