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Substrate‐enzyme interactions and catalytic mechanism in phospholipase C: A molecular modeling study using the GRID program
Author(s) -
Byberg Jette R.,
Jørgensen Flemming S.,
Hansen Sissel,
Hough Edward
Publication year - 1992
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340120405
Subject(s) - mechanism (biology) , substrate (aquarium) , grid , enzyme , catalysis , chemistry , computer science , materials science , biophysics , biochemistry , biology , physics , geography , ecology , geodesy , quantum mechanics
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.