| | 1 | Author
| KenjiM. Atsui, Hiroyuki Shinta, H. Irom, Itsu Toyota, Tadahiko Kajiwara, AkikazuH. Atanaka | Requires cookie* | | | Title
| Comparison of the Substrate Specificities of Lipoxygenases Purified from Soybean Seed, Wheat Seed, and Cucumber Cotyledons  | | | | Abstract
| Lipoxygenases were highly purified from soybean seed, wheat seed and cucumber cotyle dons. Substrate specificities o f these lipoxygenases were studied by using an entire series o f (co6Z ,co9Z)-C 13~C24-dienoic acids as synthetic substrate analogues. Soybean lipoxygenase-1 and cucumber lipoxygenase showed broad specificities for these substrates while wheat lipoxygenase showed narrow specificities. Position o f dioxygenation to each substrate was an alyzed by high performance liquid chromatography. W ith soybean lipoxygenase-1 elongation o f the distance between the terminal carboxyl group and the site o f hydrogen removal in a substrate decreased the positional specificity o f dioxygenation, while, with cucumber lipoxy genase, shortening the distance decreased the specificity. It was suggested that cucumber lipoxygenase and soybean lipoxygenase-1 recognized the terminal carboxyl group o f a sub strate to arrange it only in one orientation at the reaction center. In case o f wheat lipoxygen ase, recognition o f the carboxyl group was thought to have crucial and essential role to secure the activity. | | | |
Reference
| Z. Naturforsch. 47c, 85—8 (1992); received M ay 8/A ugust 27 1991 | | | |
Published
| 1992 | | | |
Keywords
| Lipoxygenase, Cucumber Cotyledons, Soybean Seed, W heat Seed, Substrate Specificity | | | |
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| default:Reihe_C/47/ZNC-1992-47c-0085.pdf | | | | Identifier
| ZNC-1992-47c-0085 | | | | Volume
| 47 | |
| 2 | Author
| Kenji Matsui, Yasushi Shibata, Tadahiko Kajiwara, AkikazuH. Atanaka | Requires cookie* | | | Title
| Separation of 13-and 9-Hydroperoxide Lyase Activities in Cotyledons of Cucumber Seedlings | | | | Abstract
| In cucumber cotyledons, both C6-and C9-aldehyde were formed via hydroperoxide (H PO) lyase activity. Because it has not been elucidated whether these activities are attri buted to one enzym e which can cleave both 13-and 9-H PO or to two or more enzym es each o f which specifically cleaves 13-or 9-H PO , an attempt to separate HPO lyase activity was done. Ion exchange chromatography separated this activity into two fractions, one o f which specifically cleaved 13-hydroperoxylinoleic acid and the other specifi cally cleaved the 9-isomer. 13-H PO -specific activity was most active at pH 8.0 and 9-H PO -specific one was at pH 6.5. SH -reagents inhibited both the lyases but to differ ent extents. | | | |
Reference
| Z. Naturforsch. 44c, 883—885 (1989); received April 251989 | | | |
Published
| 1989 | | | |
Keywords
| Cucumber Cotyledons, Hydroperoxide Lyase, Fatty A cid 13-H ydroperoxide, Fatty Acid 9-H ydroperoxide, Short-Chain A ldehydes | | | |
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| default:Reihe_C/44/ZNC-1989-44c-0883_n.pdf | | | | Identifier
| ZNC-1989-44c-0883_n | | | | Volume
| 44 | |
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