BIOCHEMICAL CHANGES OCCURRING DURING GROWTH AND SPORULATION OF
            <i>BACILLUS CEREUS</i>

Nakata, H. M.; Halvorson, H. O.

doi:10.1128/jb.80.6.801-810.1960

Cited by 95 publications

(56 citation statements)

References 19 publications

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“…The disappearance of ATCase correlates well with the rise in pH that occurs during postexponential growth. This pH rise has been shown to be due to oxidation of organic acids (mostly acetate, pyruvate, and lactate) that accumulate during growth on glucose (18). The changes in ATCase activity are not directly caused by the pH changes, since they also occur in a strongly buffered medium where the pH is constant.…”

Section: Resultsmentioning

confidence: 99%

Inactivation of Aspartic Transcarbamylase in Sporulating Bacillus subtilis : Demonstration of a Requirement for Metabolic Energy

Waindle

Switzer

1973

J Bacteriol

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The aspartic transcarbamylase (ATCase) activity of Bacillus subtilis cells disappears rapidly from stationary-phase cells prior to sporulation. ATCase activity does not appear in the culture fluid during the stationary phase; hence the enzyme appears to be inactivated in the cells. The enzyme is inactivated normally in two different mutants lacking proteases; the activity is very stable in crude extracts of cells or in the culture fluid. These results suggest that ATCase is not inactivated by the general proteolysis that occurs in sporulating bacteria. The inactivation of ATCase can be completely inhibited after it has begun by oxygen starvation or addition of fluoroacetate. Inhibitors of oxidative phosphorylation and electron transport also interrupt the inactivation of ATCase. The inactivation of ATCase is very slow in two mutant strains that are deficient in enzymes of tricarboxylic acid cycle. Addition of gluconate to stationary cultures of the mutant strains, which is known to restore depleted adenosine 5'-triphosphate pools in these bacteria, also restores inactivation of ATCase. These experiments support the conclusion that the generation of metabolic energy is necessary for the inactivation of ATCase in stationary cells.

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Section: Resultsmentioning

confidence: 99%

Inactivation of Aspartic Transcarbamylase in Sporulating Bacillus subtilis : Demonstration of a Requirement for Metabolic Energy

Waindle

Switzer

1973

J Bacteriol

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“…If it is assumed that all strains present in soil had sporulated equally well, then heat must have selected the strains forming the most heat-resistant spores (or forming spores activated by heat), and the relationship between heat resistance of spores and toxin production is an inverse one. This seems to be the case at least with C. perfringens (137,219). But it may also be assumed that oligosporogenous strains are present in soil, along with sporogenous ones; being a small minority, their spores, although heatresistant, might escape detection after heat treatment.…”

Section: Biochemical Aspectmentioning

confidence: 99%

“…From a rapidly metabolized growth substrate, such as glucose or glycerol, and in the presence of an utilizable nitrogen source, metabolites would be formed that would repress the synthesis of extracellular enzymes and of at least one early sporulation-specific enzyme, possibly related to the Krebs cycle. The repressing metabolites, which need not to be the same for all these enzymes, should not be produced from the substrates oxidized during sporulation, i.e., organic acids (80,137) and amino acids (24).…”

Section: Cytological Classification Of the Mutantsmentioning

confidence: 99%

Sporulation and the production of antibiotics, exoenzymes, and exotonins.

Schaeffer¹

1969

Bacteriological Reviews

213

137

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“…induces cell death via apoptosis (12)(13)(14). In particular, PA showed high antimicrobial activity at concentrations as low as 8 g/liter (15)(16)(17).…”

mentioning

confidence: 98%

Identification and Characterization of a Novel pic Gene Cluster Responsible for Picolinic Acid Degradation in Alcaligenes faecalis JQ135

Qiu

Zhao

et al. 2019

J Bacteriol

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Picolinic acid (PA) is a natural toxic pyridine derivative. Microorganisms can degrade and utilize PA for growth. However, the full catabolic pathway of PA and its physiological and genetic foundation remain unknown. In this study, we identified a gene cluster, designated picRCEDFB4B3B2B1A1A2A3, responsible for the degradation of PA from Alcaligenes faecalis JQ135. Our results suggest that PA degradation pathway occurs as follows: PA was initially 6-hydroxylated to 6-hydroxypicolinic acid (6HPA) by PicA (a PA dehydrogenase). 6HPA was then 3-hydroxylated by PicB, a four-component 6HPA monooxygenase, to form 3,6-dihydroxypicolinic acid (3,6DHPA), which was then converted into 2,5-dihydroxypyridine (2,5DHP) by the decarboxylase PicC. 2,5DHP was further degraded to fumaric acid through PicD (2,5DHP 5,6-dioxygenase), PicE (N-formylmaleamic acid deformylase), PicF (maleamic acid amidohydrolase), and PicG (maleic acid isomerase). Homologous pic gene clusters with diverse organizations were found to be widely distributed in Alpha-, Beta-, and Gammaproteobacteria. Our findings provide new insights into the microbial catabolism of environmental toxic pyridine derivatives. IMPORTANCE Picolinic acid is a common metabolite of L-tryptophan and some aromatic compounds and is an important intermediate in organic chemical synthesis. Although the microbial degradation/detoxification of picolinic acid has been studied for over 50 years, the underlying molecular mechanisms are still unknown. Here, we show that the pic gene cluster is responsible for the complete degradation of picolinic acid. The pic gene cluster was found to be widespread in other Alpha-, Beta-, and Gammaproteobacteria. These findings provide a new perspective for understanding the catabolic mechanisms of picolinic acid in bacteria.

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BIOCHEMICAL CHANGES OCCURRING DURING GROWTH AND SPORULATION OF BACILLUS CEREUS

Cited by 95 publications

References 19 publications

Inactivation of Aspartic Transcarbamylase in Sporulating Bacillus subtilis : Demonstration of a Requirement for Metabolic Energy

Inactivation of Aspartic Transcarbamylase in Sporulating Bacillus subtilis : Demonstration of a Requirement for Metabolic Energy

Sporulation and the production of antibiotics, exoenzymes, and exotonins.

Identification and Characterization of a Novel pic Gene Cluster Responsible for Picolinic Acid Degradation in Alcaligenes faecalis JQ135

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