A multispecific quintet of aromatic aminotransferases that overlap different biochemical pathways in Pseudomonas aeruginosa.

Whitaker, Robert J.; Gaines, C G; Jensen, Roy A.

doi:10.1016/s0021-9258(18)33482-3

Cited by 56 publications

(5 citation statements)

References 22 publications

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“…Thus, three subfamily Iβ paralogs of aminotransferase are expressed in P. aeruginosa : one for aromatic biosynthesis in the cytoplasm, one for histidine biosynthesis in the cytoplasm, and one for phenylalanine synthesis in the periplasm. Previous enzymological work had demonstrated the existence of five aminotransferases in P. aeruginosa that were capable of functioning as aromatic aminotransferases in vitro [ 35 ].…”

Section: Discussionmentioning

confidence: 99%

The emerging periplasm-localized subclass of AroQ chorismate mutases, exemplified by those from Salmonella typhimurium and Pseudomonas aeruginosa

Calhoun

Bonner²,

Gu³

et al. 2001

Genome Biol

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Background: Chorismate mutases of the AroQ homology class are widespread in the Bacteria and the Archaea. Many of these exist as domains that are fused with other aromatic-pathway catalytic domains. Among the monofunctional AroQ proteins, that from Erwinia herbicola was previously shown to have a cleavable signal peptide and located in the periplasmic compartment. Whether or not this might be unique to E. herbicola was unknown.

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Section: Discussionmentioning

confidence: 99%

The emerging periplasm-localized subclass of AroQ chorismate mutases, exemplified by those from Salmonella typhimurium and Pseudomonas aeruginosa

Calhoun

Bonner²,

Gu³

et al. 2001

Genome Biol

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show abstract

“…Pseudomonads are well known for their ability to degrade and synthesize aromatic compounds (76). Therefore, it is not surprising that they have also developed a large repertoire of aminotransferases with activity on aromatic substrates (77,78). The only aminotransferase we identified in an aromatic amino acid condition (L-phenylalanine) is PP_3590 (24.0).…”

Section: Resultsmentioning

confidence: 99%

Nitrogen Metabolism in Pseudomonas putida: Functional Analysis Using Random Barcode Transposon Sequencing

Schmidt

Pearson

Incha

et al. 2022

Appl Environ Microbiol

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“…Pseudomonads are well known for their ability to degrade and synthesize aromatic compounds (79). Therefore, it is not surprising that they have also developed a large repertoire of aminotransferases with activity on aromatic substrates (80,81). The only aminotransferase we identified in an aromatic amino acid condition (L-phenylalanine) is PP_3590 (-4.0).…”

Section: Proteinogenic Amino Acidsmentioning

confidence: 99%

“…80 °C as zero timepoints. The libraries were washed three times in MOPS minimal medium with no nitrogen source, and then used to inoculate each experiment at a ratio of 1:100.…”

mentioning

confidence: 99%

Nitrogen metabolism in Pseudomonas putida: functional analysis using random barcode transposon sequencing

Schmidt

Pearson

Incha

et al. 2021

Preprint

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Pseudomonas putida KT2440 has long been studied for its diverse and robust metabolisms, yet many genes and proteins imparting these growth capacities remain uncharacterized. Using pooled mutant fitness assays, we identified genes and proteins involved in the assimilation of 52 different nitrogen containing compounds. To assay amino acid biosynthesis, 19 amino acid drop-out conditions were also tested. From these 71 conditions, significant fitness phenotypes were elicited in 672 different genes including 100 transcriptional regulators and 112 transport-related proteins. We divide these conditions into 6 classes, and propose assimilatory pathways for the compounds based on this wealth of genetic data. To complement these data, we characterize the substrate range of three promiscuous aminotransferases relevant to metabolic engineering efforts in vitro. Furthermore, we examine the specificity of five transcriptional regulators, explaining some fitness data results and exploring their potential to be developed into useful synthetic biology tools. In addition, we use manifold learning to create an interactive visualization tool for interpreting our BarSeq data, which will improve the accessibility and utility of this work to other researchers.

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A multispecific quintet of aromatic aminotransferases that overlap different biochemical pathways in Pseudomonas aeruginosa.

Cited by 56 publications

References 22 publications

The emerging periplasm-localized subclass of AroQ chorismate mutases, exemplified by those from Salmonella typhimurium and Pseudomonas aeruginosa

The emerging periplasm-localized subclass of AroQ chorismate mutases, exemplified by those from Salmonella typhimurium and Pseudomonas aeruginosa

Nitrogen Metabolism in Pseudomonas putida: Functional Analysis Using Random Barcode Transposon Sequencing

Nitrogen metabolism in Pseudomonas putida: functional analysis using random barcode transposon sequencing

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