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Journal of Bacteriology, December 2001, p. 6936-6942, Vol. 183, No. 23
Institut für Mikrobiologie,
Universität Stuttgart, 70569 Stuttgart,1
and Fachgebiet Wasserreinhaltung, Technische
Universität Berlin, Sekr. KF4, 10623 Berlin,2 Germany
Received 8 June 2001/Accepted 10 September 2001
In cell extracts of Pseudaminobacter
salicylatoxidans strain BN12, an enzymatic activity was
detected which converted salicylate in an oxygen-dependent but
NAD(P)H-independent reaction to a product with an absorbance maximum at
283 nm. This metabolite was isolated, purified, and identified by mass
spectrometry and 1H and 13C nuclear magnetic
resonance spectroscopy as 2-oxohepta-3,5-dienedioic acid. This
metabolite could be formed only by direct ring fission of salicylate by
a 1,2-dioxygenase reaction. Cell extracts from P.
salicylatoxidans also oxidized 5-aminosalicylate, 3-, 4-, and 5-chlorosalicylate, 3-, 4-, and 5-methylsalicylate, 3- and
5-hydroxysalicylate (gentisate), and 1-hydroxy-2-naphthoate. The
dioxygenase was purified and shown to consist of four identical
subunits with a molecular weight of about 45,000. The purified enzyme
showed higher catalytic constants with gentisate or
1-hydroxy-2-naphthoate than with salicylate. It was therefore concluded
that P. salicylatoxidans synthesized a gentisate
1,2-dioxygenase with an extraordinary substrate range, which also
allowed the oxidation of salicylate.
0021-9193/01/$04.00+0 DOI: 10.1128/JB.183.23.6936-6942.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
Direct Ring Fission of Salicylate by a Salicylate
1,2-Dioxygenase Activity from Pseudaminobacter
salicylatoxidans
*
Corresponding author. Mailing address: Institut
für Mikrobiologie, Universität Stuttgart, Allmandring 31, 70569 Stuttgart, Germany. Phone: 49-711-6855489. Fax: 49-711-6855725. E-mail: Andreas.Stolz{at}PO.Uni-Stuttgart.de.
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