Direct involvement of the C-terminal extremity of pancreatic lipase (403-449) in colipase binding.
After a selective cleavage of a lipase/colipase cross-linked complex, the colipase has been shown to be bound to a 5 kDa lipase fragment identified as the C-terminal extremity of the chain extending from residue 403 to the C-terminus (Cys 449). The colipase binding site on lipase is therefore localized in a restricted contact area. Moreover, from sequence comparison of lipase from various species, an acidic residue, Glu 440, is likely to be involved in ion pairing with colipase.
Chaillan
C
C
Centre de biochimie et de Biologie Moléculaire du CNRS, Marseille, France.
Kerfelec
B
B
Foglizzo
E
E
Chapus
C
C
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D003028:CME-Carbodiimide / Q000031:analogs & derivatives*; D002234:Carbodiimides / Q000494:pharmacology*; D003089:Colipases / Q000378:metabolism*; D003432:Cross-Linking Reagents / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D008049:Lipase / Q000302:isolation & purification / Q000378:metabolism*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010179:Pancreas / Q000201:enzymology*; D010446:Peptide Fragments / Q000378:metabolism; D012689:Sequence Homology, Nucleic Acid; D013552:Swine; D014364:Tryptophan
D002234:Carbodiimides; D003089:Colipases; D003432:Cross-Linking Reagents; D010446:Peptide Fragments; C074111:N-cyclohexyl-N'-2-morpholinoethyl-carbodiimide-methyl-4-toluolsulfonate; D003028:CME-Carbodiimide; D014364:Tryptophan; D008049:Lipase