Phosphoenolpyruvate:carbohydrate phosphotransferase system of bacteria.

Postma, Pieter W.; Lengeler, Joseph W.

doi:10.1128/mmbr.49.3.232-269.1985

Cited by 303 publications

(187 citation statements)

References 256 publications

(539 reference statements)

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“…7C). Both sets of thermodynamic magnitudes resulted in a free energy curve which had a maximum, as it was expected from Eqn (14). The fitting to this curve yielded a value of m DC pi of 117 ± 2 calAEmol )1 AEK )1 AEM )1 , which agreed, within the error, with that determined from the variation of m DH i with the temperature.…”

Section: Heat-denaturationsupporting

confidence: 69%

“…The straight line through the data is a linear least square fit of the data to Eqn (13), whose slope is m DCpi and it has a value of 115 ± 4 calAEmol )1 AEK )1 AEM )1 . (C) Temperature dependence of m. The solid line through the data is a least square fit of the data to Eqn (14). The fitting yield a m DCpi equals to 117 ± 2 calAEmol )1 AEK )1 AEM )1 .…”

Section: Heat-denaturationmentioning

confidence: 98%

“…where m(T) ¼ 0). Equation 14 indicates that the protein-urea interactions are temperature-dependent. The temperature dependencies of the free energy, DG¢, the enthalpy, DH¢, and the entropy, DS¢, at any urea concentrations are given by equations identical to Eqns (7, 5 and 6), respectively.…”

Section: Data Analysesmentioning

confidence: 99%

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The conformational stability of theStreptomyces coelicolorhistidine‐phosphocarrier protein

Neira

Gómez

2004

European Journal of Biochemistry

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Thermodynamic parameters describing the conformational stability of the histidine-containing phosphocarrier protein from Streptomyces coelicolor, scHPr, have been determined by steady-state fluorescence measurements of isothermal urea-denaturations, differential scanning calorimetry at different guanidinium hydrochloride concentrations and, independently, by far-UV circular dichroism measurements of isothermal urea-denaturations, and thermal denaturations at fixed urea concentrations. The equilibrium unfolding transitions are described adequately by the two-state model and they validate the linear free-energy extrapolation model, over the large temperature range explored, and the urea concentrations used. At moderate urea concentrations (from 2 to 3 M), scHPr undergoes both high-and lowtemperature unfolding. The free-energy stability curves have been obtained for the whole temperature range and values of the thermodynamic parameters governing the heat-and cold-denaturation processes have been obtained. Colddenaturation of the protein is the result of the combination of an unusually high heat capacity change (1.4 ± 0.3 kcalAEmol )1 AEK )1 , at 0 M urea, being the average of the fluorescence, circular dichroism and differential scanning calorimetry measurements) and a fairly low enthalpy change upon unfolding at the midpoint temperature of heat-denaturation (59 ± 4 kcalAEmol )1 , the average of the fluorescence, circular dichroism and differential scanning calorimetry measurements). The changes in enthalpy (m DH i ), entropy (m DS i ) and heat capacity (m DC pi ), which occur upon preferential urea binding to the unfolded state vs. the folded state of the protein, have also been determined. The m DH i and the m DS i are negative at low temperatures, but as the temperature is increased, m DH i makes a less favourable contribution than m DS i to the change in free energy upon urea binding. The m DC pi is larger than those observed for other proteins; however, its contribution to the global heat capacity change upon unfolding is small.Keywords: calorimetry; denaturant-binding interactions; histidine-phosphocarrier; protein stability.A full understanding of the physical interactions underlying the structure, folding and the function of a protein requires a detailed description of its conformational stability in terms of the free energy of unfolding. Such a thermodynamic description relies on the quantitative analysis of denaturant-induced or thermally induced folding-unfolding transitions, measured either spectroscopically or calorimetrically. In both cases, data analyses involves the extrapolation of the thermodynamic parameters to standard conditions, usually 298 K in the absence of denaturant. To extrapolate thermal denaturation data, the change in DC p , and its temperature dependence must be known [1,2]. The extrapolation of data from chemical-denaturation [with either urea or guanidinium hydrochloride (Gdm Cl) as denaturants] is carried out using either the linear free energy model, LEM [3][4][5], or the binding...

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Section: Heat-denaturationsupporting

confidence: 69%

Section: Heat-denaturationmentioning

confidence: 98%

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The conformational stability of theStreptomyces coelicolorhistidine‐phosphocarrier protein

Neira

Gómez

2004

European Journal of Biochemistry

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“…This could not be of any help in competing for the acquisition of nutrients, if we assume that the exclusive role of these transport systems is to permit the entry of hydrophylic substrates into the cell. It is known, however, that the PTS has regulatory functions and participates in the control of sugar utilization [2]. Recent resuits indicate that the constitutive mannose PTS of oral streptococci that also transports glucose is involved in those control mechanisms [5].…”

Section: Discussionmentioning

confidence: 99%

“…In S. mutans, many sugars are transported by the phosphoenolpyruvate (PEP)-sugar phosphotransferase system (PTS). The PTS consists of a number of soluble (HPr and El) and membrane-bound enzymes (Enzyme II and Enzyme III), which catalyse concomitantly the transport and the phosphorylation of an incoming sugar (see [2] for review). The presence of more than one PTS for a specific sugar has been reported in S. mutans for sucrose [3], fructose [4] and glucose [5].…”

Section: Introductionmentioning

confidence: 99%

Evidence for the presence of two distinct phosphoenolpyruvate: Mannose phosphotransferase systems in Streptococcus mutans GS5-2

Néron

1987

FEMS Microbiology Letters

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We have isolated a spontaneous 2-deoxyglucose (2DG) resistant mutant from Streptococcus mutans GS5-2, called GM500, that grew as well as the parental strain on mannose. Membranes of glucose-grown cells of the mutant strain were, however, unable to catalyse the phosphoenolpyruvate-dependent phosphorylation of mannose in the presence of purified enzyme I (El) and hydroxyproline (HPr) unlike the wild-type cells. Resting cells of strain GM500 were also unable to transport mannose after growth at the expense of glucose, whereas glucose-grown cells of strain GS5-2 transported and metabolized mannose at a high rate. These activities were recovered in the mutant strain after growth on mannose. Our resuits indicate the presence of 2 phosphoenolpyru-

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The genus Lactococcus

Kim

2014

Lactic Acid Bacteria

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Phosphoenolpyruvate:carbohydrate phosphotransferase system of bacteria.

Cited by 303 publications

References 256 publications

The conformational stability of theStreptomyces coelicolorhistidine‐phosphocarrier protein

The conformational stability of theStreptomyces coelicolorhistidine‐phosphocarrier protein

Evidence for the presence of two distinct phosphoenolpyruvate: Mannose phosphotransferase systems in Streptococcus mutans GS5-2

The genus Lactococcus

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