3P2P

ENHANCED ACTIVITY AND ALTERED SPECIFICITY OF PHOSPHOLIPASE A2 BY DELETION OF A SURFACE LOOP

3P2P の概要

• エントリーDOI: 10.2210/pdb3p2p/pdb
• 分子名称: PHOSPHOLIPASE A2, CALCIUM ION (3 entities in total)
• 機能のキーワード: hydrolase(carboxyl ester)
• 由来する生物種: Sus scrofa (pig)
• 細胞内の位置: Secreted: P00592
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 26914.27

構造登録者

Dijkstra, B.W.,Thunnissen, M.M.G.M.,Kalk, K.H.,Drenth, J. (登録日: 1989-11-29, 公開日: 1990-01-15, 最終更新日: 2024-10-30)

主引用文献

Kuipers, O.P.,Thunnissen, M.M.,de Geus, P.,Dijkstra, B.W.,Drenth, J.,Verheij, H.M.,de Haas, G.H.
Enhanced activity and altered specificity of phospholipase A2 by deletion of a surface loop.
Science, 244:82-85, 1989

PubMed Abstract: 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 A2 does not change the binding constant for micelles significantly, but it improves catalytic activity up to 16 times on micellar (zwitterionic) lecithin substrates. In contrast, the decrease in activity on negatively charged substrates is greater than fourfold. A crystallographic study of the mutant enzyme shows that the region of the deletion has a well-defined structure that differs from the structure of the wild-type enzyme. No structural changes in the active site of the enzyme were detected.

PubMed: 2704992

実験手法

X-RAY DIFFRACTION (2.1 Å)