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 |
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Hauptverfasser: | , , , , , , |
Format: | Artikel |
Sprache: | eng |
Online-Zugang: | Volltext |
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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. |
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ISSN: | 0036-8075 |