Inactivation of soybean lipoxygenase 1 by 12-iodo-cis-9-octadecenoic acid

Rotenberg, Susan A.; Grandizio, Anna Marie; Selzer, Aaron T.; Clapp, Charles H.

doi:10.1021/bi00424a019

Cited by 10 publications

(20 citation statements)

References 34 publications

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“…Neither 9,ll-ODA (Rotenberg et al, 1988) nor iodide inactivates the enzyme. The inactivation by 12-IODE can be blocked by ascorbate, hydroxylamine or dithiothreitol.…”

Section: Biochemistrymentioning

confidence: 85%

“…Protein concentrations are based on M, 94 000 (Shibata et al, 1987) and = 1.6 (Petersson et al, 1987). Lipoxygenase was assayed as described previously (Rotenberg et al, 1988) on a Beckman DU-40 spectrophotometer interfaced with an IBM PC for data analysis. Linoleic acid was obtained from Sigma and converted enzymatically to Biochemistry, Vol.…”

Section: Methodsmentioning

confidence: 99%

“…Methyl ricinoleate was prepared from castor oil by the method of Swem and Jordan (1952). 12-IODE, truns-12-IODE, and 12-BrODE were synthesized as previously reported (Rotenberg et al, 1988). Glutathione peroxidase (from bovine erythrocytes), glutathione, and dithiothreitol were obtained from Sigma, and L-ascorbic acid was obtained from Aldrich.…”

Section: Methodsmentioning

confidence: 99%

“…Lipoxygenase was assayed as described previously (Rotenberg et al, 1988) on a Beckman DU-40 spectrophotometer interfaced with an IBM PC for data analysis. Linoleic acid was obtained from Sigma and converted enzymatically to 13-HPOD (Gibian & Galaway, 1976).…”

Section: Methodsmentioning

confidence: 99%

“…These studies led to the unexpected discovery that 12-iodocis-9-octadecenoic acid (12-IODE) is a time-dependent, irreversible inactivator of soybean lipoxygenase (Rotenberg et al, 1988). No inactivation was observed with 12-BrODE, 12-iodooctadecanoic acid, or 9,l I-octadecadienoic acid (9,11-ODA), which would be formed by the elimination of HI from 12-IODE.…”

Section: -Iode X=i 12-brode X=brmentioning

confidence: 99%

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Action of Soybean Lipoxygenase 1 on 12-Iodo-cis-9-octadecenoic Acid and 12-Bromo-cis-9-octadecenoic Acid

Clapp¹,

Grandizio²,

McAskill³

et al. 1995

Biochemistry

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The ferric form of soybean lipoxygenase catalyzes an elimination reaction on 12-iodo-cis-9-octadecenoic acid (12-IODE) to produce iodide ions and 9,11-octadecadienoic acid (9, 11-ODA). If excess 13(S)-hydroperoxy-cis-9,trans-11-octadecadienoic acid (13-HPOD) is present, the reaction proceeds until about one-half of the racemic 12-IODE is consumed; in the absence of excess 13-HPOD, the reaction stops after about three turnovers. Ferric lipoxygenase also catalyzes the conversion of 12-bromo-cis-9-octadecenoic acid (12-BrODE) to 9,11-ODA at a rate that is less than 25% of that observed with 12-IODE. These elimination reactions cannot be detected with ferrous lipoxygenase or with lipoxygenase that has been inactivated by 5,8,11,14-eicosatetraynoic acid. In the case of 12-IODE, elimination is accompanied by a loss of enzymatic activity; at pH 9.0, about 10 iodide ions are produced per molecule of enzyme inactivated. No inactivation can be detected with 12-BrODE. Ascorbate and hydroxylamine, which can act as free-radical traps, block the inactivation by 12-IODE but do not inhibit the elimination reaction. When the enzyme is inactivated by [1-14C]-12-IODE at pH 9.0, the amount of radioactivity that is covalently bound to the protein is less than 30% of that expected for 1:1 incorporation.(ABSTRACT TRUNCATED AT 250 WORDS)

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“…Neither 9,ll-ODA (Rotenberg et al, 1988) nor iodide inactivates the enzyme. The inactivation by 12-IODE can be blocked by ascorbate, hydroxylamine or dithiothreitol.…”

Section: Biochemistrymentioning

confidence: 85%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: -Iode X=i 12-brode X=brmentioning

confidence: 99%

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