TY - JOUR
T1 - Molecular analysis of a plasmid-encoded phenol hydroxylase from Pseudomonas CF600
AU - Shingler, V.
AU - Franklin, C. H.
AU - Tsuda, M.
AU - Holroyd, D.
AU - Bagdasarian, M.
N1 - Copyright:
Copyright 2020 Elsevier B.V., All rights reserved.
PY - 1989
Y1 - 1989
N2 - Pseudomonas strain CF600 is able to ultilize phenol and 3,4-dimethylphenol as sole carbon and energy source. We demonstrate that growth on these substrates is by virtue of plasmid-encoded phenol hydroxylase and a meta-cleavage pathway. Screening of a genomic bank, with DNA from the previously cloned catechol 2,3-dioxygenase gene of the TOL plasmid pWW0, was used in the identification of a clone which could complement a phenol-hydroxylase-deficient transposon insertion mutant. Deletion mapping and polypeptide production analysis identified a 1.2 kb region of DNA encoding a 39.5 kDa polypeptide which mediated this complementation. Enzyme activities and growth properties of Pseudomonas strains harbouring this fragment on a broad-host-range expression vector indicate that phenol hydroxylase is a multicomponent enzyme containing the 39.5 kDa polypeptide as one component.
AB - Pseudomonas strain CF600 is able to ultilize phenol and 3,4-dimethylphenol as sole carbon and energy source. We demonstrate that growth on these substrates is by virtue of plasmid-encoded phenol hydroxylase and a meta-cleavage pathway. Screening of a genomic bank, with DNA from the previously cloned catechol 2,3-dioxygenase gene of the TOL plasmid pWW0, was used in the identification of a clone which could complement a phenol-hydroxylase-deficient transposon insertion mutant. Deletion mapping and polypeptide production analysis identified a 1.2 kb region of DNA encoding a 39.5 kDa polypeptide which mediated this complementation. Enzyme activities and growth properties of Pseudomonas strains harbouring this fragment on a broad-host-range expression vector indicate that phenol hydroxylase is a multicomponent enzyme containing the 39.5 kDa polypeptide as one component.
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U2 - 10.1099/00221287-135-5-1083
DO - 10.1099/00221287-135-5-1083
M3 - Article
C2 - 2559941
AN - SCOPUS:0024335543
VL - 135
SP - 1083
EP - 1092
JO - Microbiology (Reading, England)
JF - Microbiology (Reading, England)
SN - 1350-0872
IS - 5
ER -