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Literature summary for 1.13.11.60 extracted from
- 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.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli and in insect cells | Gaeumannomyces graminis |
| expression in Escherichia coli and in insect cells | Aspergillus fumigatus |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| C1006S | the hydroperoxide isomerase activity of 5,8-LDS mutant is abolished | Aspergillus fumigatus |
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 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]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | kinetic data of truncated enzymes | Gaeumannomyces graminis | |
| additional information | - |
additional information | kinetic data of truncated enzymes | Aspergillus fumigatus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| linoleate + O2 | Gaeumannomyces graminis | - |
(8R,10E,12Z)-8-hydroperoxy-10,12-octadecadienoate | - |
? |  |
| linoleate + O2 | Aspergillus fumigatus | i.e. (9Z,12Z)-octadeca-9,12-dienoate | (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate | - |
? | |
| linoleate + O2 | Aspergillus fumigatus | all-cis-9,12-octadecadienoic acid | (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Aspergillus fumigatus | - |
- |
- |
| Aspergillus fumigatus | C1KH66 | - |
- |
| Gaeumannomyces graminis | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| mycelium | - |
Gaeumannomyces graminis | - |
| mycelium | - |
Aspergillus fumigatus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| (11Z)-icosa-11-enoate + O2 | - |
Aspergillus fumigatus | ? | - |
? | |
| (11Z,14Z)-icosa-11,14-dienoic acid + O2 | - |
Aspergillus fumigatus | ? | - |
? | |
| alpha-linolenate + O2 | - |
Aspergillus fumigatus | ? | - |
? | |
| elaidate + O2 | - |
Aspergillus fumigatus | ? | - |
? | |
| linoleate + O2 | - |
Gaeumannomyces graminis | (8R,10E,12Z)-8-hydroperoxy-10,12-octadecadienoate | - |
? | |
| linoleate + O2 | i.e. (9Z,12Z)-octadeca-9,12-dienoate | Gaeumannomyces graminis | (8R,10E,12Z)-8-hydroperoxy-10,12-octadecadienoate | - |
? | |
| linoleate + O2 | i.e. (9Z,12Z)-octadeca-9,12-dienoate | Aspergillus fumigatus | (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate | - |
? | |
| linoleate + O2 | all-cis-9,12-octadecadienoic acid | Aspergillus fumigatus | (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate | - |
? | |
| 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 | ? | - |
? | |
| palmitoleate + O2 | - |
Aspergillus fumigatus | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| 5,8-LDS | - |
Aspergillus fumigatus |
| 5,8-LDS | bifunctional enzyme | Aspergillus fumigatus |
| 5,8-linoleate diol synthase | - |
Aspergillus fumigatus |
| 5,8-linoleate diol synthase | bifunktional enzyme | Aspergillus fumigatus |
| 7,8-LDS | bifunctional enzyme | Gaeumannomyces graminis |
| 7,8-linoleate diol synthase | bifunktional enzyme | Gaeumannomyces graminis |
| 8-DOX | - |
Aspergillus fumigatus |
| 8-DOX | - |
Gaeumannomyces graminis |
| 8R-dioxygenase | - |
Aspergillus fumigatus |
General Information
| General Information | Comment | Organism |
|---|---|---|
| malfunction | replacements of Tyr and Cys in the conserved YRWH and FXXGPHXCLG sequences abolished 8R-dioxygenase and hydroperoxide isomerase activities, respectively | Aspergillus fumigatus |
| 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 |
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