Some observations on the phosphoroclastic dissimilation of pyruvate by cell-free extracts of Escherichia coli

Asnis, Robert E.; Fritz, Maryann; Glick, Mary Catherine

doi:10.1016/0006-3002(56)90074-9

Cited by 5 publications

(7 citation statements)

References 2 publications

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“…However, it seems likely that this factor is a protein and it may be identical to the protein of low molecular weight and considerable stability at pH 4.0 reported to be a component of the pyruvate formate-lyase system of Midwinter et al (Federation Proc., p. 531, 1965). In consideration of the heat stability of the activation factor of E. coli, it is likely that such a factor is also an active component of the stimulatory heated extract preparations from M. lactilyticus, C. butyricwn, C. pasteurianum, and Peptococcus aerogenes (16); however, these preparations may also contain SAM, which is probably the stimulatory component of rat liver and yeast (1,13,24).…”

Section: Discussionmentioning

confidence: 99%

“…Proc., p. 97,1954), Clostridium butyricum (17), and Micrococcus lactilyticus (15,17) show disproportionately low activity with low amounts of extract, a phenomenon termed "dilution effect." The E. coli system has also been reported to be stimulated by boiled extract of yeast (1,24), and both the E. coli and M. lactilyticus systems are stimulated by a heated (65 C) extract of these bacteria (1, 16) as well as by preparations derived from bacteria that do not carry out the pyruvate-formate exchange reaction (16; Novelli et al, Bacteriol. Proc., p. 97, 1954).…”

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confidence: 99%

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Role of Pyruvate and S -Adenosylmethionine in Activating the Pyruvate Formate-Lyase of Escherichia coli

Chase

Rabinowitz

1968

J Bacteriol

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The pyruvate formate-lyase activity of extracts of Escherichia coli is stimulated and the dilution effect is abolished by the addition of pyruvate to the extract. The activity can be purified fourfold from pyruvate-supplemented extracts by isoelectric precipitation under anaerobic conditions. The activity of extracts not supplemented with pyruvate has been separated into two fractions by treatment with protamine sulfate-fraction PS, the soluble portion, and fraction N, an extract of the precipitate formed upon the addition of protamine sulfate. After treatment of these fractions with charcoal, pyruvate formate-lyase activity is stimulated by the addition of S-adenosylmethionine. When sodium pyruvate is added to the crude extract before the fractionation, fraction PS has full enzymatic activity and is not stimulated by fraction N or by S-adenosylmethionine. Incubation of the inactive fractions with pyruvate and S-adenosylmethionine in the absence of other substrates similarly results in a highly active preparation, not subject to the "dilution effect" obtained

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Section: Discussionmentioning

confidence: 99%

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confidence: 99%

Role of Pyruvate and S -Adenosylmethionine in Activating the Pyruvate Formate-Lyase of Escherichia coli

Chase

Rabinowitz

1968

J Bacteriol

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“…Micrococcus LC (Peel, 1960) degrades a-ketobutyrate, but not a-ketoglutarate, by the same pathway of oxidative decarboxylation, whereas Streptococcus faecalis (Gunsalus, 1953) carries out a dismutation of a-ketobutyrate. Formate is not produced from these a-keto acids by extracts of E. coli (Asnis et al, 1956).…”

Section: Effectmentioning

confidence: 96%

“…Reaction 2 was first demonstrated in extracts of Escherichia coli (Utter and Werkman, 1943) and shown to be reversible by measurements of the exchange of C'3-labeled formate into pyruvate (Utter, Werkman, and Lipmann, 1944;Utter, Lipmann, and Werkman, 1945). CoA, DPT, and possibly magnesium or manganese ions (Chantrenne and Lipmann, 1950;Strecker, 1951;Asnis, Fritz, and Glick, 1956) have been reported to be cofactors for both the degradation of pyruvate and formate exchange via reaction 2. Although the C1 compound exchanges rapidly with the carboxyl group of pyruvate, only a very low exchange of the C2 moiety, as acetate, acetate plus adenosine triphosphate (ATP), acetyl phosphate, or acetyl-CoA has been observed.…”

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confidence: 99%

DEGRADATION OF PYRUVATE BY MICROCOCCUS LACTILYTICUS I

1962

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At an alkaline pH, extracts of Micrococcus lactilyticus2 catalyze the phosphoroclastic degradation of pyruvate to formate and acetyl phosphate and the rapid exchange of formate into the carboxyl group of pyruvate. At an acid pH, hydrogen, carbon dioxide, and acetyl phosphate are produced, and carbon dioxide is exchanged into the carboxyl group of pyruvate. A concentration of approximately 1 M phosphate is required for the phosphoroclastic reaction and formate exchange; the production of carbon dioxide and hydrogen is greatly inhibited by high concentrations of phosphate. Formate exchange requires a divalent metal ion and is stimulated by reducing agents and an atmosphere of hydrogen. Inhibition by p-chloromercuribenzoate, ZnH, Cd+, and arsenite indicates that sulfhydryl groups on the enzyme are involved in the reaction; the inhibition by arsenite and Cd may be relieved by 2,3-dimercaptopropanol, suggesting that vicinal dithiols may be required. Inhibition by hypophosphite may reflect a competition with formate for a site on the enzyme. At an alkaline pH, oa-ketobutyrate is degraded to propionate and formate, whereas a-ketoglutarate is fermented to succinate, propionate, carbon dioxide, hydrogen, and formate. Formate is exchanged into the carboxyl groups of aketobutyrate and a-ketoglutarate under these conditions. Only traces of a-ketovalerate and

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“…yeast extract), and heatinactivated crude extracts ("kochsaft"). Studies with Escherichia coli (Strecker, 1951;Novelli, Gest, and Krampitz, 1954; Asnis, Fritz, and Glick, 1956) and Streptococcuis faecalis (Wood and O'Kane, 1960) showed that natural products or "kochsafts" could be replaced only partially, or not at all, by mixtures of known cofactors although certain cofactors stimulated exchange. Thus in E. coli, coenzyme A (CoA) and diphosphothiamine (DPT) are required (Chantrenne and Lipmann, 1950; Strecker, 1951), and tetrahydrofolate is stimulatory (Chin, Krampitz, and Novelli, 1957), wvhereas in S.faecalis exchange is enhanced by tetrahydrofolate (Wood and O'-Kane, 1960).…”

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confidence: 99%