Substrate-enzyme interactions and catalytic mechanism in phospholipase C: a molecular modeling study using the GRID program
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Substrate-enzyme interactions and catalytic mechanism in phospholipase C : a molecular modeling study using the GRID program. / Byberg, J R; Jørgensen, Flemming Steen; Hansen, S; Hough, E.
In: Proteins: Structure, Function, and Bioinformatics, Vol. 12, No. 4, 1992, p. 331-8.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Substrate-enzyme interactions and catalytic mechanism in phospholipase C
T2 - a molecular modeling study using the GRID program
AU - Byberg, J R
AU - Jørgensen, Flemming Steen
AU - Hansen, S
AU - Hough, E
PY - 1992
Y1 - 1992
N2 - 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.
AB - 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.
KW - Binding Sites
KW - Catalysis
KW - Computer Simulation
KW - Models, Molecular
KW - Oxygen
KW - Phosphates
KW - Quaternary Ammonium Compounds
KW - Software
KW - Substrate Specificity
KW - Type C Phospholipases
KW - Zinc
U2 - 10.1002/prot.340120405
DO - 10.1002/prot.340120405
M3 - Journal article
C2 - 1579567
VL - 12
SP - 331
EP - 338
JO - Proteins: Structure, Function, and Bioinformatics
JF - Proteins: Structure, Function, and Bioinformatics
SN - 0887-3585
IS - 4
ER -
ID: 38394585