Crystal structure of chloromuconate cycloisomerase from<i>Alcaligenes eutrophus</i>JMP134 (pJP4) at 3 Å resolution

Hoier, Helga; Schlömann, Michael; Hammer, Angela; Glusker, J.P.; Carrell, H. L.; Goldman, Alan S.; Stezowski, John J.; Heinemann, Udo

doi:10.1107/s090744499300900x

Cited by 27 publications

(27 citation statements)

References 18 publications

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“…We expect that the available sequence information (1,15,17,38,51,58) and especially the known structures of P. putida muconate cycloisomerase (18) and pJP4-encoded chloromuconate cycloisomerase (20,22) will allow us in the near future to better understand the mechanism of dehalogenation and its evolution at the molecular level. …”

Section: Discussionmentioning

confidence: 99%

Inability of muconate cycloisomerases to cause dehalogenation during conversion of 2-chloro-cis,cis-muconate

et al. 1994

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The conversion of 2-chloro-cis,cis-muconate by muconate cycloisomerase from Pseudomonas putida PRS2000 yielded two products which by nuclear magnetic resonance spectroscopy were identified as 2-chloro-and 5-chloromuconolactone. High-pressure liquid chromatography analyses showed the same compounds to be formed also by muconate cycloisomerases from Acinetobacter calcoaceticus ADP1 and Pseudomonas sp. strain B13. During 2-chloro-cis,cis-muconate turnover by the enzyme from P. putida, 2-chloromuconolactone initially was the major product. After prolonged incubation, however, 5-chloromuconolactone dominated in the resulting equilibrium. In contrast to previous assumptions, both chloromuconolactones were found to be stable at physiological pH. Since the chloromuconate cycloisomerases of Pseudomonas sp. strain B13 and Akaligenes eutrophus JMP134 have been shown previously to produce the trans-dienelactone (trans4-carboxymethylenebut-2-en-4-olide) from 2-chloro-cis,cis-muconate, they must have evolved the capability to cleave the carbonchlorine bond during their divergence from normal muconate cycloisomerases.The bacterial mineralization of chloroaromatic compounds necessarily involves the cleavage of carbon-chlorine bonds, liberating inorganic chloride. In several cases, this is achieved prior to the opening of the aromatic ring by reductive, oxygenolytic, or hydrolytic reactions (for reviews, see references 12, 19, and 45). In many other cases, however, chloride elimination occurs only after ring cleavage has been accomplished. Corresponding catabolic pathways have been described mainly for mono-and dichlorosubstituted phenoxyacetates, phenols, benzoates, benzenes, anilines, salicylates, and metabolic precursors of them. Under aerobic conditions, all of these compounds are usually first converted to chlorocatechols as central intermediates. These are then subject to intradiol (ortho) ring cleavage, giving rise to chlorosubstituted cis,cismuconates. It has long been known (3,13,14,57) that chloride elimination on this pathway is related to the conversion of mono-and dichloromuconates to unsubstituted or chlorosubstituted dienelactones (4-carboxymethylenebut-2-en-4-olides) (Fig. 1). The dienelactones are then cleaved hydrolytically, and the products are finally funneled into the 3-oxoadipate pathway (10,13,14,24,48,52,57,60).Bacteria, employing the modified ortho cleavage pathway outlined above, usually do so by inducing a set of plasmidencoded enzymes which are specially adapted for the turnover of chlorocatechols or their respective metabolites (9,41,48). With the exception of maleylacetate reductase, these enzymes catalyze reactions analogous to those of the ordinary 3-oxoadipate pathway.Muconate cycloisomerase (EC 5.5.1.1) and chloromuconate cycloisomerase (EC 5.5.1.7) were first differentiated by Schmidt and Knackmuss (48) in the 3-chlorobenzoate-utilizing strain Pseudomonas sp. strain B13. The authors reported that both enzymes catalyze basically the same reactions and that they differ only with respect to their...

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Section: Discussionmentioning

confidence: 99%

Inability of muconate cycloisomerases to cause dehalogenation during conversion of 2-chloro-cis,cis-muconate

et al. 1994

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“…Numbers above the sequences refer to positions in the alignment, not in single sequences. Amino acids in those positions in which at least six of the seven sequences are identical (highlighted), aspartate and glutamate residues involved in manganese coordination (arrows pointing upward), as well as lysine and glutamate residues directly involved in the enzyme mechanism (arrows pointing downward) (17,22,24) are indicated. Accession numbers and references for the published sequences (order as in the alignment) are as follows: U12557 (26), M19460 (1), M76991 (55), M35097 (48), M16964 (15), and M57629 (62).…”

Section: Discussionmentioning

confidence: 99%

Characterization of catechol catabolic genes from Rhodococcus erythropolis 1CP

1997

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The biochemical characterization of the muconate and the chloromuconate cycloisomerases of the chlorophenol-utilizing Rhodococcus erythropolis strain 1CP previously indicated that efficient chloromuconate conversion among the gram-positive bacteria might have evolved independently of that among gram-negative bacteria. Based on sequences of the N terminus and of tryptic peptides of the muconate cycloisomerase, a fragment of the corresponding gene has now been amplified and used as a probe for the cloning of catechol catabolic genes from R. erythropolis. The clone thus obtained expressed catechol 1,2-dioxygenase, muconate cycloisomerase, and muconolactone isomerase activities. Sequencing of the insert on the recombinant plasmid pRER1 revealed that the genes are transcribed in the order catA catB catC. Open reading frames downstream of catC may have a function in carbohydrate metabolism. The predicted protein sequence of the catechol 1,2-dioxygenase was identical to the one from Arthrobacter sp. strain mA3 in 59% of the positions. The chlorocatechol 1,2-dioxygenases and the chloromuconate cycloisomerases of gram-negative bacteria appear to be more closely related to the catechol 1,2-dioxygenases and muconate cycloisomerases of the gram-positive strains than to the corresponding enzymes of gram-negative bacteria.

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“…The molecular mass of the native MCI was estimated by gel filtration to be 255 Ϯ 20 kDa, and a single band at 40 Ϯ 2 kDa was observed by SDS-PAGE. Thus, it can be assumed that this enzyme, like MCI of Pseudomonas putida PRS2000 (16) or chloromuconate cycloisomerase of Ralstonia eutropha JMP 134 (18), is a homooctamer.…”

Section: Growth Ofmentioning

confidence: 99%

New Bacterial Pathway for 4- and 5-Chlorosalicylate Degradation via 4-Chlorocatechol and Maleylacetate in Pseudomonas sp. Strain MT1

Nikodem¹,

Hecht

Schlömann

et al. 2003

J Bacteriol

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Pseudomonas sp. strain MT1 is capable of degrading 4-and 5-chlorosalicylates via 4-chlorocatechol, 3-chloromuconate, and maleylacetate by a novel pathway. 3-Chloromuconate is transformed by muconate cycloisomerase of MT1 into protoanemonin, a dominant reaction product, as previously shown for other muconate cycloisomerases. However, kinetic data indicate that the muconate cycloisomerase of MT1 is specialized for 3-chloromuconate conversion and is not able to form cis-dienelactone. Protoanemonin is obviously a dead-end product of the pathway. A trans-dienelactone hydrolase (trans-DLH) was induced during growth on chlorosalicylates. Even though the purified enzyme did not act on either 3-chloromuconate or protoanemonin, the presence of muconate cylcoisomerase and trans-DLH together resulted in considerably lower protoanemonin concentrations but larger amounts of maleylacetate formed from 3-chloromuconate than the presence of muconate cycloisomerase alone resulted in. As trans-DLH also acts on 4-fluoromuconolactone, forming maleylacetate, we suggest that this enzyme acts on 4-chloromuconolactone as an intermediate in the muconate cycloisomerase-catalyzed transformation of 3-chloromuconate, thus preventing protoanemonin formation and favoring maleylacetate formation. The maleylacetate formed in this way is reduced by maleylacetate reductase. Chlorosalicylate degradation in MT1 thus occurs by a new pathway consisting of a patchwork of reactions catalyzed by enzymes from the 3-oxoadipate pathway (catechol 1,2-dioxygenase, muconate cycloisomerase) and the chlorocatechol pathway (maleylacetate reductase) and a trans-DLH.

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Crystal structure of chloromuconate cycloisomerase fromAlcaligenes eutrophusJMP134 (pJP4) at 3 Å resolution

Cited by 27 publications

References 18 publications

Inability of muconate cycloisomerases to cause dehalogenation during conversion of 2-chloro-cis,cis-muconate

Inability of muconate cycloisomerases to cause dehalogenation during conversion of 2-chloro-cis,cis-muconate

Characterization of catechol catabolic genes from Rhodococcus erythropolis 1CP

New Bacterial Pathway for 4- and 5-Chlorosalicylate Degradation via 4-Chlorocatechol and Maleylacetate in Pseudomonas sp. Strain MT1

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