Title : The molecular basis of phosphatidylcholine preference of human group-V phospholipase A2.

Pub. Date : 2000 Jun 15

PMID : 10839997






4 Functional Relationships(s)
Download
Sentence
Compound Name
Protein Name
Organism
1 We showed that hVPLA(2) can bind phosphatidylcholine membranes and hydrolyse phosphatidylcholine molecules much more efficiently than human group-IIa PLA(2), which accounts for its high activity on the outer plasma membrane of mammalian cells. Phosphatidylcholines phospholipase A2 group V Homo sapiens
2 We showed that hVPLA(2) can bind phosphatidylcholine membranes and hydrolyse phosphatidylcholine molecules much more efficiently than human group-IIa PLA(2), which accounts for its high activity on the outer plasma membrane of mammalian cells. Phosphatidylcholines phospholipase A2 group V Homo sapiens
3 To understand the molecular basis of the high phosphatidylcholine specificity of hVPLA(2), we mutated several residues (Gly-53, Glu-56 and Glu-57) that might be involved in interaction with an active-site-bound phospholipid molecule. Phosphatidylcholines phospholipase A2 group V Homo sapiens
4 Together, these steric and electrostatic properties of the active site of hVPLA(2) allow for effective binding and hydrolysis of a bulky cationic choline head group of phosphatidylcholine, which is unique among mammalian secretory PLA(2)s. Phosphatidylcholines phospholipase A2 group V Homo sapiens