Purification and properties of a plasmid-encoded 2,4-dichlorophenol hydroxylase.
2,4-Dichlorophenol hydroxylase, an enzyme involved in the bacterial degradation of the herbicide 2,4-dichlorophenoxyacetate (2,4-D) was purified from two bacterial strains that harbored the same 2,4-D plasmid, pJP4. The purified enzymes (Mr 224 000) from the two transconjugants were indistinguishable; they contained FAD and were composed of non-identical subunits, Mr 67 000 and 45 000, respectively. Various substituted phenols were hydroxylated, using either NADH or NADPH. The amino acid composition of the native enzyme was determined.
D000150:Acinetobacter / Q000201:enzymology* / Q000235:genetics; D000596:Amino Acids / Q000032:analysis; D007700:Kinetics; D006899:Mixed Function Oxygenases / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D008970:Molecular Weight; D010957:Plasmids; D011549:Pseudomonas / Q000201:enzymology* / Q000235:genetics; D013379:Substrate Specificity
D000596:Amino Acids; D006899:Mixed Function Oxygenases; C034354:2,4-dichlorophenol hydroxylase