Abstract
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.
MeSH Terms
Amino Acid Sequence
Base Sequence
Catechol 1,2-Dioxygenase
Catechols/metabolism
Chemical Phenomena
Chemistry
Dioxygenases
Gene Expression Regulation
Genes, Bacterial
Intramolecular Lyases
Isomerases/genetics,metabolism
Oxygenases/genetics,metabolism
Pseudomonas/enzymology,genetics,metabolism
Substrate Specificity
Chemicals
Catechols
Oxygenases
Dioxygenases
Catechol 1,2-Dioxygenase
Isomerases
Intramolecular Lyases
chloromuconate cycloisomerase
4-chlorocatechol
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Ngai K L
Department of Biology, Yale University, New Haven, Connecticut 06511.
Ornston L N
References (12)
12 references, click to expand
-
Genes specifying degradation of 3-chlorobenzoic acid in plasmids pAC27 and pJP4.
Proc Natl Acad Sci U S A. 1985 Mar;82(6):1638-42
PMID: 3856842
-
Dienelactone hydrolase from Pseudomonas sp. strain B13.
J Bacteriol. 1987 Feb;169(2):699-703
PMID: 3804973
-
Nucleotide sequence and expression of clcD, a plasmid-borne dienelactone hydrolase gene from Pseudomonas sp. strain B13.
J Bacteriol. 1987 Feb;169(2):704-9
PMID: 3804974
-
Organization and nucleotide sequence determination of a gene cluster involved in 3-chlorocatechol degradation.
Proc Natl Acad Sci U S A. 1987 Jul;84(13):4460-4
PMID: 3299368
-
Cloning and complete nucleotide sequence determination of the catB gene encoding cis,cis-muconate lactonizing enzyme.
Gene. 1987;52(2-3):185-95
PMID: 3609743
-
Chemical structure and biodegradability of halogenated aromatic compounds. Conversion of chlorinated muconic acids into maleoylacetic acid.
Biochem J. 1980 Oct 15;192(1):339-47
PMID: 7305906
-
The conversion of catechol and protocatechuate to beta-ketoadipate by Pseudomonas putida. 3. Enzymes of the catechol pathway.
J Biol Chem. 1966 Aug 25;241(16):3795-9
PMID: 5330966
-
Relationships among enzymes of the beta-ketoadipate pathway. I. Properties of cis,cis-muconate-lactonizing enzyme and muconolactone isomerase from Pseudomonas putida.
Biochemistry. 1973 Aug 28;12(18):3523-30
PMID: 4199894
-
A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding.
Anal Biochem. 1976 May 7;72:248-54
PMID: 942051
-
Refinement of the coomassie blue method of protein quantitation. A simple and linear spectrophotometric assay for less than or equal to 0.5 to 50 microgram of protein.
Anal Biochem. 1978 May;86(1):142-6
PMID: 655375
-
Chemical structure and biodegradability of halogenated aromatic compounds. Two catechol 1,2-dioxygenases from a 3-chlorobenzoate-grown pseudomonad.
Biochem J. 1978 Jul 15;174(1):73-84
PMID: 697765
-
Studies on oxygenases; pyrocatechase.
J Biol Chem. 1957 Dec;229(2):905-20
PMID: 13502352