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. 1977 Apr;59(4):667–672. doi: 10.1104/pp.59.4.667

Biochemistry of Suberization

ω-Hydroxyacid Oxidation in Enzyme Preparations from Suberizing Potato Tuber Disks 1

Vishwanath P Agrawal a,2, P E Kolattukudy a,3
PMCID: PMC542470  PMID: 16659915

Abstract

A cell-free extract obtained from suberizing potato (Solanum tuberosum L.) tuber disks catalyzed the conversion of 16-hydroxy[G-3H]hexadecanoic acid to the corresponding dicarboxylic acid with NADP or NAD as the cofactor, with a slight preference for the former. This ω-hydroxyacid dehydrogenase activity, located largely in the 100,000g supernatant fraction, has a pH optimum of 9.5. It showed an apparent Km of 50 μM for 16-hydroxyhexadecanoic acid. The dehydrogenase activity was inhibited by thiol reagents, such as p-chloromercuribenzoate, N-ethylmaleimide, and iodoacetamide, and this dehydrogenase is shown to be different from alcohol dehydrogenase. That 16-oxohexadecanoic acid was an intermediate in the conversion of 16-hydroxyhexadecanoic acid to the corresponding dicarboxylic acid was suggested by the observation that the cell-free extract also catalyzed the conversion of 16-oxohexadecanoic acid to the dicarboxylic acid, with NADP as the preferred cofactor. The time course of development of the ω-hydroxyacid dehydrogenase activity in the suberizing potato disks correlated with the rate of deposition of suberin. Experiments with actinomycin D and cycloheximide suggested that the transcriptional processes, which are directly related to suberin biosynthesis and ω-hydroxyacid dehydrogenase biosynthesis, occurred between 72 and 96 hours after wounding. These results strongly suggest that a wound-induced ω-hydroxyacid dehydrogenase is involved in suberin biosynthesis in potato disks.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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