L. Farhana et Pb. New, THE 2,4-DICHLOROPHENOL HYDROXYLASE OF ALCALIGENES-EUTROPHUS JMP134 ISA HOMOTETRAMER, Canadian journal of microbiology, 43(2), 1997, pp. 202-205
2,4-Dichlorophenol hydroxylase (DCP-hydroxylase) is a key enzyme in th
e pathway for degradation of 2,4-dichlorophenoxyacetic acid (2,4-D) in
many bacteria. In Alcaligenes eutrophus JMP134, DCP-hydroxylase was r
eported 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 c
hromatography, we have purified active enzyme from JMP134 and show tha
t 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 flavoprot
ein monooxygenase enzymes. A 45-kDa polypeptide, found in partially pu
rified enzyme preparations, was not required for enzyme activity but h
ad some serologic and N-terminal amino acid sequence similarity to the
66-kDa enzyme subunit.