The 2,4-dichlorophenol hydroxylase of Alcaligenes eutrophus JMP134 is a homotetramer.
2,4-Dichlorophenol hydroxylase (DCP-hydroxylase) is a key enzyme in the pathway for degradation of 2,4-dichlorophenoxyacetic acid (2,4-D) in many bacteria. In Alcaligenes eutrophus JMP134, DCP-hydroxylase was reported to consist of two dissimilar types of subunit of 66 and 45 kDa, a structure which is different from that in other bacteria. Using a different procedure involving affinity purification and ion-exchange chromatography, we have purified active enzyme from JMP134 and show that it has a native molecular mass of approximately 245 kDa and consists of a single type of subunit of 66 kDa, similar to all other flavoprotein monooxygenase enzymes. A 45-kDa polypeptide, found in partially purified enzyme preparations, was not required for enzyme activity but had some serologic and N-terminal amino acid sequence similarity to the 66-kDa enzyme subunit.
Farhana
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Department of Microbiology, University of Sydney, N.S.W., Australia.
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D000421:Alcaligenes / Q000201:enzymology*; D001426:Bacterial Proteins / Q000276:immunology; D015153:Blotting, Western; D002846:Chromatography, Affinity; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D006899:Mixed Function Oxygenases / Q000737:chemistry* / Q000276:immunology / Q000302:isolation & purification*; D008970:Molecular Weight; D011487:Protein Conformation
D001426:Bacterial Proteins; D006899:Mixed Function Oxygenases; C034354:2,4-dichlorophenol hydroxylase