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Substrate-enzyme interactions and catalytic mechanism in phospholipase C: A molecular modeling study using the GRID program

✍ Scribed by Jette R. Byberg; Flemming S. Jørgensen; Sissel Hansen; Edward Hough

Publisher
John Wiley and Sons
Year
1992
Tongue
English
Weight
684 KB
Volume
12
Category
Article
ISSN
0887-3585

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✦ Synopsis

Abstract

Based on the high‐resolution X‐ray crystallographic structure of phospholipase C from Bacillus cereus, the orientation of the phosphatidylcholine substrate in the active site of the enzyme is proposed. The proposal is based on extensive calculations using the GRID program and molecular mechanics geometry relaxations. The substrate model has been constructed by successively placing phosphate, choline and diacylglycerol moieties in the positions indicated from GRID calculations. On the basis of the resulting orientation of a complete phosphatidylcholine molecule, we propose a mechanism for the hydrolysis of the substrate.

📜 SIMILAR VOLUMES

Substrate binding and catalytic mechanis
Substrate binding and catalytic mechanism in phospholipase C from Bacillus Cereus: A molecular mechanics and molecular dynamics study
✍ Dorthe da Graça Thrige; Jette R. Byberg Buur; Flemming Steen Jørgensen 📂 Article 📅 1997 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 970 KB

For the first time a consistent catalytic mechanism of phospholipase C from Bacillus cereus is reported based on molecular mechanics calculations. We have identified the position of the nucleophilic water molecule, which is directly involved in the hydrolysis of the natural substrate, phosphatidylch