Enhanced activity and altered specificity of phospholipase A sub(2) by deletion of a surface loop

Protein engineering and x-ray crystallography have been used to study the role of a surface loop that is present in pancreatic phospholipases but is absent in snake venom phospholipases. Removal of residues 62 to 66 from porcine pancreatic phospholipase A sub(2) does not change the binding constant...

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Veröffentlicht in:Science (American Association for the Advancement of Science) 1989-01, Vol.244 (4900), p.82-85
Hauptverfasser: Kuipers, O P, Thunnissen, M, Geus, P, Dijkstra, B W, Drenth, J, Verheij, H M, de Haas, GH
Format: Artikel
Sprache:eng
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Zusammenfassung:Protein engineering and x-ray crystallography have been used to study the role of a surface loop that is present in pancreatic phospholipases but is absent in snake venom phospholipases. Removal of residues 62 to 66 from porcine pancreatic phospholipase A sub(2) does not change the binding constant for micelles significantly, but it improves catalytic activity up to 16 times on micellar (switterionic) lecithin substrates.
ISSN:0036-8075