Abundant expression of Pseudomonas genes for chlorocatechol metabolism.
The respective specific activities of catechol 1,2-oxygenase II (catechol 1,2-dioxygenase; EC 1.13.11.1) and muconate cycloisomerase II (chloromuconate cycloisomerase; EC 5.5.1.7) in crude extracts of chlorobenzoate-grown Pseudomonas cells corresponded to about 16 and 11% of the soluble cell protein. High levels of protein synthesis appeared to compensate for a loss in catalytic activity that accompanied evolutionary acquisition of broad substrate specificity required for the enzymes to accommodate halogenated substrates.
Ngai
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KL
Department of Biology, Yale University, New Haven, Connecticut 06511.
Ornston
L N
LN
D000595:Amino Acid Sequence; D001483:Base Sequence; D050548:Catechol 1,2-Dioxygenase; D002396:Catechols / Q000378:metabolism*; D055598:Chemical Phenomena; D002621:Chemistry; D049308:Dioxygenases; D005786:Gene Expression Regulation; D005798:Genes, Bacterial; D019753:Intramolecular Lyases; D007535:Isomerases / Q000235:genetics / Q000378:metabolism; D010105:Oxygenases / Q000235:genetics / Q000378:metabolism; D011549:Pseudomonas / Q000201:enzymology / Q000235:genetics* / Q000378:metabolism; D013379:Substrate Specificity
D002396:Catechols; D010105:Oxygenases; D049308:Dioxygenases; D050548:Catechol 1,2-Dioxygenase; D007535:Isomerases; D019753:Intramolecular Lyases; C055773:chloromuconate cycloisomerase; C038861:4-chlorocatechol