Research Article| Volume 13, ISSUE 2, P139-142, February 1984

Structure of the active site of prostaglandin synthase from studies of depsides: An alternate view

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      Evaluation of the structure of the lichen depside, 4-0-methylcryptochlorophaeic acid, the most potent inhibitor of prostaglandin synthesis known, and its potential interaction with heme supports a model of the active site of prostaglandin synthase initially suggested by studies of arachidonic acid-heme interaction.
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