Open AccessFunctional and structural relationship of various extradiol aromatic ring‐cleavage dioxygenases of Pseudomonas origin
Author(s) -
Hirose Jun,
Kimura Nobutada,
Suyama Akiko,
Kobayashi Akiko,
Hayashida Shinsaku,
Furukawa Kensuke
Publication year - 1994
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1994.tb06840.x
Subject(s) - dioxygenase , pseudomonas putida , catechol , pseudomonas , biphenyl , stereochemistry , substrate (aquarium) , escherichia coli , bacteria , pseudomonadaceae , pseudomonadales , plasmid , biology , chemistry , biochemistry , dna , enzyme , organic chemistry , gene , genetics , ecology
The extradiol ring‐cleavage dioxygenases derived from seven different Pseudomonas strains were expressed in Escherichia coli and the substrate specificities were investigated for a variety of catecholic compounds. The substrate range of four 2,3‐dihydroxybiphenyl dioxygenases from biphenyl‐utilizing bacteria, 3‐methylcatechol dioxygenase from toluene utilizing Pseudomonas putida F1, 1,2‐dihydroxynaphthalene dioxygenase from a NAH7 plasmid, and catechol 2,3‐dioxygenase from a TOL plasmid pWW0 were compared. Among the dioxygenases, that from Pseudomonas pseudoalcaligenes KF707 showed a very narrow substrate range. Contrary to this, the dioxygenase from pWW0 showed a relaxed substrate range. The seven extradiol dioxygenases from the various Pseudomonas strains are highly diversified in terms of substrate specificity.