Open AccessThe specificity of 1‐naphthol oxygenases from three bacterial isolates, Pseudomonas spp. (NCIB 12042 and 12043) and Rhodococcus sp. (NCIB 12038) isolated from garden oil
Author(s) -
Larkin M.J.
Publication year - 1988
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.1574-6968.1988.tb02590.x
Subject(s) - oxygenase , pseudomonas , 1 naphthol , pseudomonadaceae , monooxygenase , naphthalene , dioxygenase , pseudomonadales , rhodococcus , chemistry , bacteria , methylamine , biochemistry , stereochemistry , microbiology and biotechnology , biology , enzyme , organic chemistry , cytochrome p450 , genetics
Three bacterial isolates which appeared to use the insecticide, carbaryl (1‐naphthyl, N ‐methyl‐carbamate) as their sole carbon and nitrogen sources were originally selected from garden soil. Only one isolate, Pseudomonas sp. (NCIB 12043) could metabolise carbaryl rapidly to 1‐naphthol and methylamine. The other two isolates, Pseudomonas sp. (NCIB 12042) and Rhodococcus sp. (NCIB 12038) relied on slow chemical hydrolysis of carbaryl to 1‐naphthol and methylamine. All three isolates used 1‐naphthol as their sole carbon source; however, their ability to use naphthalene and a range of mono‐ and dihydroxy‐substituted naphthalene compounds varied. NCIB 12038 and NCIB 12043 showed little or no growth on naphthalene, 2,3‐dihydroxynaphthalene or 1,3‐dihydroxynaphthalene as sole carbon sources and their 1‐naphthol oxygenases had little activity with these substrates. In contrast, NCIB 12042 could use these compounds as sole carbon sources and its 1‐naphthol oxygenase also showed activity with them. We conclude that 1‐naphthol oxygenase from NCIB 12042 is a relatively non‐specific dioxygenase, whereas the 1‐naphthol oxygenases from NCIB 12038 and NCIB 12043 are relatively specific monooxygenases requiring hydroxylated naphthalene compounds as substrates.