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

Research output: Contribution to journalJournal articleResearchpeer-review

J R Byberg, Flemming Steen Jørgensen, S Hansen, E Hough

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.
Original languageEnglish
JournalProteins: Structure, Function, and Bioinformatics
Volume12
Issue number4
Pages (from-to)331-8
Number of pages8
ISSN0887-3585
DOIs
Publication statusPublished - 1992

    Research areas

  • Binding Sites, Catalysis, Computer Simulation, Models, Molecular, Oxygen, Phosphates, Quaternary Ammonium Compounds, Software, Substrate Specificity, Type C Phospholipases, Zinc

ID: 38394585