The enzyme contains heme . The bifunctional enzyme from Aspergillus nidulans uses different heme domains to catalyse two separate reactions. Linoleic acid is oxidized within the N-terminal heme peroxidase domain to (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate (cf. EC 1.13.11.60, linoleate 8R-lipoxygenase), which is subsequently isomerized to (5S,8R,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate within the C-terminal P-450 heme thiolate domain .
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The enzyme appears in viruses and cellular organisms
The enzyme contains heme [3]. The bifunctional enzyme from Aspergillus nidulans uses different heme domains to catalyse two separate reactions. Linoleic acid is oxidized within the N-terminal heme peroxidase domain to (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate (cf. EC 1.13.11.60, linoleate 8R-lipoxygenase), which is subsequently isomerized to (5S,8R,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate within the C-terminal P-450 heme thiolate domain [3].
i.e. (9Z,12Z)-octadeca-9,12-dienoate. Mechanism of biosynthesis: the enzyme oxidizes linoleic acid to (8R)-hydroperoxylinoleic acid and to (5S,8R)-dihydroxylinoleic acids as major products. This occurs by abstraction of the pro-S hydrogen at C-8 and antarafacial dioxygenation at C-8 or at C-10 with double bond migration. (8R,9Z,12Z)-8-Hydroperoxy-9,12-octadecadienoate is then isomerized to (5S,8R,9Z,12Z)-5,8-dihydroperoxy-9,12-octadecadienoate by abstraction of the pro-S hydrogens at C-5 of (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate, respectively, followed by suprafacial oxygenation
the enzyme is involved in the regulation of the life cycle of Aspergillus nidulans. Synthesis of the psi factor (8R,9E,12Z)-8-hydroperoxy-9,12-octadecadienoate, that influences the development of the asexual conidiophores and sexual cleistothecia
the N-terminal heme peroxidase domain is responsible for the dioxygenase reaction as the first step of the PpoA reaction, i.e. oxidation of linoleic acid to (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate as an intermediate product. The C-terminal P450 domain catalyzes the second reaction step, the isomerization of (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate to (5S,8R,9Z,12Z)-5,8-dihydroxy-9,12-octadecadienoate, and is therefore termed the 8-hydroperoxide isomerase P450 domain
the enzyme is involved in the regulation of the life cycle of Aspergillus nidulans. Synthesis of the psi factor (8R,9E,12Z)-8-hydroperoxy-9,12-octadecadienoate, that influences the development of the asexual conidiophores and sexual cleistothecia
PpoA contains a high spin ferriheme. PpoA uses different heme domains to catalyze two separate reactions. Within the heme peroxidase domain, linoleic acid is oxidized to (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate by abstracting a H-atom from C-8 of the fatty acid, yielding a carbon-centered radical that reacts with molecular dioxygen. In the second reaction step, (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate is isomerized within the P450 heme thiolate domain to (5S,8R,9Z,12Z)-5,8-dihydroxy-9,12-octadecadienoate
mutation in the conserved sequence YRWH results in loss of linoleate 8R-lipoxygenase activity, whereas the hydroperoxide isomerase activity is retained
the mutant enzyme shows no detectable activity when incubated with (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate as a substrate. When incubated with the intermediate product (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoateit it is able to catalyze isomerization to (5S,8R,9Z,12Z)-5,8-dihydroperoxy-9,12-octadecadienoate
replacements of Tyr and Cys in the conserved YRWH and FXXGPHXCLG sequences abolishes 8R-dioxygenase (8-DOX) and hydroperoxide isomerase activities, respectively. Val328 of 5,8-LDS does not influence the position of oxygenation