The Effect of Carbohydrates on the Tryptophanase Activity of Bacteria

Boyd, William L.; Lichstein, Herman C.

doi:10.1128/jb.69.5.584-589.1955

Cited by 30 publications

(10 citation statements)

References 7 publications

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“…The relatively low activity of the other compounds tested would presumably reflect the fact that they are not as efficiently converted to an inhibitor of tryptophanase. It is pertinent in this regard that the addition of pyruvate to preadapted resting cells caused a marked suppression of tryptophanase activity (Boyd, 1954).…”

Section: Resultsmentioning

confidence: 99%

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Inhibitory Effect of Glucose on Tryptophanase

Freundlich

Lichstein

1960

J Bacteriol

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Earlier studies from this and other laboratories have shown that the presence of glucose inhibits the formation of certain inducible enzymes in bacteria (Boyd and Lichstein, 1955; Magasanik, 1957). This phenomenon is not specific to glucose, but rather is shared by other carbohydrates utilized by the bacterial cells. Although several mechanisms have been proposed to explain this carbohydrate effect, the basic nature of the inhibition is still unknown. The present studies were initiated in an attempt to elucidate the mechanism of the inhibitory effect of glucose on the formation of tryptophanase in Escherichia coli.

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Section: Resultsmentioning

confidence: 99%

“…Two strains of E. coli were employed, namely Crookes (ATCC 8739) and ATCC 9723E. The growth medium was identical to that used in previous studies (Boyd and Lichstein, 1955) and contained 5 X 104 M DL-tryptophan. The vitamin -free acid hydrolyzed casein (Difco) employed in the medium was free of tryptophan as determined by microbiological assay.…”

Section: Methodsmentioning

confidence: 99%

Inhibitory Effect of Glucose on Tryptophanase

Freundlich

Lichstein

1960

J Bacteriol

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“…Glucose concentration in medium also does not appear to play a critical role in loss of 3MI-forming activity. On the basis of work with mixed ruminal cultures (29), it was suggested that glucose may cause repression of the 3MIforming enzyme analogous to glucose repression of tryptophanase (2,10). In this present study, induction of the 3MI-forming enzyme was achieved at 55 mM glucose.…”

Section: Discussionmentioning

confidence: 99%

Effect of Indoleacetic Acid and Related Indoles on Lactobacillus sp. Strain 11201 Growth, Indoleacetic Acid Catabolism, and 3-Methylindole Formation

Honeyfield

Carlson

1990

Appl Environ Microbiol

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A study was conducted to determine the activity of the 3-methylindole (3MI)-forming enzyme in Lactobacillus sp. strain 11201. Cells were incubated anaerobically with 17 different indolic and aromatic compounds. Indoleacetic acid (IAA), 5-hydroxyindoleacetic acid, 5-methoxy-3-indoleacetic acid, indole-3-pyruvate, or indole-3-propionic acid induced 3MI-forming activity. The highest total enzyme activity induced by IAA was observed in cells incubated with an initial concentration of 1.14 mM IAA. Peak activity of the 3MI-forming enzyme occurred 4 h after bacteria were incubated with either 0.114 or 1.14 mM IAA. Enzyme activity peaked earlier (2 h) and disappeared more rapidly at 5.7 mM IAA than at other concentrations of IAA. The effects of IAA and 3MI on the growth of Lactobacilus sp. strain 11201 and formation of 3MI from IAA also were determined. Bacterial growth and 3MI formation from IAA were reduced in medium containing exogenous 3MI. The growth depression observed in medium containing 5.7 mM IAA appears to be due to the toxicity of 3MI rather than IAA. The formation of 3MI in this ruminal Lactobacillus sp. is mediated by an inducible enzyme, and as 3MI accumulates, bacterial growth and rates of 3MI formation from IAA are reduced.

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“…Virtually no enzyme was produced in media containing trehalose or maltose while all the other sugars tested permitted the development of tyrosinase. In this connection, it is worth noting that Boyd and Lichstein (1955) found that carbohydrates depressed tryptophanase activity in bacteria while Epps and Gale (1942) found the same to be true for bacterial deaminase and other systems. As in the present work, no correlation could be found with the amount of growth in these various media.…”

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confidence: 89%