Psi-factor producing oxygenase, N-terminal heme peroxidase domain (IPR034812)

Short name: Ppo_N

Overlapping homologous superfamilies

Domain relationships



This entry represents the N-terminal heme peroxidase domain of Psi-factor producing oxygenase and related proteins.

Oxylipins may be synthesized via multi step processes that consist of dioxygenation and isomerization of the intermediately formed hydroperoxy fatty acid. These processes are typically catalyzed by two distinct enzyme classes: dioxygenases and cytochrome P450 enzymes. In fungi both enzymatic activities are combined in a single bifunctional enzyme and are known as are named Psi-factor producing oxygenases (Ppo) [PMID: 23797010]. These enzymes consist of an N-terminal heme peroxidase domain and a C-terminal cytochrome P450 domain.

These fungal enzymes, related to animal heme peroxidases, catalyze the oxygenation of linoleate and similar targets. They are responsible for the synthesis of various fatty acid-derived oxylipins. Linoleate diol synthase from Gaeumannomyces graminis catalyzes the dioxygenation of linoleic acid to (8R)-hydroperoxylinoleate and isomerization of the resulting hydroperoxide to (7S,8S)-dihydroxylinoleate [PMID: 8662736, PMID: 10497176]. Other members are 5,8-linoleate dioxygenase (ppoA) and linoleate 10R-dioxygenase (ppoC) [PMID: 16040966, PMID: 19289462].

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0016491 oxidoreductase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
  • cd09817 (linoleate_diol_synthase_like)