Affiliation:
1. Biotechnology Center for Agriculture and the Environment, Cook College, Rutgers University, New Brunswick, New Jersey 08901-8520
Abstract
ABSTRACT
Anthranilate (2-aminobenzoate) is an important intermediate in tryptophan metabolism. In order to investigate the degradation of tryptophan through anthranilate by
Burkholderia cepacia
, several plasposon mutations were constructed of strain DBO1 and one mutant with the plasposon insertion in the anthranilate dioxygenase (AntDO) genes was chosen for further study. The gene sequence obtained from flanking DNA of the plasposon insertion site revealed unexpected information.
B. cepacia
DBO1 AntDO (designated AntDO-3C) is a three-component Rieske-type [2Fe-2S] dioxygenase composed of a reductase (AndAa), a ferredoxin (AndAb), and a two-subunit oxygenase (AndAcAd). This is in contrast to the two-component (an oxygenase and a reductase) AntDO enzyme from
Acinetobacter
sp. strain ADP1,
P. aeruginosa
PAO1, and
P. putida
P111. AntDO from strains ADP1, PAO1, and P111 are closely related to benzoate dioxygenase, while AntDO-3C is closely related to aromatic hydrocarbon dioxygenases from
Novosphingobium aromaticivorans
F199 and
Sphingomonas yanoikuyae
B1 and 2-chlorobenzoate dioxygenase from
P. aeruginosa
strains 142 and JB2.
Escherichia coli
cells expressing the functional AntDO-3C genes transform anthranilate and salicylate (but not 2-chlorobenzoate) to catechol. The enzyme includes a novel reductase whose absence results in less efficient transformation of anthranilate by the oxygenase and ferredoxin. AndR, a possible AraC/XylS-type transcriptional regulator, was shown to positively regulate expression of the
andAcAdAbAa
genes. Anthranilate was the only effector (of 12 aromatic compounds tested) that was able to induce expression of the genes.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
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