Decarboxylase and other Reactions of some Gram-negative Rods

Steel, Karl; Midgley, J.

doi:10.1099/00221287-29-1-171

Cited by 9 publications

(1 citation statement)

References 26 publications

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“…M0ller's method (12) for detecting amino acid decarboxylation reactions in the Enterobacteriaceae has been adopted as the standard reference method for most clinical microbiologists (4-7, 15, 18,21). The designations of ornithine and lysine decarboxylase are very straightforward.…”

Section: Resultsmentioning

confidence: 99%

Rapid Methods for Determining Decarboxylase Activity: Arginine Decarboxylase

Goldschmidt¹,

Lockhart²

1971

Applied Microbiology

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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 1to 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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Section: Resultsmentioning

confidence: 99%

Rapid Methods for Determining Decarboxylase Activity: Arginine Decarboxylase

Goldschmidt¹,

Lockhart²

1971

Applied Microbiology

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Determination of bacterial decarboxylases of some amino acids by means of high voltage paper electrophoresis

Ferencík

1965

Folia Microbiol

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Catabolism of L-Lysine by Pseudomonas aeruginosa

Fothergill

Guest

1977

Journal of General Microbiology

123

102

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SUMMARYPseudomonas aeruginosa PACI grows poorly on L-lysine as sole source of carbon but mutant derivatives which grow rapidly were readily isolated. Studies with one such mutant, P. aeruginosa ~~~5 8 6 , supported the existence of a route for L-lysine catabolism which differs from those reported previously in other species of Pseudomonas. The postulated route, the cadaverine or decarboxylase pathway, is initiated by the decarboxylation of L-lysine and involves the following steps: L-lysine -+ cadaverine -+ I -piperideine -+ 5-aminovalerate + glutarate semialdehyde -+ glutarate. Evidence for this pathway is based on the characterization of the pathway reactions and the induction of the corresponding enzymes by growth on Llysine. The first three enzymes were also induced by growth on cadaverine and to a lesser extent by 5-aminovalerate. No evidence was obtained for the presence of pathways involving L-lysine 2-monooxygenase or L-pipecolate dehydrogenase, but another potential route for L-lysine catabolism initiated by L-lysine 6-aminotransferase was detected. Studies with mutants unable to grow on L-lysine supported the existence of more than one catabolic pathway for L-lysine in this organism and indicated that all routes converge on a pathway for glutarate catabolism which generates acetyl-CoA. Pipecolate catabolism also appeared to converge on the glutarate pathway in P. aeruginosa. The results suggested that the growth rate of the parental strain is limited by the rate of transport and/or decarboxylation of L-lysine. The cadaverine pathway was present, but not so highly induced, in the parental strain P. aeruginosa PACI . Pseudomonas JEuorescens contained enzymes of both the cadaverine (decarboxylase) and oxygenase pathways, strains of P. putida (biotypes A and B) contained enzymes of the oxygenase pathway but not the decarboxylase pathway and P. multivorans appeared deficient in both. All these species possessed L-lysine aminotransferase activity.

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Decarboxylase and other Reactions of some Gram-negative Rods

Cited by 9 publications

References 26 publications

Rapid Methods for Determining Decarboxylase Activity: Arginine Decarboxylase

Rapid Methods for Determining Decarboxylase Activity: Arginine Decarboxylase

Determination of bacterial decarboxylases of some amino acids by means of high voltage paper electrophoresis

Catabolism of L-Lysine by Pseudomonas aeruginosa

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