The specificity of induction of β-glucosidase in Saccharomyces cerevisiae

Duerksen, Jacob D.; Halvorson, Harlyn O.

doi:10.1016/0006-3002(59)90068-x

Cited by 40 publications

(27 citation statements)

References 17 publications

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“…Several types of 3-glucosidase (EC 3.2.1.21) and j3-galactosidase (EC 3.2.1.23) activity have been studied in microorganisms (18)(19)(20)(21)(22). However, there are no detailed reports on the isolation or analysis of their properties from Rhizobium, although the presence of the enzymes, which degrade the cell wall of root hair, would be expected during the early step of infection.…”

Section: Discussionmentioning

confidence: 99%

.BETA.-Glucosidase and .BETA.-galactosidase from the periplasmic space of Rhizobium trifolii cells.

Abe

Higashi

1982

J. Gen. Appl. Microbiol.

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Section: Discussionmentioning

confidence: 99%

.BETA.-Glucosidase and .BETA.-galactosidase from the periplasmic space of Rhizobium trifolii cells.

Abe

Higashi

1982

J. Gen. Appl. Microbiol.

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“…Competent inducers, structurally related to the substrates of induced enzymes, though incapable of acting as substrates have been described for a variety of bacterial systems (Monod, Cohen- Duerksen & Halvorson, 1959). The failure to detect urocanate and glutamate formation from D-histidine by extracts of organism 232 supports the view that the D-isomer is behaving as a 'non-metabolizable' inducer.…”

Section: Discussionmentioning

confidence: 99%

The Adaptive Degradation of L-Histidine by Paracolobactrum aerogenoides

Tristram¹

1960

Journal of General Microbiology

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SUMMARYThe cliaracteristics of an induced enzyme system responsible for the degradation of L-histidine by a soil organism were studied. Induction could be achieved by exposing cells to L-histidine, D-histidine, urocanate, p-alanyl-L-histidine or L-histidyl-L-histidine, but not by exposure to a variety of other imidazoles. The kinetics of induction by L-and D-histidine differed considerably and the D-isomer was shown to be metabolized only very slowly by fully induced cells. Chloramphenicol and DL-p-fluorophenylalanine strongly inhibited enzyme synthesis, whilst a variety of purine and pyrimidine analogues were without effect. Nitrogen starvation of noninduced cells decreased but did not completely prevent the appearance of the enzyme system on induction with D-histidine. Non-induced cells possess a low level of ' basal ' enzymes before exposure to an inducing substance.

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“…To conclude, the Kluyver effect is not simply 'an extreme case of the Pasteur effect', as Gancedo and Serrano (1989) have suggested. It is true that some analogous regulatory mechanisms, such as the lessening of glycolytic flux, are concerned in Duerksen and Halvorson (1959) both effects. However, as these authors point out, the Pasteur effect involves other controls as, for example, competition for pyruvate between PDC and pyruvate dehydrogenase and the activation of 6-phosphofructokinase by increased concentration of inorganic phosphate.…”

Section: 7mentioning

confidence: 99%

The role of pyruvate decarboxylase in the Kluyver effect in the food yeast, Candida utilis

Sims¹,

Stålbrand²,

Barnett³

1991

Yeast

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The glucose‐fermenting yeast, Candida utilis cannot use the β‐D‐glucoside, cellobiose, anaerobically, although it is able to do so aerobically. β‐Glucoside transport and hydrolysis and pyruvate decarboxylase activities of this yeast were measured aerobically and anaerobically. β‐Glucoside transport was five‐fold faster aerobically than anaerobically, but there was no corresponding difference in β‐glucosidase activity. Pyruvate decarboxylase activity varied greatly, being synthesized de novo in response to the presence of D‐glucose and anaerobic conditions and about 50% deactivated on the removal of D‐glucose or the addition of air. Activation and deactivation were rapidly reversible. Failure to utilize cellobiose anaerobically, in particular, and the Kluyver effect, in general, probably depends on much reduced glycolytic flux, associated under anaerobic conditions, with (i) lower transport rate, (ii) low substrate affinity of the relevant glycosidase and (iii) deactivation of pyruvate decarboxylase. So, in addition to the complex effects of oxygen, anaerobiosis and specific sugars on induction, repression and derepression, there are fine controls on pyruvate decarboxylase activity, leading to fast activation or deactivation of the enzyme.

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The specificity of induction of β-glucosidase in Saccharomyces cerevisiae

Cited by 40 publications

References 17 publications

.BETA.-Glucosidase and .BETA.-galactosidase from the periplasmic space of Rhizobium trifolii cells.

.BETA.-Glucosidase and .BETA.-galactosidase from the periplasmic space of Rhizobium trifolii cells.

The Adaptive Degradation of L-Histidine by Paracolobactrum aerogenoides

The role of pyruvate decarboxylase in the Kluyver effect in the food yeast, Candida utilis

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