Prostaglandin endoperoxide synthetase from bovine vesicular gland microsomes. Inactivation and activation by heme and other metalloporphyrins.

Ogino, Nobuchika; Ohki, S; Yamamoto, Shozo; Hayaishi, Osamu

doi:10.1016/s0021-9258(17)34657-4

Cited by 158 publications

(24 citation statements)

References 18 publications

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“…A number of authors have reported that prostaglandin biosynthesis is markedly stimulated by hemes and heme proteins (Yoshimoto et al, 1970;Ogino et al, 1978;Hemler et al, 1978). 1.8 ± 0.5 Fe3+ADP…”

Section: Resultsmentioning

confidence: 99%

Peroxidatic oxidation of benzo[a]pyrene and prostaglandin biosynthesis

Marnett¹,

Reed²

1979

Biochemistry

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The arachidonic acid dependent oxidation of benzo[a]pyrene to a mixture of 3,6-, 1,6-, and 6,12-quinones has been studied by using enzyme preparations from sheep seminal vesicles. Maximal oxidation is observed at 100 microM benzo[a]pyrene and 150 microM arachidonic acid. The arachidonic acid dependent oxidation is peroxidatic and utilizes prostaglandin G2 (PGG2), generated in situ from arachidonate, as the hydroperoxide substrate. 15-Hydroperoxy-5,8,11,13-eicosatetraenoic acid is equivalent to PGG2 as a hydroperoxide substrate, but hydrogen peroxide, cumene hydroperoxide, and tert-butyl hydroperoxide are much poorer substrates. Arachidonic acid dependent benzo[a]pyrene oxidation by microsomal and solubilized enzyme preparations is markedly.

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Section: Resultsmentioning

confidence: 99%

Peroxidatic oxidation of benzo[a]pyrene and prostaglandin biosynthesis

Marnett¹,

Reed²

1979

Biochemistry

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“…The peroxidase function must also be discussed briefly in light of its role in activation of the system . It is of note that the enzyme containing Mn-substituted protophyrin IX (PPIX) has cyclooxygenase activity but not the peroxidase function. , …”

Section: C–c Bond Forming Reactionsmentioning

confidence: 99%

“…143 It is of note that the enzyme containing Mnsubstituted protophyrin IX (PPIX) has cyclooxygenase activity but not the peroxidase function. 142,144 The catalytic mechanism involves initial abstraction of the 13pro-(S) hydrogen atom of arachidonic acid (Figure 29). 142 The resulting radical reacts with O 2 to form a peroxy radical, which then reacts with the 8,9-double bond to form a 9,11endoperoxide and move the radical to carbon 8.…”

Section: Prostaglandin Synthesismentioning

confidence: 99%

Formation and Cleavage of C–C Bonds by Enzymatic Oxidation–Reduction Reactions

2018

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Many oxidation-reduction (redox) enzymes, particularly oxygenases, have roles in reactions that make and break C-C bonds. The list includes cytochrome P450 and other heme-based monooxygenases, heme-based dioxygenases, nonheme iron mono- and dioxygenases, flavoproteins, radical S-adenosylmethionine enzymes, copper enzymes, and peroxidases. Reactions involve steroids, intermediary metabolism, secondary natural products, drugs, and industrial and agricultural chemicals. Many C-C bonds are formed via either (i) coupling of diradicals or (ii) generation of unstable products that rearrange. C-C cleavage reactions involve several themes: (i) rearrangement of unstable oxidized products produced by the enzymes, (ii) oxidation and collapse of radicals or cations via rearrangement, (iii) oxygenation to yield products that are readily hydrolyzed by other enzymes, and (iv) activation of O in systems in which the binding of a substrate facilitates O activation. Many of the enzymes involve metals, but of these, iron is clearly predominant.

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“…On the other hand, there are three forms of the enzyme which exhibit little or no peroxidase activity but which retain the ability to catalyze the cyclooxygenase reaction. These include (a) holoenzyme in which Fe3+ heme is replaced with Mn3+ heme (Ogino et al, 1978;Hemler et al, 1978a), (b) holoenzyme incubated in the presence of 250 mM NaCN (Hemler & Lands, 1980), and (c) a PGH synthase 1 mutant in which His386 (Figure 3) has been substituted with either an alanine or a glutamine residue (Shimokawa & Smith, 1991).…”

mentioning

confidence: 99%

Tyrosyl radicals and their role in hydroperoxide-dependent activation and inactivation of prostaglandin endoperoxide synthase

Smith

Eling

Kulmacz³

et al. 1992

Biochemistry

134

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I^ostaglandin endoperoxide (PGH) synthase catalyzes the formation of prostaglandin endoperoxide H2 (PGH2) from arachidonic acid [Figure 1; see for a recent review]. This is the central reaction in prostaglandin biosynthesis. In intact cells, arachidonic acid, cleaved in a hormone-dependent manner from glycerophospholipids, is converted to PGH2 through the action of PGH synthase, and then, depending on the cell type, PGH2 is enzymically isomerized or reduced to PGD2, PGE2, PGF2a, thromboxane A2 (TxA2), or prostacyclin (PGI2). PGH synthase is important thera-

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Prostaglandin endoperoxide synthetase from bovine vesicular gland microsomes. Inactivation and activation by heme and other metalloporphyrins.

Cited by 158 publications

References 18 publications

Peroxidatic oxidation of benzo[a]pyrene and prostaglandin biosynthesis

Peroxidatic oxidation of benzo[a]pyrene and prostaglandin biosynthesis

Formation and Cleavage of C–C Bonds by Enzymatic Oxidation–Reduction Reactions

Tyrosyl radicals and their role in hydroperoxide-dependent activation and inactivation of prostaglandin endoperoxide synthase

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