Bacterial metabolism of 5-aminosalicylic acid. Initial ring cleavage.
Bacterial metabolism of 5-aminosalicylic acid. Initial ring cleavage.
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DOI：
10.1042/bj2820675
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发表时间：
1992-03
期刊：
影响因子：
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通讯作者：
A. Stolz;B. Nörtemann;H. Knackmuss
中科院分区：
文献类型：
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作者：
A. Stolz;B. Nörtemann;H. Knackmuss
The metabolism of 5-aminosalicylate (5AS) by a bacterial strain, Pseudomonas sp. BN9, was studied. Intact cells of Pseudomonas sp. BN9 grown with 5AS oxidized 5AS and 2,5-dihydroxybenzoate (gentisate), whereas cells grown with gentisate oxidized only the growth substrate of all substituted salicylates tested. Cell extracts from Pseudomonas sp. BN9 catalysed the stoichiometric reaction of 1 mol of oxygen with 1 mol of 5AS to a metabolite with an intense u.v.-absorption maximum at 352 nm (pH 8.0). This metabolite was accumulated under neutral conditions, but was rapidly destroyed at acid pH. It was identified by m.s. and acid-catalysed deamination to fumarylpyruvate (trans-2,4-dioxohept-5-enedioic acid) as cis-4-amino-6-carboxy-2-oxohexa-3,5-dienoate, thus demonstrating direct cleavage of the monohydroxylated substrate 5AS to a non-aromatic ring-fission product. The enzyme responsible for conversion of 5AS was shown to be Fe(II)-dependent and to be distinct from gentisate 1,2-dioxygenase in strain BN9.
