期刊
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
卷 301, 期 2, 页码 350-357出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/S0006-291X(02)03036-X
关键词
salicylate 1-hydroxylase; phenanthrene; Sphingohium sp.; sphingomonads; polycyclic aromatic hydrocarbon
Five sets of large and small subunits of terminal oxygenase (ahdA1[a-e] and ahdA2[a-e]) and a single gene set encoding ferredoxin (ahdA3) and ferredoxin reductase (ahdA4) were found to be scattered through 15.8- and 14-kb DNA fragments of phenanthrene-degrading Sphingobium sp. strain P2. RT-PCR analysis indicated the inducible and specific expression of ahdA3, ahdA4, and three sets of genes for terminal oxygenase (ahdA1[c-e] and ahdA2[c-e]) in this strain grown on phenanthrene. The biotransformation experiments with resting cells of Escherichia coli JM 109 harboring recombinant ahd genes revealed that AhdA2cA1c, AhdA1dA2d, and AhdA1eA2e can all function as a salicylate 1-hydroxylase which converts salicylate, a metabolic intermediate of phenanthrene, to catechol in cooperation with the electron transport proteins AhdA3A4. The first two oxygenases exhibited a broad range of substrate specificities such that they also catalyzed the hydroxylation of methyl- and chloro-substituted salicylates to produce their corresponding substituted catechols. (C) 2003 Elsevier Science (USA). All rights reserved.
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