The pathway for degradation of the xenobiotic pesticide pentachlorophenol i
n Sphingomonas chlorophenolica probably evolved in the past few decades by
the recruitment of enzymes from two other catabolic pathways. The first and
third enzymes in the pathway, pentachlorophenol hydroxylase and 2,6-dichlo
rohydroquinone dioxygenase, may have originated from enzymes in a pathway f
or degradation of a naturally occurring chlorinated phenol. The second enzy
me, a reductive dehalogenase, may have evolved from a maleylacetoacetate is
omerase normally involved in degradation of tyrosine. This apparently recen
tly assembled pathway does not function very well: pentachlorophenol hydrox
ylase is quite slow, and tetrachlorohydroquinone dehalogenase is subject to
severe substrate inhibition.