Amino Acid-β-Naphthylamide Hydrolysis by
            <i>Pseudomonas aeruginosa</i>
            Arylamidase

Riley, P. S.; Běhal, Francis J.

doi:10.1128/jb.108.2.809-816.1971

Cited by 23 publications

(12 citation statements)

References 23 publications

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“…Examination of the different strains determined, which is one half of the value reported for the enzyme from N. catarrhalis (6). However, it is quite close to the values determined for the arylamidases of Sarcina lutea (5) and P. aeruginosa (25).…”

Section: Discussionsupporting

confidence: 77%

“…The highest activity of the B. sphaericus enzyme was obtained with L-alanine-4-nitroanilide as substrate. A similar 2 S -specificity for L-alanine-fl-naphthylamide was Is)-1 106.M-1 also found for the enzymes of N. catarrhalis 7, P. aeruginosa (25), pathogen strains of Lepto-10 spira (11), and mammalian tissue (4). of B. sphaericus (Table 1) revealed a similar relationship in that those strains having a high rate of linuron degradation showed also some sporulation.…”

Section: Discussionmentioning

confidence: 54%

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Purification and Properties of an Aryl Acylamidase of Bacillus sphaericus, Catalyzing the Hydrolysis of Various Phenylamide Herbicides and Fungicides

Engelhardt¹,

Wallnöfer²,

Plapp³

1973

Applied Microbiology

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From Bacillus sphaericus ATCC 12123 an aryl acylamidase (EC 3.5.1.13) was purified to homogeneity by ion exchange chromatography, gel filtration, and polyacrylamide gel electrophoresis. The enzyme is inducible by various phenylamides of the acylanilide, phenylcarbamate, and methoxysubstituted phenylurea type. It has a molecular weight of 75,000. Enzyme activity was inhibited by sulfhydryl reagents, several metal ions, and 3,4-dichloroaniline (a product of linuron degradation). A requirement for divalent metal ions in enzyme activity could not be demonstrated. In the presence of 6 M urea an irreversible inactivation of the enzyme occurred. The hydrolysis of L-alanine-4-nitroanilide was competitively inhibited by puromycin.

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Section: Discussionsupporting

confidence: 77%

Section: Discussionmentioning

confidence: 54%

Purification and Properties of an Aryl Acylamidase of Bacillus sphaericus, Catalyzing the Hydrolysis of Various Phenylamide Herbicides and Fungicides

Engelhardt¹,

Wallnöfer²,

Plapp³

1973

Applied Microbiology

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“…Arylamidase enzymes mainly hydrolyse peptides containing L-amino acids with an unsubstituted a-amino group in the N-terminal residue 31 and one of the main amino acids released by this enzyme is leucine. 32 Therefore, the PC-DFA loading plots from GC-MS were produced (Fig. S3 †) and it was found that two variables were highly discriminatory (variables 17 and 49).…”

Section: Interpretation Of Gc-ms Prolesmentioning

confidence: 99%

Multiple metabolomics of uropathogenic E. coli reveal different information content in terms of metabolic potential compared to virulence factors

AlRabiah

Rattray

et al. 2014

Analyst

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No single analytical method can cover the whole metabolome and the choice of which platform to use may inadvertently introduce chemical selectivity. In order to investigate this we analysed a collection of uropathogenic Escherichia coli. The selected strains had previously undergone extensive characterisation using classical microbiological methods for a variety of metabolic tests and virulence factors. These bacteria were analysed using Fourier transform infrared (FT-IR) spectroscopy; gas chromatography mass spectrometry (GC-MS) after derivatisation of polar non-volatile analytes; as well as reversed-phase liquid chromatography mass spectrometry in both positive (LC-MS(+ve)) and negative (LC-MS(-ve)) electrospray ionisation modes. A comparison of the discriminatory ability of these four methods with the metabolic test and virulence factors was made using Procrustes transformations to ascertain which methods produce congruent results. We found that FT-IR and LC-MS(-ve), but not LC-MS(+ve), were comparable with each other and gave highly similar clustering compared with the virulence factors tests. By contrast, FT-IR and LC-MS(-ve) were not comparable to the metabolic tests, and we found that the GC-MS profiles were significantly more congruent with the metabolic tests than the virulence determinants. We conclude that metabolomics investigations may be biased to the analytical platform that is used and reflects the chemistry employed by the methods. We therefore consider that multiple platforms should be employed where possible and that the analyst should consider that there is a danger of false correlations between the analytical data and the biological characteristics of interest if the full metabolome has not been measured.

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“…The appearance of aminopeptidases, intracellularly and extracellularly, in cultures of many bacterial species has been noted (e.g., 4,5,18,22). In the genus Bacillus, Aubert and Millet (2) reported an aminopeptidase in B. megaterium which increases fivefold in activity during sporulation.…”

mentioning

confidence: 99%

Aminopeptidases of Bacillus subtilis

Desmond¹,

Starnes²,

Běhal³

1975

J Bacteriol

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Three enzymes with Land one enzyme with D-aminopeptidase (EC 3.4.11; a-aminoacyl peptide hydrolase) activity have been separated from each other and partially purified from Bacillus subtilis 168 W. T., distinguished with respect to their molecular weights and catalytic properties, and studied in relation to the physiology of this bacterium. One L-aminopeptidase, designated aminopeptidase I, has a molecular weight of 210,000 i 20,000, is produced early in growth, and hydrolyzes L-alanyl- ,-naphthylamide most rapidly. Another, designated aminopeptidase II, molecular weight 67,000 i 10,000, is also produced early in growth and hydrolyzes L-lysyl-,@-naphthylamide most rapidly. A third, aminopeptidase III, molecular weight 228,000 i 20,000, is produced predominantly in early stationary phase and most efficiently utilizes L-a-aspartyl- ,-naphthylamide as substrate. The synthesis of aminopeptidase III in early stationary phase suggests that selective catabolism of peptides occurs at this time, perhaps related to the cessation of growth or the onset of early sporulation-associated events. A D-aminopeptidase which hydrolyzes the carboxyl-blocked dipeptide D-alanyl-Dalanyl-B-naphthylamide (as well as D-alanyl-,B-naphthylamide and D-alanyl-Dalanyl-D-alanine) has also been identified, separated from aminopeptidase II, and purified 170-fold. D-Aminopeptidase, molecular weight 220,000 1 20,000, is localized predominantly in the cell wall and periplasm of the organism. This evidence and the variation of the activity during the growth cycle suggest an important function in cell wall or peptide antibiotic metabolism.

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Amino Acid-β-Naphthylamide Hydrolysis by Pseudomonas aeruginosa Arylamidase

Cited by 23 publications

References 23 publications

Purification and Properties of an Aryl Acylamidase of Bacillus sphaericus, Catalyzing the Hydrolysis of Various Phenylamide Herbicides and Fungicides

Purification and Properties of an Aryl Acylamidase of Bacillus sphaericus, Catalyzing the Hydrolysis of Various Phenylamide Herbicides and Fungicides

Multiple metabolomics of uropathogenic E. coli reveal different information content in terms of metabolic potential compared to virulence factors

Aminopeptidases of Bacillus subtilis

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