Rapid Methods for Determining Decarboxylase Activity: Ornithine and Lysine Decarboxylases

The catabolic products of arginine metabolism were observed in Aphanocapsa 6308, a unicellular cyanobacterium, by thin layer chromatography of growth media, by limiting growth conditions, and by enzymatic analysis. Of the organic, nitrogenous compounds examined, only arginine supported growth in CO2-free media. The excretion of ornithine at a concentration level greater than citrulline suggested the existence in Aphanocapsa 6308 of the arginine dihydrolase pathway which produced ornithine, CO2,NH4,+ adenosine 5'-triphosphate. Its existence was confirmed by enzymatic analysis. Although cells could not grow on urea as a sole carbon source a very active urease and subsequently an arginase were also demonstrated, indicating that Aphanocapsa can metabolize arginine via the arginase pathway. The level of enzymes for both pathways indicates a lack of genetic control. It is suggested that the arginase pathway provides only nitrogen for the cells wheras the arginine dihydrolase pathway provides not only nitrogen, but also CO2 and adenosine 5'-triphosphate.

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Arginine catabolism in Aphanocapsa 6308

Weathers

Chee

Allen

1978

Arch. Microbiol.

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Rapid Methods for Determining Decarboxylase Activity: Arginine Decarboxylase

Goldschmidt

Lockhart

1971

Appl Microbiol

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A rapid biochemical method for the determination of arginine decarboxylase (EC 4.1.1.19) activity has been developed for use in the routine clinical microbiology laboratory and correlated with similar procedures for ornithine and lysine decarboxylase (EC 4.1.1.18) systems. It is based on the detection of agmatine, the amine end product formed during growth on a synthetic medium containing arginine as the key amino acid. A modified diacetyl reagent is used to detect this amine after a differential butanol extraction of the cultures. This procedure can be used to detect this amine after a 1- to 4-hr incubation period (with the use of an initial concentrated inoculum) or with an overnight culture. Thus, both an indirect measurement based on the alkalinization of the medium and a lengthy incubation period were avoided. Parameters for optimal enzyme activity and the pertinent enzyme systems involved in arginine and agmatine catabolism are discussed in detail.

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Rapid Ornithine Decarboxylase Test for the Identification of Enterobacteriaceae

Fay

Barry

1972

Appl Microbiol

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Conventional methods for detecting ornithine decarboxylase activity require an extended period of incubation. However, with a few simple modifications, accurate results were obtained within a few hours rather than several days. The broth medium was modified, primarily by omitting glucose and by decreasing the p H to 5.5. A 1-ml amount of this broth was inoculated with one colony and then overlaid with sterile mineral oil. Within 2 to 4 hr, the p H increased if ornithine was decarboxylated, thus changing the color of the internal p H indicator to a dark purple. If the amino acid was not decarboxylated, the p H decreased to p H 5.0 to 5.2, enough to give a definite yellow color. With 347 selected clinical isolates, the rapid test gave results identical to those obtained in 1 to 4 days with Moeller's decarboxylase medium. Less reliable results were obtained with Difco's decarboxylase medium with 0.3% agar which was stabinoculated and read after 18 to 24 hr without a mineral oil seal. The rapid ornithine decarboxylase test represents a simple, accurate technique which is well suited for the clinical microbiology laboratory.

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Rapid Methods for Determining Decarboxylase Activity: Ornithine and Lysine Decarboxylases

Cited by 10 publications

References 7 publications

Arginine catabolism in Aphanocapsa 6308

Arginine catabolism in Aphanocapsa 6308

Rapid Methods for Determining Decarboxylase Activity: Arginine Decarboxylase

Rapid Ornithine Decarboxylase Test for the Identification of Enterobacteriaceae

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