Abstract
It has long been proposed that the higher activity of phospholipase A2 (PLA2) for substrates presented as multimolecular aggregates compared to dispersed molecules (interfacial activation) arises due to a conformational change in the enzyme. X-ray studies have, however, failed to identify any such change. Here we report the solution structures of porcine pancreatic PLA2 both free and as a ternary complex with micelles and a competitive inhibitor. Important differences between these structures indicate that conformational changes may play an important role in the mechanism of interfacial activation in PLA2s.
Original language | English |
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Pages (from-to) | 402-406 |
Number of pages | 5 |
Journal | Nature Structural Biology |
Volume | 2 |
Issue number | 5 |
DOIs | |
Publication status | Published - 1 May 1995 |
Keywords
- phospholipase A2
- article
- competitive inhibition
- conformational transition
- enzyme activation
- enzyme activity
- enzyme conformation
- nonhuman
- nuclear magnetic resonance
- priority journal
- structure analysis
- pig