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

J. M. Gerrard; D. A. Peterson

doi:10.1016/0262-1746(84)90003-9

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

J. M. Gerrard, D. A. Peterson

Research output: Contribution to journal › Article › peer-review

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Abstract

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.

Original language	English (US)
Pages (from-to)	139-142
Number of pages	4
Journal	Prostaglandins, Leukotrienes and Medicine
Volume	13
Issue number	2
DOIs	https://doi.org/10.1016/0262-1746(84)90003-9
State	Published - Feb 1984
Externally published	Yes

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title = "Structure of the active site of prostaglandin synthase from studies of depsides: An alternate view",

abstract = "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.",

author = "Gerrard, {J. M.} and Peterson, {D. A.}",

year = "1984",

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AU - Peterson, D. A.

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AB - 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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ER -

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

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