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J Bacteriol. 1993 April; 175(7): 2162-2167

research-article

Characterization of an Escherichia coli aromatic hydroxylase with a broad substrate range.

M A Prieto, A Perez-Aranda and J L Garcia

Unidad de Genética Bacteriana, Centro de Investigaciones Biológicas, Consejo Superior de Investigaciones Cientificas, Velázquez, Madrid.

ABSTRACT

The hpaB gene encoding an aromatic hydroxylase of Escherichia coli ATCC 11105, a penicillin G acylase-producing strain, has been cloned and expressed in E. coli K-12. This gene was located near the pacA gene coding for penicillin G acylase. The hydroxylase has a molecular mass of 59,000 Da, uses NADH as a cosubstrate, and was tentatively classified as a 4-hydroxyphenylacetic acid hydroxylase, albeit it exhibited a rather broad substrate specificity acting on different monohydric and dihydric phenols. E. coli W, C, and B as well as Klebsiella pneumoniae M5a1 and Kluyvera citrophila ATCC 21285 (a penicillin G acylase-producing strain) but not E. coli K-12 contained sequences homologous to hpaB. Our results support the hypothesis that hpaB is a component of the 4-hydroxyphenylacetic acid degradative pathway of E. coli W.


J Bacteriol. 1993 April; 175(7): 2162-2167




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