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Literature summary extracted from
- Pichia expression and mutagenesis of 7,8-linoleate diol synthase change the dioxygenase and hydroperoxide isomerase (2008), Biochem. Biophys. Res. Commun., 373, 579-583.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.13.11.60 | expression in Pichia pastoris changes the position and stereospecificity of a hydroperoxide isomerase possibly due to N- or O-linked mannosides in the vicinity of the heme group, whereas the 8(R)-dioxygenase activity is identical with native 7,8-linoleate diol synthase | Gaeumannomyces graminis |
| 5.4.4.6 | expression in Pichia pastoris changes the position and stereospecificity of a hydroperoxide isomerase possibly due to N- or O-linked mannosides in the vicinity of the heme group, whereas the 8(R)-dioxygenase activity is identical with native 7,8-linoleate diol synthase | Gaeumannomyces graminis |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 1.13.11.60 | H379Q | inactive mutant enzyme, no 8(R)-dioxygenase activity | Gaeumannomyces graminis |
| 1.13.11.60 | additional information | treatment with alpha-mannosidase to shorten N- and O-linked mannosides inhibis the hydroperoxide isomerase but not the 8(R)-dioxygenase | Gaeumannomyces graminis |
| 1.13.11.60 | N216Q | inactive mutant enzyme, no 8(R)-dioxygenase activity | Gaeumannomyces graminis |
| 5.4.4.6 | H379Q | inactive mutant enzyme | Gaeumannomyces graminis |
| 5.4.4.6 | additional information | treatment with alpha-mannosidase to shorten N- and O-linked mannosides inhibis the hydroperoxide isomerase but not the 8(R)-dioxygenase | Gaeumannomyces graminis |
| 5.4.4.6 | N216Q | inactive mutant enzyme | Gaeumannomyces graminis |
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,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate | - |
? |  |
| 1.13.11.60 | linoleate + O2 | Gaeumannomyces graminis var. avenae | - |
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate | - |
? | |
| 5.4.4.6 | (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate | Gaeumannomyces graminis | - |
(7S,8S,9Z,12Z)-7,8-dihydroxy-9,12-octadecadienoate | - |
? | |
| 5.4.4.6 | (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate | Gaeumannomyces graminis var. avenae | - |
(7S,8S,9Z,12Z)-7,8-dihydroxy-9,12-octadecadienoate | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.13.11.60 | Gaeumannomyces graminis | - |
- |
- |
| 1.13.11.60 | Gaeumannomyces graminis var. avenae | - |
- |
- |
| 5.4.4.6 | Gaeumannomyces graminis | - |
- |
- |
| 5.4.4.6 | Gaeumannomyces graminis | Q9UUS2 | - |
- |
| 5.4.4.6 | Gaeumannomyces graminis var. avenae | - |
- |
- |
| 5.4.4.6 | Gaeumannomyces graminis var. avenae | Q9UUS2 | - |
- |
Posttranslational Modification
| EC Number | Posttranslational Modification | Comment | Organism |
|---|---|---|---|
| 1.13.11.60 | glycoprotein | 7,8-LDS contains five tentative N-linked glycosylation sites, one of which has high probability of glycosylation. This N-glycosylation site, Asn216, is located near the distal heme-binding region along with tentative sites for O-linked glycosylation. Asn216Gln shows no detectable enzyme activity, although expression of Asn216Gln is confirmed by Western blot analysis. alpha-Mannosidase treatment does not change the 8R-dioxygenase activity but abolishes the hydroperoxide isomerase activity. Proper N- and O-linked glycosylation could be important for the hydroperoxide isomerase. Expression of 7,8-LDS in insect cells yields recombinant 7,8-LDS with the native hydroperoxide isomerase activity | Gaeumannomyces graminis |
| 5.4.4.6 | glycoprotein | 7,8-LDS contains five tentative N-linked glycosylation sites, one of which has high probability of glycosylation. This N-glycosylation site, Asn216, is located near the distal heme-binding region along with tentative sites for O-linked glycosylation. Asn216Gln shows no detectable enzyme activity, although expression of Asn216Gln is confirmed by Western blot analysis. alpha-Mannosidase treatment does not change the 8R-dioxygenase activity but abolishes the hydroperoxide isomerase activity. Proper N- and O-linked glycosylation could be important for the hydroperoxide isomerase. Expression of 7,8-LDS in insect cells yields recombinant 7,8-LDS with the native hydroperoxide isomerase activity | Gaeumannomyces graminis |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.13.11.60 | - |
Gaeumannomyces graminis |
| 5.4.4.6 | - |
Gaeumannomyces graminis |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.13.11.60 | linoleate + O2 | - |
Gaeumannomyces graminis | (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate | - |
? | |
| 1.13.11.60 | linoleate + O2 | expression in Pichia pastoris changes the position and stereospecificity of a hydroperoxide isomerase. The recombinant enzyme forms (5S,8R)-dihydroxylinoleic acid (60% 5S) and 8R,13-dihydroxyoctadeca-(9E,11E)-dienoic acid possibly due to N- or O-linked mannosides in the vicinity of the heme group, whereas the 8R-dioxygenase activity is identical with native 7,8-linoleate diol synthase | Gaeumannomyces graminis | (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate | - |
? | |
| 1.13.11.60 | linoleate + O2 | - |
Gaeumannomyces graminis var. avenae | (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate | - |
? | |
| 1.13.11.60 | linoleate + O2 | expression in Pichia pastoris changes the position and stereospecificity of a hydroperoxide isomerase. The recombinant enzyme forms (5S,8R)-dihydroxylinoleic acid (60% 5S) and 8R,13-dihydroxyoctadeca-(9E,11E)-dienoic acid possibly due to N- or O-linked mannosides in the vicinity of the heme group, whereas the 8R-dioxygenase activity is identical with native 7,8-linoleate diol synthase | Gaeumannomyces graminis var. avenae | (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate | - |
? | |
| 5.4.4.6 | (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate | - |
Gaeumannomyces graminis | (7S,8S,9Z,12Z)-7,8-dihydroxy-9,12-octadecadienoate | - |
? | |
| 5.4.4.6 | (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate | expression in Pichia pastoris changes the position and stereospecificity of a hydroperoxide isomerase (the recombinant enzyme forms 5,8(R)-dihydroxylinoleic acid (60% 5S) and 8(R),13-dihydroxyoctadeca-(9E,11E)-dienoic acid) possibly due to N- or O-linked mannosides in the vicinity of the heme group, whereas the (8R)-dioxygenase activity is identical with native 7,8-linoleate diol synthase | Gaeumannomyces graminis | (7S,8S,9Z,12Z)-7,8-dihydroxy-9,12-octadecadienoate | - |
? | |
| 5.4.4.6 | (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate | - |
Gaeumannomyces graminis var. avenae | (7S,8S,9Z,12Z)-7,8-dihydroxy-9,12-octadecadienoate | - |
? | |
| 5.4.4.6 | (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate | expression in Pichia pastoris changes the position and stereospecificity of a hydroperoxide isomerase (the recombinant enzyme forms 5,8(R)-dihydroxylinoleic acid (60% 5S) and 8(R),13-dihydroxyoctadeca-(9E,11E)-dienoic acid) possibly due to N- or O-linked mannosides in the vicinity of the heme group, whereas the (8R)-dioxygenase activity is identical with native 7,8-linoleate diol synthase | Gaeumannomyces graminis var. avenae | (7S,8S,9Z,12Z)-7,8-dihydroxy-9,12-octadecadienoate | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.13.11.60 | 7,8-LDS | - |
Gaeumannomyces graminis |
| 1.13.11.60 | 8(R)-dioxygenase | - |
Gaeumannomyces graminis |
| 5.4.4.6 | 7,8-LDS | - |
Gaeumannomyces graminis |
| 5.4.4.6 | 7,8-LDS | bifunctional enzyme | Gaeumannomyces graminis |
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