Active site and catalytic mechanism of phospholipa...[Nature. 1981]

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1: Nature. 1981 Feb 12;289(5798):604-6.Links

Active site and catalytic mechanism of phospholipase A2.

Dijkstra BW, Drenth J, Kalk KH.

The esterolytic enzyme phospholipase A2 specificially splits the 2-acyl linkage of phosphoglycerides in a calcium-dependent reaction. In the pancreas the enzyme occurs as a zymogen which is activated on secretion into the duodenal tract by the removal of seven amino acid residues from the N terminus by trypsin. Having refined our X-ray analysis of the crystal structure of bovine pancreatic phospholipase A2 from 2.4 A (ref. 4) to 1.7 A resolution, we now describe how the structure of the molecule may account for the specificity of the enzyme and for the sudden and dramatic change in activity when the substrate concentration passes the critical micelle concentration.

PMID: 7464926 [PubMed - indexed for MEDLINE]

Role of the N-terminus in the interaction of pancreatic phospholipase A2 with aggregated substrates. Properties and crystal structure of transaminated phospholipase A2. [Biochemistry. 1984]
Binding of porcine pancreatic phospholipase A2 to various micellar substrate analogues. Involvement of histidine-48 and aspartic acid-49 in the binding process. [Biochemistry. 1981]
Catalytic Ca2+-binding site of pancreatic phospholipase A2: laser-induced Eu3+ luminescence study. [Biochemistry. 1985]
ReviewStructure, function and interfacial allosterism in phospholipase A2: insight from the anion-assisted dimer. [Arch Biochem Biophys. 2005]
ReviewPhospholipase A2 at the bilayer interface. [Proteins. 1991]

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Active site and catalytic mechanism of phospholipase A2.

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