Purification of pyruvate formate-lyase from Streptococcus mutans and its regulatory properties

Takahashi, S; Abbe, K; Yamada, Tadashi

doi:10.1128/jb.149.3.1034-1040.1982

Cited by 95 publications

(42 citation statements)

References 19 publications

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“…When the pH drops to values below 6.0 no more formate is produced from citrate or lactose. This is in agreement with the narrow pH opti- mum of 7.5 as reported for PFL in the lactic acid bacterium Streptococcus mutans [68].…”

Section: P);rut'ate Formate Lyase (Reaction 2)supporting

confidence: 91%

“…Pyruvate formate lyase (PFL) is in many (facultative) anaerobic bacteria responsible for the production of formate, acetate and ethanol from pyruvate; the so-called mixed acid fermentation [67,68]. The enzyme is present in most homofermentative lactic acid bacteria, but has not been found in the heterofermentative Leuconostoc [14,54,55].…”

Section: P);rut'ate Formate Lyase (Reaction 2)mentioning

confidence: 99%

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Citrate metabolism in lactic acid bacteria

Hugenholtz¹

1993

FEMS Microbiology Reviews

347

170

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Citrate metabolism plays an important role in many food fermentations involving lactic acid bacteria. Since citrate is a highly oxidized substrate, no reducing equivalents are produced during its degradation, resulting in the formation of metabolic end products other than lactic acid. Some of these end products, such as diacetyl and acetaldehyde, have very distinct aroma properties and contribute significantly to the quality of the fermented foods. In this review the metabolic pathways involved in product formation from citrate are described, the bioenergetic consequences of this metabolism for the lactic acid bacteria are discussed and detailed information on some key enzymes in the citrate metabolism is presented. The combined knowledge is used for devising strategies to avoid, control or improve product formation from citrate.

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Section: P);rut'ate Formate Lyase (Reaction 2)supporting

confidence: 91%

Section: P);rut'ate Formate Lyase (Reaction 2)mentioning

confidence: 99%

Citrate metabolism in lactic acid bacteria

Hugenholtz¹

1993

FEMS Microbiology Reviews

347

170

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“…A gradual increase in the aeration level led to a gradual increase in acetate and a decrease in formate and ethanol [65]. The main reason for these effects is the extreme sensitivity of pyruvate formate-lyase to O z [63,64,[66][67][68]. Cells of S. mutans exposed to 02 for 2 min lost 94% of their activity [63].…”

Section: The Pyruvate Formate-lyase Pathway To Formate Acetate and Ementioning

confidence: 99%

Responses of lactic acid bacteria to oxygen

Condón

1987

FEMS Microbiology Letters

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Key words: Lactic acid bacteria; Oxygen SUMMARY 2. INTRODUCTIONA small number of flavoprotein oxidase enzymes are responsible for the direct interaction of lactic acid bacteria (LAB) with oxygen; hydrogen peroxide or water are produced in these reactions. In some cultures exposed to oxygen, hydrogen peroxide accumulates to inhibitory levels.Through these oxidase enzymes and NADH peroxidase, 02 and H202 can accept electrons from sugar metabolism, and thus have a sparing effect on the use of metabolic intermediates, such as pyruvate or acetaldehyde, as electron acceptors. Consequently, sugar metabolism in aerated cultures of LAB can be substantially different from that in unaerated cultures. Energy and biomass yields, end-products of sugar metabolism and the range of substrates which can be metabolised are affected.Lactic acid bacteria exhibit an inducible oxidative stress response when exposed to sublethal levels of H202. This response protects them if they are subsequently exposed to lethal concentrations of H202. The effect appears to be related to other stress responses such as heat-shock and is similar, in some but not all respects, to that previously reported for enteric bacteria.

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“…For pyruvate kinase and LDH, the results from our own experiments were used. Most of the Michaelis constants were derived from enzymes of related organisms found in the literature [13,34,36,40,43,[57][58][59][60][61][62][63][64], for example, from Streptococcus mutans or Streptococcus thermophilus. If no information was available, we adopted the missing parameters from the L. lactis model.…”

Section: Methodsmentioning

confidence: 99%

“…Enzyme-specific activities were converted into V max values as described for L. lactis. V max values were derived from previous publications [13,[35][36][37]39,43,[57][58][59][62][63][64][65].…”

Section: Methodsmentioning

confidence: 99%

Role of phosphate in the central metabolism of two lactic acid bacteria – a comparative systems biology approach

et al. 2012

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Lactic acid-producing bacteria survive in distinct environments, but show common metabolic characteristics. Here we studied the dynamic interactions of the central metabolism in Lactococcus lactis, extensively used as a starter culture in the dairy industry, and Streptococcus pyogenes, a human pathogen. Glucose-pulse experiments and enzymatic measurements were performed to parameterize kinetic models of glycolysis. Significant improvements were made to existing kinetic models for L. lactis, which subsequently accelerated the development of the first kinetic model of S. pyogenes glycolysis. The models revealed an important role for extracellular phosphate in the regulation of central metabolism and the efficient use of glucose. Thus, phosphate, which is rarely taken into account as an independent species in models of central metabolism, should be considered more thoroughly in the analysis of metabolic systems in the future. Insufficient phosphate supply can lead to a strong inhibition of glycolysis at high glucose concentrations in both species, but this was more severe in S. pyogenes. S. pyogenes is more efficient at converting glucose to ATP, showing a higher tendency towards heterofermentative energy metabolism than L. lactis. Our comparative systems biology approach revealed that the glycolysis of L. lactis and S. pyogenes have similar characteristics, but are adapted to their individual natural habitats with respect to phosphate regulation. DatabaseThe mathematical models described here have been submitted to the Online Cellular Systems Modelling Database and can be accessed at http://jjj.biochem.sun.ac.za/database/Levering/ index.html free of charge.Abbreviations 2-PGA, 2-phosphoglycerate; 3-PGA, 3-phosphoglycerate; Fru(1,6)P 2, fructose 1,6-bisphosphate; GA3P, glyceraldehyde 3-phosphate; GAPDH, glyceraldehyde-3-phosphate dehydrogenase; GAPN, non-phosphorylating NADP + -dependent glyceraldehyde-3-phosphate dehydrogenase;Glc6P, glucose 6-phosphate; HPr, a low-molecular-weight, heat-stable protein, part of PTS; HPr-ser-P, serine-phosphorylated HPr; LDH, L-lactate dehydrogenase; NTP, nucleoside triphosphate; PaseII, HPr(ser-P)-activated sugar-phosphate phosphatase II; P i, unbound inorganic phosphate; PTS, phosphotransferase system; triose-P, GA3P and dihydroxyacetone.

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Purification of pyruvate formate-lyase from Streptococcus mutans and its regulatory properties

Cited by 95 publications

References 19 publications

Citrate metabolism in lactic acid bacteria

Citrate metabolism in lactic acid bacteria

Responses of lactic acid bacteria to oxygen

Role of phosphate in the central metabolism of two lactic acid bacteria – a comparative systems biology approach

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