37443-67-7Relevant articles and documents
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Tsuji,J.,Yasuda,H.
, p. 133 - 135 (1977)
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PpoC from Aspergillus nidulans is a fusion protein with only one active haem
Brodhun, Florian,Schneider, Stefan,Goebel, Cornelia,Hornung, Ellen,Feussner, Ivo
experimental part, p. 553 - 565 (2011/02/23)
In Aspergillus nidulans Ppos [psi (precocious sexual inducer)-producing oxygenases] are required for the production of so-called psi factors, compounds that control the balance between the sexual and asexual life cycle of the fungus. The genome of A. nidulans harbours three different ppo genes: ppoA, ppoB and ppoC. For all three enzymes two different haem-containing domains are predicted: a fatty acid haem peroxidase/ dioxygenase domain in the N-terminal region and a P450 haem-thiolate domain in the C-terminal region. Whereas PpoA was shown to use both haem domains for its bifunctional catalytic activity (linoleic acid 8-dioxygenation and 8-hydroperoxide isomerization), we found that PpoC apparently only harbours a functional haem peroxidase/dioxygenase domain. Consequently, we observed that PpoC catalyses mainly the dioxygenation of linoleic acid (18:2Δ 9Z,12Z), yielding 10-HPODE (10-hydroperoxyoctadecadienoic acid). No isomerase activity was detected. Additionally, 10-HPODE was converted at lower rates into 10-KODE (10-keto-octadecadienoic acid) and 10-HODE (10-hydroxyoctadecadienoic acid). In parallel, decomposition of 10-HPODE into 10-ODA (10-octadecynoic acid) and volatile C-8 alcohols that are, among other things, responsible for the characteristic mushroom flavour. Besides these principle differences we also found that PpoA and PpoC can convert 8-HPODE and 10-HPODE into the respective epoxy alcohols: 12,13-epoxy-8-HOME (where HOME is hydroxyoctadecenoic acid) and 12,13-epoxy-10-HOME. By using site-directed mutagenesis we demonstrated that both enzymes share a similar mechanism for the oxidation of 18:2Δ9Z,12Z; they both use a conserved tyrosine residue for catalysis and the directed oxygenation at the C-8 and C-10 is most likely controlled by conserved valine/leucine residues in the dioxygenase domain. The Authors Journal compilation
A NEW ROUTE FOR THE SYNTHESIS OF 10-HYDROXYDEC-2E-ENOIC AND DEC-2E-ENEDIOIC ACIDS
Odinokov, V. N.,Ishmuratov, G. Yu.,Tolstikov, G. A.
, p. 658 - 660 (2007/10/02)
A new simple route for the synthesis of 10-hydroxydec-2E-enoic and dec-2E-enedioic acids from cycloocta-1Z,5Z-diene has been developed.
