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Literature summary for 1.13.11.60 extracted from

  • Garscha, U.; Oliw, E.
    Pichia expression and mutagenesis of 7,8-linoleate diol synthase change the dioxygenase and hydroperoxide isomerase (2008), Biochem. Biophys. Res. Commun., 373, 579-583.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
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

Protein Variants Comment Organism
H379Q inactive mutant enzyme, no 8(R)-dioxygenase activity Gaeumannomyces graminis
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
N216Q inactive mutant enzyme, no 8(R)-dioxygenase activity Gaeumannomyces graminis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
linoleate + O2 Gaeumannomyces graminis
-
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
-
?
linoleate + O2 Gaeumannomyces graminis var. avenae
-
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
-
?

Organism

Organism UniProt Comment Textmining
Gaeumannomyces graminis
-
-
-
Gaeumannomyces graminis var. avenae
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
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)

Purification (Comment) Organism
-
Gaeumannomyces graminis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
linoleate + O2
-
Gaeumannomyces graminis (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
-
?
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
-
?
linoleate + O2
-
Gaeumannomyces graminis var. avenae (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
-
?
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
-
?

Synonyms

Synonyms Comment Organism
7,8-LDS
-
Gaeumannomyces graminis
8(R)-dioxygenase
-
Gaeumannomyces graminis