Affiliation:
1. Institut für Mikrobiologie, Universität Stuttgart, 70569 Stuttgart,1and
2. Fachgebiet Wasserreinhaltung, Technische Universität Berlin, Sekr. KF4, 10623 Berlin,2 Germany
Abstract
ABSTRACT
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
1
H and
13
C 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.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
66 articles.
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