| Autor: |
Van der Wiele FC; Laboratory of Biochemistry, State University of Utrecht, Transitorium III, University Center De Uithof, The Netherlands., Atsma W, Dijkman R, Schreurs AM, Slotboom AJ, De Haas GH |
| Jazyk: |
angličtina |
| Zdroj: |
Biochemistry [Biochemistry] 1988 Mar 08; Vol. 27 (5), pp. 1683-8. |
| DOI: |
10.1021/bi00405a045 |
| Abstrakt: |
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: |
MEDLINE |
| Externí odkaz: |
|
