5.4.4.6: 9,12-octadecadienoate 8-hydroperoxide 8S-isomerase
This is an abbreviated version!
For detailed information about 9,12-octadecadienoate 8-hydroperoxide 8S-isomerase, go to the full flat file.
Reaction
Synonyms
7,8-diol synthase, 7,8-LDS, 7,8-linoleate diol synthase, EC 1.13.11.44
ECTree
Advanced search results
Posttranslational Modification
Posttranslational Modification on EC 5.4.4.6 - 9,12-octadecadienoate 8-hydroperoxide 8S-isomerase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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
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
-