Evidence that operons tcb, tfd, and clc encode maleylacetate reductase, the fourth enzyme of the modified ortho pathway

Kasberg, T; Daubaras, Dayna L.; Chakrabarty, Ananda M.; Kinzelt, Dagmar; Reineke, Walter

doi:10.1128/jb.177.13.3885-3889.1995

Cited by 35 publications

(29 citation statements)

References 27 publications

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“…However, a low level of dienelactone (4-carboxymethylenebut-2-ene-4-olide) hydrolase activity and an even lower activity against 2-chloromuconate were observed in strains containing module II genes, whereas a very poor maleylacetate reductase activity was found in strains containing only module I (34). Therefore, despite its high similarity to genes encoding functional maleylacetate reductases (19), tfdF I has been said to encode a poor or nonfunctional enzyme. Moreover, attempts to purify maleylacetate reductase from R. eutropha JMP134 yielded a protein with an N-terminal sequence matching that of TfdF II (45), indicating a critical role of TfdF II for growth of strain JMP134 on 2,4-D.…”

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Importance of DifferenttfdGenes for Degradation of Chloroaromatics byRalstonia eutrophaJMP134

et al. 2002

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The tfdC I D I E I F I, and tfdD II C II E II F II gene modules of plasmid pJP4 of Ralstonia eutropha JMP134 encode complete sets of functional enzymes for the transformation of chlorocatechols into 3-oxoadipate, which are all expressed during growth on 2,4-dichlorophenoxyacetate (2,4-D). However, activity of tfd I -encoded enzymes was usually higher than that of tfd II -encoded enzymes, both in the wild-type strain grown on 2,4-D and in 3-chlorobenzoate-grown derivatives harboring only one tfd gene module. The tfdD II -encoded chloromuconate cycloisomerase exhibited special kinetic properties, with high activity against 3-chloromuconate and poor activity against 2-chloromuconate and unsubstituted muconate, thus explaining the different phenotypic behaviors of R. eutropha strains containing different tfd gene modules. The enzyme catalyzes the formation of an equilibrium between 2-chloromuconate and 5-chloro-and 2-chloromuconolactone and very inefficiently catalyzes dehalogenation to form trans-dienelactone as the major product, thus differing from all (chloro)muconate cycloisomerases described thus far.

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confidence: 90%

Importance of DifferenttfdGenes for Degradation of Chloroaromatics byRalstonia eutrophaJMP134

et al. 2002

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“…Although the maleylacetate reductase gene, tfdF, of Ralstonia eutropha JMP134(pJP4) was initially misinterpreted as encoding a chlorodienelactone isomerase (Don et al, 1985), the chlorocatechol gene clusters of pJP4, pAC27, Pseudomonas sp. B13, and pP51 by DNA sequencing, by correspondence of experimentally determined N-terminal sequences to sequences predicted from DNA and by expression of cloned genes, were shown to contain maleylacetate reductase genes in addition to genes for chlorocatechol 1,2-dioxygenases, chloromuconate cycloisomerases and dienelactone hydrolases (Frantz & Chakrabarty, 1987;Perkins et al, 1990;Laemmli et al, 2000;van der Meer et al, 1991;Schell et al, 1994;Kasberg et al, 1995Kasberg et al, , 1997Seibert et al, 1993;Plumeier et al, 2002). Sequence similarities suggest that this is true also for the chlorocatechol gene clusters of various other plasmids or strains.…”

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confidence: 99%

“…B13, and pP51 by DNA sequencing, by correspondence of experimentally determined N-terminal sequences to sequences predicted from DNA and by expression of cloned genes, were shown to contain maleylacetate reductase genes in addition to genes for chlorocatechol 1,2-dioxygenases, chloromuconate cycloisomerases and dienelactone hydrolases (Frantz & Chakrabarty, 1987;Perkins et al, 1990;Laemmli et al, 2000;van der Meer et al, 1991;Schell et al, 1994;Kasberg et al, 1995Kasberg et al, , 1997Seibert et al, 1993;Plumeier et al, 2002 During growth with 4-fluorobenzoate, R. eutropha 335 T and R. eutropha JMP222, a pJP4-free derivative of the 2,4-dichlorophenoxyacetate-utilizing strain JMP134, induce a maleylacetate reductase, but not the other enzymes typical for chlorocatechol catabolism (Schlömann et al, 1990a). Thus, these strains contain a presumably chromosomal maleylacetate reductase gene of still unknown metabolic affiliation.…”

Section: Introductionmentioning

confidence: 99%

Characterization of a gene cluster encoding the maleylacetate reductase from Ralstonia eutropha 335T, an enzyme recruited for growth with 4-fluorobenzoate

et al. 2004

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A gene cluster containing a gene for maleylacetate reductase (EC 1.3.1.32) was cloned from Ralstonia eutropha 335 T (DSM 531 T ), which is able to utilize 4-fluorobenzoate as sole carbon source. Sequencing of this gene cluster showed that the R. eutropha 335 T maleylacetate reductase gene, macA, is part of a novel gene cluster, which is not related to the known maleylacetate-reductase-encoding gene clusters. It otherwise comprises a gene for a hypothetical membrane transport protein, macB, possibly co-transcribed with macA, and a presumed regulatory gene, macR, which is divergently transcribed from macBA. MacA was found to be most closely related to TftE, the maleylacetate reductase from Burkholderia cepacia AC1100 (62 % identical positions) and to a presumed maleylacetate reductase from a dinitrotoluene catabolic gene cluster from B. cepacia R34 (61 % identical positions). By expressing macA in Escherichia coli, it was confirmed that macA encodes a functional maleylacetate reductase. Purification of maleylacetate reductase from 4-fluorobenzoate-grown R. eutropha 335 T cells allowed determination of the N-terminal sequence of the purified protein, which was shown to be identical to that predicted from the cloned macA gene, thus proving that the gene is, in fact, recruited for growth of R. eutropha 335 T with this substrate. INTRODUCTIONMaleylacetate reductases (EC 1.3.1.32) play a crucial role in the aerobic microbial degradation of aromatic compounds. They catalyse the NADH-or NADPH-dependent reduction of maleylacetate or 2-chloromaleylacetate to 3-oxoadipate ( Fig. 1) or of substituted maleylacetates to substituted 3-oxoadipates. In fungi, maleylacetate reductases contribute to the catabolism of very common substrates, such as tyrosine, gentisate, benzoate, 4-hydroxybenzoate, protocatechuate, vanillate, resorcinol and phenol (Karasevich & Ivoilov, 1977;Buswell & Eriksson, 1979;Gaal & Neujahr, 1979;Sparnins et al., 1979;Anderson & Dagley, 1980;Jones et al., 1995). For bacteria, it has been shown that maleylacetate reductases are involved in the degradation of resorcinol and 2,4-dihydroxybenzoate via hydroxyquinol (Larway & Evans, 1965;Chapman & Ribbons, 1976;Stolz & Knackmuss, 1993). Other substrates whose catabolic routes comprise this activity have a more complex structure, such as 2-hydroxydibenzo-p-dioxin and 3-hydroxydibenzofuran (Armengaud et al., 1999), or carry unusual substituents, such as nitro or sulfo groups (Spain & Gibson, 1991;Feigel & Knackmuss, 1993;Jain et al., 1994;Rani & Lalithakumari, 1994), fluorine or chlorine atoms (Duxbury et al., 1970; Schlömann et al., 1990a;Latus et al., 1995;Zaborina et al., 1995;Daubaras et al., 1996;Miyauchi et al., 1999).The maleylacetate reductase genes characterized so far tend to belong to specialized gene clusters for the degradation of aromatic compounds. Thus, 3-hydroxydibenzofuran and 2-hydroxydibenzo-p-dioxin degradation via hydroxyquinol appears to be encoded by a specialized gene cluster comprising most of the genes for the pathway including a maleylac...

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“…While the genes tcbCDE, tfdCDE, and clcABD have long been known to encode chlorocatechol 1,2-dioxygenase, chloromuconate cycloisomerase, and (chloro)dienelactone hydrolase, respectively, information on the functions of the TcbF, TfdF, and ClcE gene products were obtained more recently. After it had been reported that TcbF and TfdF are homologous to ironcontaining alcohol dehydrogenases (19), our groups provided evidence that these proteins and ClcE encoded by pAC27 are in fact maleylacetate reductases (9,16,18). This paper deals with the isolation of the maleylacetate reductase gene from Pseudomonas sp.…”

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Cloning, characterization, and sequence analysis of the clcE gene encoding the maleylacetate reductase of Pseudomonas sp. strain B13

et al. 1997

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A 3,167-bp PstI fragment of genomic DNA from Pseudomonas sp. strain B13 was cloned and sequenced. The gene clcE consists of 1,059 nucleotides encoding a protein of 352 amino acids with a calculated mass of 37,769 Da which showed maleylacetate reductase activity. The protein had significant sequence similarities with the polypeptides encoded by tcbF of pP51 (59.4% identical positions), tfdF of pJP4 (55.1%), and tftE of Burkholderia cepacia AC1100 (53.1%). The function of TcbF as maleylacetate reductase was established by an enzyme assay.

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Evidence that operons tcb, tfd, and clc encode maleylacetate reductase, the fourth enzyme of the modified ortho pathway

Cited by 35 publications

References 27 publications

Importance of DifferenttfdGenes for Degradation of Chloroaromatics byRalstonia eutrophaJMP134

Importance of DifferenttfdGenes for Degradation of Chloroaromatics byRalstonia eutrophaJMP134

Characterization of a gene cluster encoding the maleylacetate reductase from Ralstonia eutropha 335T, an enzyme recruited for growth with 4-fluorobenzoate

Cloning, characterization, and sequence analysis of the clcE gene encoding the maleylacetate reductase of Pseudomonas sp. strain B13

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