Open AccessComparison of enzymatic and immunochemical properties of 2,3‐dihydroxybiphenyl‐1,2‐dioxygenases from four Pseudomonas strains
Author(s) -
Lee Jeongrai,
Kyung Sung Tae,
Moon Jangho,
Rak Min Kyung,
Kim ChiKyung,
Kim Youngsoo
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.tb07058.x
Subject(s) - pseudomonas putida , dioxygenase , pseudomonas , catechol , biochemistry , pseudomonadales , pseudomonadaceae , biology , enzyme , chemistry , stereochemistry , bacteria , genetics
A 2,3‐dihydroxybiphenyl‐1,2‐dioxygenase gene has been cloned from chromosomal DNA of Pseudomonas sp. DJ‐12 which can grow on biphenyl or 4‐chlorobiphenyl as the sole carbon and energy source. Enzymatic and immunochemical properties of the cloned 2,3‐dihydroxybiphenyl‐1,2‐dioxygenase were characterized, and compared with those of P. pseudoalcaligenes KF707, Pseudomonas sp. KKS102, and P. putida OU83. The dioxygenase of Pseudomonas sp. DJ‐12 was similar to those of P. pseudoalcaligenes KF707, and Pseudomonas sp. KKS102, but significantly different from that of P. putida OU83 in electrophoretic mobilities on native PAGE and SDS‐PAGE. The dioxygenases of Pseudomonas sp. DJ‐12 and P. putida OU83 exhibited the highest ring‐fission activity to 3‐methylcatechol, and those of P. pseudoalcaligenes KF707 and Pseudomonas sp. KKS102 to 2,3‐dihydroxybiphenyl among 2,3‐dihydroxybiphenyl, catechol, 3‐methylcatechol, 4‐methylcatechol, and 4‐chlorocatechol as substrates. 2,3‐dihydroxybiphenyl‐1,2‐dioxygenase of P. pseudoalcaligenes KF707 was immunochemically related to that of Pseudomonas sp. KKS102, but was different from those of Pseudomonas sp. DJ‐12 and P. putida OU83.