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JBC, Vol. 253, Issue 14, 5061-5068, Jul, 1978
N. Ogino, S. Ohki, S. Yamamoto and O. Hayaishi
Prostaglandin endoperoxide synthetase purified to apparent homogeneity from
bovine vesicular gland microsomes contained iron far below the equimolar
amount and essentially no heme. However, the enzyme required various
metalloporphyrins including hematin or several hemoproteins such as
hemoglobin. Preincubation of the enzyme with hematin or hemoglobin resulted
in the loss of enzyme activity. The enzyme inactivation was protected by
tryptophan or various other aromatic compounds. Furthermore, the
simultaneous presence of tryptophan brought about activation of enzyme;
namely, the enzyme preincubated with heme and tryptophan showed an almost
full activity with a heme concentration in the reaction mixture far below
the saturating level. Such inactivation and activation of the enzyme were
also observed with manganese protoporphyrin. An identical heme requirement,
heme-induced inactivation, and activation of the enzyme were observed in
three types of reactions catalyzed by the enzyme: 1) bis-dioxygenation of
8,11,14-eicosatrienoic acid to produce prostaglandin G1, 2)
15-hydroperoxide cleavage of prostaglandin G1 to produce prostaglandin H1,
and 3) guaiacol peroxidation. When heme was replaced by manganese
protoporphyrin, the enzyme catalyzed only the bis-dioxygenation producing
prostaglandin G1 and the activities of the latter two reactions were not
detectable.
Prostaglandin endoperoxide synthetase from bovine vesicular gland microsomes. Inactivation and activation by heme and other metalloporphyrins
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