Role of 4-aminobutyrate aminotransferase in the arginine metabolism of Pseudomonas aeruginosa

Voellym, R; Leisinger, Thomas

doi:10.1128/jb.128.3.722-729.1976

Cited by 55 publications

(24 citation statements)

References 21 publications

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“…This enzyme belongs to the fold-type I subgroup II pyridoxalphosphate-dependent aminotransferase family, in which GABA-AT is also categorized (Mehta et al, 1993). Indeed, in Pseudomonas aeruginosa a transaminase has comparable specific activity with GABA and N-acetylornithine (Voellmy and Leisinger, 1976).…”

Section: Figmentioning

confidence: 99%

“…A GABA shunt may be advantageous to cyanobacteria (Nogales et al, 2012), and we had hypothesized that Slr1022 might function as GABA aminotransferase (GABA-AT) as this protein is the Synechocystis protein closest to GABA-AT from E. coli, with 34% identity with E. coli GABA-AT over 400 of its 429 residues. Also, in Pseudomonas aeruginosa a transaminase was reported to have comparable specific activity with GABA and N-acetylornithine (Voellmy and Leisinger, 1976). A comparison of the GABA and N-acetylornithine aminotransferases is provided in Supporting Information, including in Fig.…”

Section: Metabolites In the Gaba Pathway Affect The Growth Of Individmentioning

confidence: 99%

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The γ‐aminobutyric acid shunt contributes to closing the tricarboxylic acid cycle in Synechocystis sp. PCC 6803

Xiong

Brune

Vermaas

2014

Molecular Microbiology

105

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SummaryA traditional 2-oxoglutarate dehydrogenase complex is missing in the cyanobacterial tricarboxylic acid cycle. To determine pathways that convert 2-oxoglutarate into succinate in the cyanobacterium Synechocystis sp. PCC 6803, a series of mutant strains, Δsll1981, Δslr0370, Δslr1022 and combinations thereof, deficient in 2-oxoglutarate decarboxylase (Sll1981), succinate semialdehyde dehydrogenase (Slr0370), and/or in γ-aminobutyrate metabolism (Slr1022) were constructed. Like in Pseudomonas aeruginosa, N-acetylornithine aminotransferase, encoded by slr1022, was shown to also function as γ-aminobutyrate aminotransferase, catalysing γ-aminobutyrate conversion to succinic semialdehyde. As succinic semialdehyde dehydrogenase converts succinic semialdehyde to succinate, an intact γ-aminobutyrate shunt is present in Synechocystis. The Δsll1981 strain, lacking 2-oxoglutarate decarboxylase, exhibited a succinate level that was 60% of that in wild type. However, the succinate level in the Δslr1022 and Δslr0370 strains and the Δsll1981/Δslr1022 and Δsll1981/Δslr0370 double mutants was reduced to 20-40% of that in wild type, suggesting that the γ-aminobutyrate shunt has a larger impact on metabolite flux to succinate than the pathway via 2-oxoglutarate decarboxylase. 13C-stable isotope analysis indicated that the γ-aminobutyrate shunt catalysed conversion of glutamate to succinate. Independent of the 2-oxoglutarate decarboxylase bypass, the γ-aminobutyrate shunt is a major contributor to flux from 2-oxoglutarate and glutamate to succinate in Synechocystis sp. PCC 6803.

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Section: Figmentioning

confidence: 99%

Section: Metabolites In the Gaba Pathway Affect The Growth Of Individmentioning

confidence: 99%

The γ‐aminobutyric acid shunt contributes to closing the tricarboxylic acid cycle in Synechocystis sp. PCC 6803

Xiong

Brune

Vermaas

2014

Molecular Microbiology

105

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“…In addition, putrescine is a reported substrate for 4-aminobutyrate aminotransferase ( [24], see below) and oJ-amino acid aminotransferase ( [25], see below), but it seems improbable that these activities are physiologically significant.…”

Section: Breakdown Of Putrescinementioning

confidence: 99%

Enzymes and pathways of polyamine breakdown in microorganisms

Large

1992

FEMS Microbiology Letters

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The information currently available on the breakdown of spermidine and putrescine by microorganisms is reviewed. Two major metabolic routes have been described, one for the free bases via δ1‐pyrroline (4‐aminobutyraldehyde), the other via N‐acetyl derivatives. In both pathways oxidases or aminotransferases are the key enzymes in removing the nitrogen atoms. The two routes converge at 4‐aminobutyrate, which is then metabolized via succinate. The degradation of putrescine in Escherichia coli has been well characterized at both genetic and biochemical levels, but for other bacteria much less information is available. The C3 moiety of spermidine is broken down via β‐alanine, but the metabolism of this compound and its precursors is poorly understood. In yeasts, a catabolic route for spermidine and putrescine via N‐acetyl derivatives has been described in Candida boidinii, and the evidence for its occurrence in other species is reviewed. Except for the terminal step of this pathway, the same group of enzymes can metabolize both the C3 and C4 moieties of spermidine. It is likely that other routes of polyamine catabolism also exist in both bacteria and yeasts.

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“…These apparent discrepancies could be explained by putrescine formation from arginine uia agmatine, through the sequential action of arginine decarboxylase and agmatine ureohydrolase (Abdelal 1979), a pathway thought to exist in Ps. aeruginosa (Voellmy & Leisinger 1976) despite some evidence to the contrary (Moss et al. 1972).…”

Section: S I N G L E C U L T U R E Smentioning

confidence: 99%

Bacterial sources of putrescine and cadaverine in chill stored vacuum‐packaged beef

Dainty

Edwards

Hibbard

et al. 1986

Journal of Applied Bacteriology

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Of the meat strains of streptobacteria, leuconostocs, Enterobacteriaceae and Brochothrix thermosphacta tested, only Hafnia alvei and Serratia liquefaciens showed diamine-producing potential during growth in pure culture on beef stored in vacuum packs at 1 degree C. Both organisms produced cadaverine at concentrations similar to those reported previously in naturally contaminated beef stored under the same conditions. Putrescine concentrations produced by the two organisms, however, were an order of magnitude lower. During the growth on beef of either H. alvei or S. liquefaciens in mixed culture with arginine-utilizing strains of streptobacteria, putrescine as well as cadaverine concentrations were similar to those detected in naturally contaminated samples.

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Role of 4-aminobutyrate aminotransferase in the arginine metabolism of Pseudomonas aeruginosa

Cited by 55 publications

References 21 publications

The γ‐aminobutyric acid shunt contributes to closing the tricarboxylic acid cycle in Synechocystis sp. PCC 6803

The γ‐aminobutyric acid shunt contributes to closing the tricarboxylic acid cycle in Synechocystis sp. PCC 6803

Enzymes and pathways of polyamine breakdown in microorganisms

Bacterial sources of putrescine and cadaverine in chill stored vacuum‐packaged beef

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