Contrasting patterns of evolutionary divergence within the Acinetobacter calcoaceticus pca operon

Kowalchuk, George A.; Hartnett, Gail B.; Benson, Amanda; Houghton, John E.; Ngai, Ka-Leung; Ornston, L N

doi:10.1016/0378-1119(94)90829-x

Cited by 62 publications

(65 citation statements)

References 39 publications

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“…strain CF600 (64); Hpa and Hpc are from the 4-hydroxyphenylacetate and homoprotocatechuate pathways of E. coli W (57) and C (58, 59), respectively; Nah proteins are from the naphthalene pathway of Pseudomonas sp. strain NCIMB9816 (54); Tod proteins are from the toluene pathway of P. putida F1 (74); Xyl proteins are from the toluene-xylene pathway of P. putida mt-2 (29); PcaRK (30) and PcaT (U48776) are from the protocatechuate pathway of P. putida PRS2000; PcaU (U04359) and PcaK_Ac (37) sequence 112-GNSMGG-117 around the potential active-site serine of MphC fits very well in the nucleophilic motif present in all members of the ␣/␤ hydrolase fold family (20). Moreover, the conserved dipeptide 42-HG-43 at the NH 2 terminus of the MhpC molecule can be tentatively assigned as the central dipeptide that characterizes the oxyanion hole in ␣/␤ fold hydrolases (20).…”

Section: Resultsmentioning

confidence: 99%

Genetic characterization and expression in heterologous hosts of the 3-(3-hydroxyphenyl)propionate catabolic pathway of Escherichia coli K-12

1997

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We report the complete nucleotide sequence of the gene cluster encoding the 3-(3-hydroxyphenyl)propionate (3-HPP) catabolic pathway of Escherichia coli K-12. Sequence analysis revealed the existence of eight genes that map at min 8 of the chromosome, between the lac and hemB regions. Six enzyme-encoding genes account for a flavin-type monooxygenase (mhpA), the extradiol dioxygenase (mhpB), and the meta-cleavage pathway (mhpCDFE). The order of these catabolic genes, with the sole exception of mhpF, parallels that of the enzymatic steps of the pathway. The mhpF gene may encode the terminal acetaldehyde dehydrogenase (acylating) not reported previously in the proposed pathway. Enzymes that catalyze the early reactions of the pathway, MhpA and MhpB, showed the lowest level of sequence similarity to analogous enzymes of other aromatic catabolic pathways. However, the genes mhpCDFE present the same organization and appear to be homologous to the Pseudomonas xyl, dmp, and nah meta-pathway genes, supporting the hypothesis of the modular evolution of catabolic pathways and becoming the first example of this type of catabolic module outside the genus Pseudomonas. Two bacterial interspersed mosaic elements were found downstream of the mhpABCDFE locus and flank a gene, orfT, which encodes a protein related to the superfamily of transmembrane facilitators that might be associated with transport. All of the genes of the 3-HPP cluster are transcribed in the same direction, with the sole exception of mhpR. Inducible expression of the mhp catabolic genes depends upon the presence, in the cis or trans position, of a functional mhpR gene, which suggests that the mhpR gene product is the activator of the 3-HPP biodegradative pathway. The primary structure of MhpR revealed significant similarities to that of members of the IclR subfamily of transcriptional regulators. A 3-HPP catabolic DNA cassette was engineered and shown to be functional not only in enteric bacteria (E. coli and Salmonella typhimurium) but also in Pseudomonas putida and Rhizobium meliloti, thus facilitating its potential application to improve the catabolic abilities of bacterial strains for degradation of aromatic compounds.

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Section: Resultsmentioning

confidence: 99%

Genetic characterization and expression in heterologous hosts of the 3-(3-hydroxyphenyl)propionate catabolic pathway of Escherichia coli K-12

1997

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“…Analysis of the paa cluster involved in PA degradation in E. coli (Ferrández et al, 1998) revealed the existence of the paaE gene (formerly named paaJ), whose product showed a significant amino acid sequence identity with the b-ketoadipyl-CoA thiolase (PcaF) that acts in the b-ketoadipate pathway of P. putida (71 %) (Harwood et al, 1994) and Acinetobacter sp. ADP1 (66.5 %) (Kowalchuk et al, 1994). Homologous paaE genes are also present in the paa clusters of P. putida strains Jiménez et al, 2002;Bartolomé-Martín et al, 2004).…”

Section: Pa Consumption By Wild-type and Sucd Mutant Strainsmentioning

confidence: 98%

Characterization of the last step of the aerobic phenylacetic acid degradation pathway

et al. 2007

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“…These reactions were analysed by HPLC because 3-sulfomuconate, unlike most other substituted muconates, does not have pronounced The accession numbers and references for the published sequences of the enzymes from P. putida, Acinetobacter sp. ADP1 and Agrobacterium tumefaciens C58 are P32427 (Williams et al, 1992), Q59092 (Kowalchuk et al, 1994), and AAK88905 (Wood et al, 2001), respectively. absorbance at 260 nm (Feigel & Knackmuss, 1993).…”

Section: Turnover Of 3-sulfomuconate By Hicmle2 and Arcmle2mentioning

confidence: 99%

Characterization of the genes encoding the 3-carboxy-cis,cis-muconate-lactonizing enzymes from the 4-sulfocatechol degradative pathways of Hydrogenophaga intermedia S1 and Agrobacterium radiobacter S2

et al. 2006

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Hydrogenophaga intermedia strain S1 and Agrobacterium radiobacter strain S2 form a mixed bacterial culture which degrades sulfanilate (4-aminobenzenesulfonate) by a novel variation of the b-ketoadipate pathway via 4-sulfocatechol and 3-sulfomuconate. It was previously proposed that the further metabolism of 3-sulfomuconate is catalysed by modified 3-carboxy-cis, cis-muconate-lactonizing enzymes (CMLEs) and that these 'type 2' enzymes were different from the conventional CMLEs ('type 1') from the protocatechuate pathway in their ability to convert 3-sulfomuconate in addition to 3-carboxy-cis,cis-muconate. In the present study the genes for two CMLEs (pcaB2S1 and pcaB2S2) were cloned from H. intermedia S1 and A. radiobacter S2, respectively. In both strains, these genes were located close to the previously identified genes encoding the 4-sulfocatechol-converting enzymes. The gene products of pcaB2S1 and pcaB2S2 were therefore tentatively identified as type 2 enzymes involved in the metabolism of 3-sulfomuconate. The genes were functionally expressed and the gene products were shown to convert 3-carboxy-cis,cis-muconate and 3-sulfomuconate. 4-Carboxymethylene-4-sulfo-but-2-en-olide (4-sulfomuconolactone) was identified by HPLC-MS as the product, which was enzymically formed from 3-sulfomuconate. His-tagged variants of both CMLEs were purified and compared with the CMLE from the protocatechuate pathway of Pseudomonas putida PRS2000 for the conversion of 3-carboxy-cis,cis-muconate and 3-sulfomuconate. The CMLEs from the 4-sulfocatechol pathway converted 3-sulfomuconate with considerably higher activities than 3-carboxy-cis,cis-muconate. Also the CMLE from P. putida converted 3-sulfomuconate, but this enzyme demonstrated a clear preference for 3-carboxy-cis,cis-muconate as substrate. Thus it was demonstrated that in the 4-sulfocatechol pathway, distinct CMLEs are formed, which are specifically adapted for the preferred conversion of sulfonated substrates.

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Contrasting patterns of evolutionary divergence within the Acinetobacter calcoaceticus pca operon

Cited by 62 publications

References 39 publications

Genetic characterization and expression in heterologous hosts of the 3-(3-hydroxyphenyl)propionate catabolic pathway of Escherichia coli K-12

Genetic characterization and expression in heterologous hosts of the 3-(3-hydroxyphenyl)propionate catabolic pathway of Escherichia coli K-12

Characterization of the last step of the aerobic phenylacetic acid degradation pathway

Characterization of the genes encoding the 3-carboxy-cis,cis-muconate-lactonizing enzymes from the 4-sulfocatechol degradative pathways of Hydrogenophaga intermedia S1 and Agrobacterium radiobacter S2

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