P. Hein et al., BIPHENYL-ASSOCIATED META-CLEAVAGE DIOXYGENASES FROM COMAMONAS-TESTOSTERONI B-356, Canadian journal of microbiology, 44(1), 1998, pp. 42-49
In addition to 2,3-dihydroxybiphenyl 1,2-dioxygenase (B1,2O), biphenyl
-grown cells of Comamonas testosteroni B-356 were shown to produce a c
atechol 2,3-dioxygenase (C2,3O). B1,2O showed strong sequence homology
with B1,2Os found in other biphenyl catabolic pathways, while partial
sequence analysis of the C2,3O of B-356 suggested a relationship with
xylEII-encoded C2,3O. The coexistence of two meta-cleavage dioxygenas
es in this strain prompted a comparison between the catalytic properti
es of the two enzymes. C2,3O has a much broader substrate specificity
than native or His-tagged B1,2O: both enzymes were inhibited by chloro
catechols, but B1,2O was more sensitive than C2,3O. The results are di
scussed in terms of the physiological implications of interaction betw
een metabolites from the lower biphenyl-chlorobiphenyl pathway and enz
ymes of the upper pathway.