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Induction of 4-hydroxycinnamate decarboxylase in Klebsiella oxytoca cells exposed to substrates and non-substrate 4-hydroxycinnamate analogs.

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Please use this identifier to cite or link to this item:http://hdl.handle.net/2115/15847

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)

Submitter: 橋床 泰之

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