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Literature summary extracted from

  • Hoffmann, I.; Jerneren, F.; Garscha, U.; Oliw, E.H.
    Expression of 5,8-LDS of Aspergillus fumigatus and its dioxygenase domain. A comparison with 7,8-LDS, 10-dioxygenase, and cyclooxygenase (2010), Arch. Biochem. Biophys., 506, 216-222.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.13.11.60 expression in Escherichia coli and in insect cells Gaeumannomyces graminis
1.13.11.60 expression in Escherichia coli and in insect cells Aspergillus fumigatus
5.4.4.5 expression in Escherichia coli and in insect cells Aspergillus fumigatus

Protein Variants

EC Number Protein Variants Comment Organism
1.13.11.60 C1006S the hydroperoxide isomerase activity of 5,8-LDS mutant is abolished Aspergillus fumigatus
1.13.11.60 C1006S/V328F the mutant forms after reduction of hydroperoxides to alcohols, (8R)-hydroperoxy-(9Z,12Z)-octadecadienoic acid and (10R)-hydroxy-(8E,12Z)-octadecadienoic acid in the same relative amounts Aspergillus fumigatus
1.13.11.60 C1006S/V328L the mutant forms after reduction of hydroperoxides to alcohols, (8R)-hydroperoxy-(9Z,12Z)-octadecadienoic acid and (10R)-hydroxy-(8E,12Z)-octadecadienoic acid in the same relative amounts Aspergillus fumigatus
1.13.11.60 C1006S/V328S the mutant forms after reduction of hydroperoxides to alcohols, (8R)-hydroperoxy-(9Z,12Z)-octadecadienoic acid and (10R)-hydroxy-(8E,12Z)-octadecadienoic acid in the same relative amounts Aspergillus fumigatus
1.13.11.60 additional information 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 Aspergillus fumigatus
1.13.11.60 additional information replacements of Tyr and Cys in the conserved YRWH and FXXGPHXCLG sequences abolished 8R-dioxygenase and hydroperoxide isomerase activities, respectively. N-terminal expression constructs of 5,8- and 7,8-LDS (674 of 1079, and 673 of 1165 residues), containing one additional alpha-helix compared to cyclooxygenase-1, yields prominent 8R-DOX activities with apparently unchanged or slightly lower substrate affinities, respectively Aspergillus fumigatus
1.13.11.60 Y374F mutation in the conserved sequence YRWH results in loss of linoleate 8R-lipoxygenase activity, whereas the hydroperoxide isomerase activity is retained Aspergillus fumigatus
5.4.4.5 C1006S the hydroperoxide isomerase activity of 5,8-LDS mutant is abolished Aspergillus fumigatus
5.4.4.5 additional information 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 Aspergillus fumigatus
5.4.4.5 Y374F mutation in the conserved sequence YRWH results in loss of linoleate 8R-lipoxygenase activity, whereas the hydroperoxide isomerase activity is retained Aspergillus fumigatus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.13.11.60 additional information
-
additional information kinetic data of truncated enzymes Gaeumannomyces graminis
1.13.11.60 additional information
-
additional information kinetic data of truncated enzymes Aspergillus fumigatus
5.4.4.5 additional information
-
additional information kinetic data of truncated enzymes Aspergillus fumigatus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.13.11.60 linoleate + O2 Gaeumannomyces graminis
-
(8R,10E,12Z)-8-hydroperoxy-10,12-octadecadienoate
-
?
1.13.11.60 linoleate + O2 Aspergillus fumigatus i.e. (9Z,12Z)-octadeca-9,12-dienoate (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
-
?
1.13.11.60 linoleate + O2 Aspergillus fumigatus all-cis-9,12-octadecadienoic acid (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate
-
?
5.4.4.5 (8R,9Z,12Z)-8-hydroperoxy-10,12-octadecadienoate Aspergillus fumigatus
-
(7S,8S,9Z,12Z)-7,8-dihydroxyoctadeca-9,12-dienoate
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.13.11.60 Aspergillus fumigatus
-
-
-
1.13.11.60 Aspergillus fumigatus C1KH66
-
-
1.13.11.60 Gaeumannomyces graminis
-
-
-
5.4.4.5 Aspergillus fumigatus C1KH66
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.13.11.60 mycelium
-
Gaeumannomyces graminis
-
1.13.11.60 mycelium
-
Aspergillus fumigatus
-
5.4.4.5 mycelium
-
Aspergillus fumigatus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.11.60 (11Z)-icosa-11-enoate + O2
-
Aspergillus fumigatus ?
-
?
1.13.11.60 (11Z,14Z)-icosa-11,14-dienoic acid + O2
-
Aspergillus fumigatus ?
-
?
1.13.11.60 alpha-linolenate + O2
-
Aspergillus fumigatus ?
-
?
1.13.11.60 elaidate + O2
-
Aspergillus fumigatus ?
-
?
1.13.11.60 linoleate + O2
-
Gaeumannomyces graminis (8R,10E,12Z)-8-hydroperoxy-10,12-octadecadienoate
-
?
1.13.11.60 linoleate + O2 i.e. (9Z,12Z)-octadeca-9,12-dienoate Gaeumannomyces graminis (8R,10E,12Z)-8-hydroperoxy-10,12-octadecadienoate
-
?
1.13.11.60 linoleate + O2 i.e. (9Z,12Z)-octadeca-9,12-dienoate Aspergillus fumigatus (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
-
?
1.13.11.60 linoleate + O2 all-cis-9,12-octadecadienoic acid Aspergillus fumigatus (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate
-
?
1.13.11.60 additional information the recombinant enzyme expressed in insect cells, oxygenates 16:1n-7, 18:1n-7, 18:2n-6, 18:3n-3, 20:1n-9, 20:1n-11, and 20:2n-6 at the allylic carbon closest to the carboxyl group Gaeumannomyces graminis ?
-
?
1.13.11.60 palmitoleate + O2
-
Aspergillus fumigatus ?
-
?
5.4.4.5 (8R,9Z,12Z)-8-hydroperoxy-10,12-octadecadienoate
-
Aspergillus fumigatus (7S,8S,9Z,12Z)-7,8-dihydroxyoctadeca-9,12-dienoate
-
?
5.4.4.5 (8R,9Z,12Z)-9-hydroperoxy-10,12-octadecadienoate
-
Aspergillus fumigatus (5S,8R,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate
-
?

Synonyms

EC Number Synonyms Comment Organism
1.13.11.60 5,8-LDS
-
Aspergillus fumigatus
1.13.11.60 5,8-LDS bifunctional enzyme Aspergillus fumigatus
1.13.11.60 5,8-linoleate diol synthase
-
Aspergillus fumigatus
1.13.11.60 5,8-linoleate diol synthase bifunktional enzyme Aspergillus fumigatus
1.13.11.60 7,8-LDS bifunctional enzyme Gaeumannomyces graminis
1.13.11.60 7,8-linoleate diol synthase bifunktional enzyme Gaeumannomyces graminis
1.13.11.60 8-DOX
-
Aspergillus fumigatus
1.13.11.60 8-DOX
-
Gaeumannomyces graminis
1.13.11.60 8R-dioxygenase
-
Aspergillus fumigatus
5.4.4.5 5,8-LDS bifunctional enzyme Aspergillus fumigatus
5.4.4.5 5,8-linoleate diol synthase bifunctional enzyme Aspergillus fumigatus

General Information

EC Number General Information Comment Organism
1.13.11.44 additional information expression of enzyme residues 1-673, 7,8-LDS_1-673, results in only 8-DOX activity, and of residues 1-643, 7,8-LDS_1-643, in undetectable activity Aspergillus fumigatus
1.13.11.60 malfunction replacements of Tyr and Cys in the conserved YRWH and FXXGPHXCLG sequences abolished 8R-dioxygenase and hydroperoxide isomerase activities, respectively Aspergillus fumigatus
1.13.11.60 additional information Val-328 of 5,8-LDS does not influence the position of oxygenation in contrast to the homologous residues Val-349 of COX-1 and Leu-384 of 10R-dioxygenase. About 675 amino acids are sufficient to support 8-DOX activity Aspergillus fumigatus