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 Microbioljournal_title
Archives of microbiologyauthors
Yamada M,Okada Y,Yoshida T,Nagasawa Tdoi
10.1007/s00203-007-0218-9subject
Has Abstractpub_date
2007-06-01 00:00:00pages
511-7issue
6eissn
0302-8933issn
1432-072Xjournal_volume
187pub_type
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