Substrate Binding and Catalytic Mechanism in Phospholipase C from Bacillus cereus

Autor: Flemming Jørgensen, Jette Raun Byberg Buur, Dorthe da Graça Thrige
Rok vydání: 1997
Předmět:
Zdroj: Interacting Protein Domains ISBN: 9783642645839
DOI: 10.1007/978-3-642-60848-3_15
Popis: Phospholipase C from Bacillus cereus (PLCBc,) is a monomeric extracellular zinc containing enzyme consisting of 245 amino acids. l Like other PLCs it cleaves membrane phospholipids at the phospho moiety liberating the polar head group and sn-1,2-diacylglycerol (DAG) or ceramide. Although PLCBc, is a non-specific enzyme, it prefers phosphatidylcholine (PC) as a substrate. In bacteria PLC is part of a phosphate retrieval system, and in mammals PLC plays an important role in generation of second messengers, which are involved in control of cell metabolism, differentiation and growth.2,3 Presently, no structural information on mammalian PC-PLCs is available, but PLCBc, is regarded as a useful model of mammalian PC-PLCs, since antibodies against PLCBc, cross react with a PC-PLC in mammalian cells4 and since they neutralize the PC-PLC activity in Xenopus Oocytes.5,6
Databáze: OpenAIRE