J Bacteriol. 1993 April; 175(7): 2162-2167
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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Copyright © 1993 by the American Society for Microbiology. All rights reserved.