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

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

doi:10.1002/prot.340120405

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

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

22 Citationer (Scopus)

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.

Originalsprog	Engelsk
Tidsskrift	Proteins: Structure, Function, and Bioinformatics
Vol/bind	12
Udgave nummer	4
Sider (fra-til)	331-8
Antal sider	8
ISSN	0887-3585
DOI	https://doi.org/10.1002/prot.340120405
Status	Udgivet - 1992

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10.1002/prot.340120405

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@article{a963bfbef76e410eb08f405d795aa887,

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

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.",

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

author = "Byberg, {J R} and J{\o}rgensen, {Flemming Steen} and S Hansen and E Hough",

year = "1992",

doi = "10.1002/prot.340120405",

language = "English",

volume = "12",

pages = "331--8",

journal = "Proteins: Structure, Function, and Bioinformatics",

issn = "0887-3585",

publisher = "JohnWiley & Sons, Inc.",

number = "4",

}

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

SN - 0887-3585

VL - 12

SP - 331

EP - 338

JO - Proteins: Structure, Function, and Bioinformatics

JF - Proteins: Structure, Function, and Bioinformatics

IS - 4

ER -

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

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