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Induction of 4-hydroxycinnamate decarboxylase in Klebsiella oxytoca cells exposed to substrates and non-substrate 4-hydroxycinnamate analogs.
Title: | Induction of 4-hydroxycinnamate decarboxylase in Klebsiella oxytoca cells exposed to substrates and non-substrate 4-hydroxycinnamate analogs. |
Authors: | Hashidoko, Yasuyuki Browse this author →KAKEN DB | Tanaka, Tomoko Browse this author | Tahara, Satoshi Browse this author |
Keywords: | Klebsiella oxytoca | 4-hydroxycinnamate decarboxylase inducer | 6-hydroxy-2-naphthoic acid | 7-hydroxycoumarin 3-carboxylic acid | substrate analog |
Issue Date: | Dec-2001 |
Publisher: | Japan Society for Bioscience, Biotechnology, and Agrochemistry |
Journal Title: | Bioscience Biotechnology and Biochemistry |
Volume: | 65 |
Issue: | 12 |
Start Page: | 2604 |
End Page: | 2612 |
Publisher DOI: | 10.1271/bbb.65.2604 |
PMID: | 11826954 |
Abstract: | The 4-hydroxycinnamate decarboxylase (4-HCD)-inducing activity of several substrate analogs toward Klebsiella oxytoca was investigated. Four E-cinnamateclass compounds, E-4-hydroxycinnamic acid (1), caffeic acid (2), ferulic acid (3) and E-2,4-dihydroxycinnamic acid (4), all of which were accepted as substrates, all of which were accepted as substrates of 4-HCD, enable K. oxytoca cells to induce the decarboxylase at a 2.0 mM concentration, while five non-substrate compounds of the E-cinnamate class so far tested were completely in-active. However, 6-hydroxy-2-naphthoic acid (11) and 7-hydroxycoumarin 3-carboxylic acid (14), both of which are non-cinnamate-class analogs of the substrate, acted as strong 4-HCD inducers, even at a 0.5 mM concentration. The 4-HCD-inducing activities of compounds 11 and 14 at 0.5 mM were 10-12-fold higher than that of substrate 1. Compound 11 maintained its 4-HCD-inducing activity toward cultured cells through the late-log and stationary phases, unlike 1 that induced 4-HCD only in the early log phase. SDS-PAGE electrophoresis of protein mixtures from the cultured cells exposed to any 4-HCD inducer indicated that the 21.5 kDa protein was always present. |
Relation: | http://www.jstage.jst.go.jp/ |
Type: | article |
URI: | http://hdl.handle.net/2115/15847 |
Appears in Collections: | 農学院・農学研究院 (Graduate School of Agriculture / Faculty of Agriculture) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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Submitter: 橋床 泰之
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