Cloning and molecular modelling of turkey pancreatic lipase: structural explanation of the increased interaction power with lipidic interface.
Starting from total pancreatic mRNAs, turkey pancreatic lipase (TPL) cDNA was synthesized by RT-PCR and cloned into the PGEM-T vector. Amino acid sequence of the TPL is compared to that of human pancreatic lipase (HPL). A 3-D structure model of TPL was built using the 3-D structure of HPL as template, given the high amino acid sequence homology between the two lipases. Based on this model, the enhanced interaction power of TPL, as compared to that of HPL, into a phosphatidylcholine monolayer film, could be explained. We concluded that an increase in the exposed hydrophobic residues on the surface of TPL would be responsible for an enhanced interaction with a lipidic interface.
Fendri
A
A
Laboratoire de Biochimie et de Génie Enzymatique des Lipases, ENIS route de Soukra, BPW 3038 Sfax, Tunisia.
Frikha
F
F
Miled
N
N
Gargouri
Y
Y
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D020134:Catalytic Domain; D003001:Cloning, Molecular; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D008049:Lipase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D008055:Lipids / Q000737:chemistry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010179:Pancreas / Q000201:enzymology*; D011487:Protein Conformation; D016415:Sequence Alignment; D020539:Sequence Analysis, Protein; D014422:Turkeys / Q000378:metabolism*
D008055:Lipids; D008049:Lipase