9,12-octadecadienoate 8-hydroperoxide 8R-isomerase

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9,12-octadecadienoate 8-hydroperoxide 8R-isomerase
Identifiers
EC number 5.4.4.5
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

9,12-octadecadienoate 8-hydroperoxide 8R-isomerase (EC 5.4.4.5, 5,8-LDS (bifunctional enzyme), 5,8-linoleate diol synthase (bifunctional enzyme), 8-hydroperoxide isomerase, (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate mutase ((5S,8R,9Z,12Z)-5,8-dihydroxy-9,12-octadecadienoate-forming), PpoA) is an enzyme with systematic name (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate hydroxymutase ((5S,8R,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate-forming).[1][2][3] This enzyme catalyses the following chemical reaction

(8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate (5S,8R,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate

This enzyme contains heme.

References[edit]

  1. ^ Hoffmann, I.; Jerneren, F.; Garscha, U.; Oliw, E.H. (2011). "Expression of 5,8-LDS of Aspergillus fumigatus and its dioxygenase domain. A comparison with 7,8-LDS, 10-dioxygenase, and cyclooxygenase". Arch. Biochem. Biophys. 506 (2): 216–222. doi:10.1016/j.abb.2010.11.022. PMID 21130068. 
  2. ^ Jerneren, F.; Garscha, U.; Hoffmann, I.; Hamberg, M.; Oliw, E.H. (2010). "Reaction mechanism of 5,8-linoleate diol synthase, 10R-dioxygenase, and 8,11-hydroperoxide isomerase of Aspergillus clavatus". Biochim. Biophys. Acta. 1801 (4): 503–507. doi:10.1016/j.bbalip.2009.12.012. PMID 20045744. 
  3. ^ Brodhun, F.; Gobel, C.; Hornung, E.; Feussner, I. (2009). "Identification of PpoA from Aspergillus nidulans as a fusion protein of a fatty acid heme dioxygenase/peroxidase and a cytochrome P450". J. Biol. Chem. 284: 11792–11805. doi:10.1074/jbc.M809152200. PMC 2673248Freely accessible. PMID 19286665. 

External links[edit]