| Autor: |
F C, Van der Wiele, W, Atsma, R, Dijkman, A M, Schreurs, A J, Slotboom, G H, De Haas |
| Rok vydání: |
1988 |
| Předmět: |
|
| Zdroj: |
Biochemistry. 27(5) |
| ISSN: |
0006-2960 |
| Popis: |
The lipid-binding domain of pancreatic phospholipases A2 contains a number of exposed, hydrophobic amino acid side chains that are involved in the binding of the enzyme to organized lipid-water interfaces. Besides these apolar residues, at least two positively charged lysine groups are present in positions 10 and 116 of the lipid-binding domain. In order to investigate the possible function of these basic side chains in the lipid-binding process, a number of specifically acylated enzyme mutants were prepared, and their kinetic and lipid-binding properties have been compared with those of the native enzymes. It is concluded that the attachment of a long-chain acyl group in an amide linkage to Lys10 or Lys116 phospholipase A2 has only a minor influence on the catalytic properties of the enzyme. On the other hand, the lipid-binding properties of the mutant enzymes appear to be considerably reinforced. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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