Site-specific .epsilon.-amino monoacylation of pancreatic phospholipase A2. 1. Preparation and properties

Autor:	F. C. Van Der Wiele, A. M. M. Schreurs, Arend J. Slotboom, R. Dijkman, G.H. de Haas, W. Atsma
Rok vydání:	1988
Předmět:	chemistry.chemical_classification biology Lysine Phospholipase Biochemistry Amino acid Acylation chemistry.chemical_compound Enzyme Phospholipase A2 chemistry Side chain biology.protein lipids (amino acids peptides and proteins) Acyl group
Zdroj:	Biochemistry. 27:1683-1688
ISSN:	1520-4995 0006-2960
DOI:	10.1021/bi00405a045
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:	https://explore.openaire.eu/search/publication?articleId=doi_________::871b5461cb7a890bbf8728c8feaecc27 https://doi.org/10.1021/bi00405a045 Zobrazit plný text záznamu