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

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

\rightleftharpoons

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

This enzyme contains heme.

References

↑ Hoffmann, I., Jerneren, F., Garscha, U. and 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.
↑ Jerneren, F., Garscha, U., Hoffmann, I., Hamberg, M. and 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.
↑ Brodhun, F., Gobel, C., Hornung, E. and 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 2673248. PMID 19286665.

External links

9,12-octadecadienoate 8-hydroperoxide 8R-isomerase at the US National Library of Medicine Medical Subject Headings (MeSH)

Isomerase: mutases (EC 5.4)

5.4.1 Acyl Groups	Lysolecithin acylmutase Precorrin-8X methylmutase

5.4.2 Phosphomutases	Phosphoglycerate mutase Bisphosphoglycerate mutase Phosphoglucomutase Phosphomannomutase PMM1 PMM2

5.4.99 Other groups	Methylmalonyl-CoA mutase Lanosterol synthase

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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