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Volume 272, Number 23, Issue of June 6, 1997 pp. 14727-14732
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Novel Genes Encoding 2-Aminophenol 1,6-Dioxygenase from Pseudomonas Species AP-3 Growing on 2-Aminophenol and Catalytic Properties of the Purified Enzyme

(Received for publication, February 26, 1997, and in revised form, April 4, 1997)

Shinji Takenaka , Shuichiro Murakami , Ryu Shinke , Kazuhisa Hatakeyama ^§ , Hideaki Yukawa ^§ and Kenji Aoki

From the Division of Science of Biological Resources, Graduate School of Science and Technology and the  Department of Biofunctional Chemistry, Faculty of Agriculture, Kobe University, Rokko, Kobe 657 and ^§ Tsukuba Research Center, Mitsubishi Chemical, Ibaraki 300-03, Japan

2-Aminophenol 1,6-dioxygenase was purified from the cell extracts of Pseudomonas sp. AP-3 grown on 2-aminophenol. The product from 2-aminophenol by catalysis of the purified enzyme was identified as 2-aminomuconic 6-semialdehyde by gas chromatographic and mass spectrometric analyses. The molecular mass of the native enzyme was 140 kDa based on gel filtration. It was dissociated into molecular mass subunits of 32 (-subunit) and 40 kDa (-subunit) by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, indicating that the dioxygenase was a heterotetramer of ₂₂. The genes coding for the - and -subunits of the enzyme were cloned and sequenced. Open reading frames of the genes (amnA and amnB) were 816 and 918 base pairs in length, respectively. The amino acid sequences predicted from the open reading frames of amnA and amnB corresponded to the NH₂-terminal amino acid sequences of the -subunit (AmnA) and -subunit (AmnB), respectively. The deduced amino acid sequences of AmnB showed identities to some extent with HpaD (25.4%) and HpcB (24.4%) that are homoprotocatechuate 2,3-dioxygenases from Escherichia coli W and C, respectively, belonging to class III in the extradiol dioxygenases. On the other hand, AmnA had identity (23.3%) with only AmnB among the enzymes examined.

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