Purification, characterization and gene cloning of isoeugenol-degrading enzyme from Pseudomonas putida IE27.

Abstract:

:An isoeugenol-degrading enzyme was purified to homogeneity from Pseudomonas putida IE27, an isoeugenol-assimilating bacterium. The purified enzyme was a 55 kDa monomer and catalyzed the initial step of isoeugenol degradation, the oxidative cleavage of the side chain double-bond of isoeugenol, to form vanillin. Another reaction product of isoeugenol degradation besides vanillin was identified to be acetaldehyde. The values of Km and k (cat) for isoeugenol were 175 muM and 5.18 s(-1), respectively. The purified enzyme catalyzed the incorporation of an oxygen atom from either molecular oxygen or water into vanillin, suggesting that the isoeugenol-degrading enzyme is a kind of monooxygenase. The gene encoding the isoeugenol-degrading enzyme and its flanking regions were isolated from P. putida IE27. The amino acid sequence of the enzyme was similar to those of lignostilbene-alpha,beta-dioxygenases, carotenoid monooxygenases and 9-cis-epoxycarotenoid dioxygenases.

journal_name

Arch Microbiol

journal_title

Archives of microbiology

authors

Yamada M,Okada Y,Yoshida T,Nagasawa T

doi

10.1007/s00203-007-0218-9

subject

Has Abstract

pub_date

2007-06-01 00:00:00

pages

511-7

issue

6

eissn

0302-8933

issn

1432-072X

journal_volume

187

pub_type

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