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Article

Structures and molecular-dynamics studies of three active-site mutants of bovine pancreatic phospholipase A(2).

Acta crystallographica. Section D, Biological crystallography - 1 Oct 2008

Kanaujia Shankar Prasad, Sekar Kanagaraj

Abstract excerpt

Phospholipase A(2) hydrolyzes phospholipids at the sn-2 position to cleave the fatty-acid ester bond of L-glycerophospholipids. The catalytic dyad (Asp99 and His48) along with a nucleophilic water molecule is responsible for enzyme hydrolysis. Furthermore, the residue Asp49 in the calcium-binding loop is essential for controlling the binding of the calcium ion and the catalytic action of phospholipase A(2). To...

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Source

Identifiers

PMID: 18931407
DOI: 10.1107/S0907444908022713

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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