Molecular characterization of the phenylacetic acid catabolic pathway in
            <i>Pseudomonas putida</i>
            U: The phenylacetyl-CoA catabolon

Olivera, Elı́as R.; Miñambres, Baltasar; García, Borja Sánchez; Muñiz, Carmen; Moreno, M.; Ferrández, Abel; Dı́az, Eduardo; Garcı́a, José Luis; Luengo, José M.

doi:10.1073/pnas.95.11.6419

Cited by 201 publications

(228 citation statements)

References 30 publications

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“…The deduced amino acid sequence (293 aa) of the incomplete mhpP showed significant sequence similarities to porins of the Opr family, specifically to PaaM, which has been suggested to be involved in the uptake of phenylacetate by P. putida U (45 % amino acid identity) (Olivera et al, 1998). Similar proteins are usually not encoded in 2,3-dihydroxyphenylpropionate catabolic gene clusters.…”

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confidence: 95%

Degradation of chloroaromatics by Pseudomonas putida GJ31: assembled route for chlorobenzene degradation encoded by clusters on plasmid pKW1 and the chromosome

et al. 2009

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Pseudomonas putida GJ31 has been reported to grow on chlorobenzene using a meta-cleavage pathway with chlorocatechol 2,3-dioxygenase (CbzE) as a key enzyme. The CbzE-encoding gene was found to be localized on the 180 kb plasmid pKW1 in a cbzTEXGS cluster, which is flanked by transposases and encodes only a partial (chloro)catechol meta-cleavage pathway comprising ferredoxin reductase, chlorocatechol 2,3-dioxygenase, an unknown protein, 2-hydroxymuconic semialdehyde dehydrogenase and glutathione S-transferase. Downstream of cbzTEXGS are located cbzJ, encoding a novel type of 2-hydroxypent-2,4-dienoate hydratase, and a transposon region highly similar to Tn5501. Upstream of cbzTEXGS, traNEOFG transfer genes were found. The search for gene clusters possibly completing the (chloro)catechol metabolic pathway of GJ31 revealed the presence of two additional catabolic gene clusters on pKW1. The mhpRBCDFETP cluster encodes enzymes for the dissimilation of 2,3-dihydroxyphenylpropionate in a novel arrangement characterized by the absence of a gene encoding 3-(3-hydroxyphenyl)propionate monooxygenase and the presence of a GntR-type regulator, whereas the nahINLOMKJ cluster encodes part of the naphthalene metabolic pathway. Transcription studies supported their possible involvement in chlorobenzene degradation. The upper pathway cluster, comprising genes encoding a chlorobenzene dioxygenase and a chlorobenzene dihydrodiol dehydrogenase, was localized on the chromosome. A high level of transcription in response to chlorobenzene revealed it to be crucial for chlorobenzene degradation. The chlorobenzene degradation pathway in strain GJ31 is thus a mosaic encoded by four gene clusters.

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confidence: 95%

Degradation of chloroaromatics by Pseudomonas putida GJ31: assembled route for chlorobenzene degradation encoded by clusters on plasmid pKW1 and the chromosome

et al. 2009

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“…In addition, the region 79 -155 at the N terminus matches to the DUF59 domain. This domain is present in proteins of prokaryotic ring-hydroxylating multiprotein complexes (56).…”

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confidence: 99%

A Novel Protein for Photosystem I Biogenesis

Stöckel

Oelmüller

2004

Journal of Biological Chemistry

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Hcf101-1 is a high-chlorophyll-fluorescence (hcf) Arabidopsis mutant that lacks photosystem I (1). Photosystem I subunits are synthesized in the mutant but do not assemble into a stable complex. hcf101 was isolated by map-based cloning and encodes an MRP-like protein with a nucleotide-binding domain. The protein is localized in the chloroplast stroma. In green tissue, the Hcf101 level is stimulated by light, and the protein is not detectable in roots. Two independent knock-out lines, hcf101-2 and hcf101-3, are also impaired in Hcf101 accumulation, although to different extents. Like hcf101-1, hcf101-2 and hcf01-3 are hcf mutants with impaired photosystem I. Our results indicate that Hcf101 is a novel component required for photosystem I biosynthesis.

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“…benzoate, phenylacetate, and 2-aminobenzoate) that incorporates features of both the classical aerobic and anaerobic pathways. These aerobic hybrid pathways start with the CoA-dependent activation of the aromatic acids, but then the dearomatization step requires molecular oxygen and the mechanism of ring cleavage is hydrolytic rather than oxygenolytic (3,(7)(8)(9).…”

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confidence: 99%