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Digitale Medien

Substrate-enzyme interactions and catalytic mechanism in phospholipase C: A molecular modeling study using the GRID program (1992)

Byberg, Jette R. ; Jørgensen, Flemming S. ; Hansen, Sissel ; [weitere]

New York, NY : Wiley-Blackwell

Proteins: Structure, Function, and Genetics 12 (1992), S. 331-338

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Details

ISSN: 0887-3585

Schlagwort(e): phospholipase C ; molecular modeling ; GRID ; substrate-enzyme interactions ; catalytic mechanism ; Chemistry ; Biochemistry and Biotechnology

Quelle: Wiley InterScience Backfile Collection 1832-2000

Thema: Medizin

Notizen: 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.

Zusätzliches Material: 9 Ill.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1002/prot.340120405

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