Thermodynamic analysis of the nondenaturational conformational change of baker’s yeast phosphoglycerate kinase at 24°C

Ijeoma, Opral; Hollowell, Heather; Bodnar, Melissa A.; Britt, B. Mark

doi:10.1016/j.abb.2008.07.005

Cited by 4 publications

(3 citation statements)

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“…An exothermic transition at ~32˚C is observed. We have previously observed such transitions in other enzymes where we demonstrated, via the construction of protein stability curves, that this signal may be indicative of a global, nondenaturational conformational change [2]- [6]. When scans are made at the conventional scan rate of 1.0 K•min −1 no such signal is observed.…”

Section: Resultsmentioning

confidence: 77%

“…Our laboratory's current emphasis is in detecting and characterizing nondenaturational enzyme conformational changes. We have previously detected conformational changes that occur at moderate temperatures in several enzymes using slow-scan-rate differential scanning calorimetry (ssrDSC) [2]- [6]. For each enzyme studied we detected evidence for a non-unfolding change in the enzyme between the temperature where the enzyme crystal was formed for X-ray structure determination and the optimal physiological temperature of the organism from which the enzyme is isolated.…”

Section: Introductionmentioning

confidence: 99%

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Volume Change of the Random Coil to Folded Conformational Transition of Thermomyces lanuginosus Xylanase at 24&#176C and pH = 7.0 via Application of the Clausius-Clapeyron Equation

Wilks¹,

Arrington²,

Britt³

2014

JBPC

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A partial phase diagram characterizing the conformational change that occurs in Thermomyces lanuginosus xylanase as it is slowly heated in 150 mM sodium phosphate (pH = 7.0) has been constructed from slow-scan-rate differential scanning calorimetry measurements. The Clausius-Clapeyron equation was applied to determine an associated volume change of −205 L•mol −1 at 24˚C, the equilibrium transition temperature at 1.0 atm pressure. This value is in excellent agreement with that predicted using a previously published [1] empirical equation for calculating the hydrodynamic radius if the transition is regarded as from a random coil to a functional, folded state and with the assumption that the hydrodynamic radius is a good approximation of the true random coil radius. The existence of a low-temperature random coil is confirmed by circular dichroism and dynamic light scattering measurements. Thus, at 24˚C and 1.0 atm pressure the enzyme appears to fold from a random coil to a functional, folded form as it is slowly heated.

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Section: Resultsmentioning

confidence: 77%

Section: Introductionmentioning

confidence: 99%

Volume Change of the Random Coil to Folded Conformational Transition of Thermomyces lanuginosus Xylanase at 24&#176C and pH = 7.0 via Application of the Clausius-Clapeyron Equation

Wilks¹,

Arrington²,

Britt³

2014

JBPC

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“…Tetramers have been reported in rare cases as in Sulfolobus solfataricus [26] and Trypanosoma [21]. C. glutamicum PGK His showed higher temperature stability than monomeric PGKs, e.g., 40°C for Mus musculus [27] and 24°C for S. cervisiae [28]. Possibly, dimerization of PGK from C. glutamicum contributes to the stability of the protein by favoring hydrophobic interactions via the subunit contacts and by reducing the surface area exposed to the solvent in a similar manner as reported for dimeric PGKs [29].…”

Section: Discussionmentioning

confidence: 99%

Characterization of 3-phosphoglycerate kinase from Corynebacterium glutamicum and its impact on amino acid production

Reddy

Wendisch

2014

BMC Microbiology

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BackgroundCorynebacterium glutamicum cg1790/pgk encodes an enzyme active as a 3-phosphoglycerate kinase (PGK) (EC 2.7.2.3) catalyzing phosphoryl transfer from 1,3-biphosphoglycerate (bPG) to ADP to yield 3-phosphoglycerate (3-PG) and ATP in substrate chain phosphorylation.ResultsC. glutamicum 3-phosphoglycerate kinase was purified to homogeneity from the soluble fraction of recombinant E. coli. PGKHis was found to be active as a homodimer with molecular weight of 104 kDa. The enzyme preferred conditions of pH 7.0 to 7.4 and required Mg2+ for its activity. PGKHis is thermo labile and it has shown maximal activity at 50–65°C. The maximal activity of PGKHis was estimated to be 220 and 150 U mg-1 with KM values of 0.26 and 0.11 mM for 3-phosphoglycerate and ATP, respectively. A 3-phosphoglycerate kinase negative C. glutamicum strain ∆pgk was constructed and shown to lack the ability to grow under glycolytic or gluconeogenic conditions unless PGK was expressed from a plasmid to restore growth. When pgk was overexpressed in L-arginine and L-ornithine production strains the production increased by 8% and by 17.5%, respectively.ConclusionUnlike many bacterial PGKs, C. glutamicum PGK is active as a homodimer. PGK is essential for growth of C. glutamicum with carbon sources requiring glycolysis and gluconeogenesis. Competitive inhibition by ADP reveals the critical role of PGK in gluconeogenesis by energy charge. Pgk overexpression improved the productivity in L-arginine and L-ornithine production strains.

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Current awareness on yeast

2009

Yeast

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In order to keep subscribers up‐to‐date with the latest developments in their field, this current awareness service is provided by John Wiley & Sons and contains newly‐published material on yeasts. Each bibliography is divided into 10 sections. 1 Reviews; 2 General; 3 Biochemistry; 4 Biotechnology; 5 Cell Biology; 6 Gene Expression; 7 Genetics; 8 Physiology; 9 Medical Mycology; 10 Recombinant DNA Technology. Within each section, articles are listed in alphabetical order with respect to author. If, in the preceding period, no publications are located relevant to any one of these headings, that section will be omitted. (7 weeks journals ‐ search completed 11th. Feb. 2009)

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Thermodynamic analysis of the nondenaturational conformational change of baker’s yeast phosphoglycerate kinase at 24°C

Cited by 4 publications

References 16 publications

Volume Change of the Random Coil to Folded Conformational Transition of <i>Thermomyces</i> <i>lanuginosus</i> Xylanase at 24&#176C and pH = 7.0 via Application of the Clausius-Clapeyron Equation

Volume Change of the Random Coil to Folded Conformational Transition of <i>Thermomyces</i> <i>lanuginosus</i> Xylanase at 24&#176C and pH = 7.0 via Application of the Clausius-Clapeyron Equation

Characterization of 3-phosphoglycerate kinase from Corynebacterium glutamicum and its impact on amino acid production

Current awareness on yeast

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Thermodynamic analysis of the nondenaturational conformational change of baker’s yeast phosphoglycerate kinase at 24°C

Cited by 4 publications

References 16 publications

Volume Change of the Random Coil to Folded Conformational Transition of &lt;i&gt;Thermomyces&lt;/i&gt; &lt;i&gt;lanuginosus&lt;/i&gt; Xylanase at 24&amp;#176C and pH = 7.0 via Application of the Clausius-Clapeyron Equation

Volume Change of the Random Coil to Folded Conformational Transition of &lt;i&gt;Thermomyces&lt;/i&gt; &lt;i&gt;lanuginosus&lt;/i&gt; Xylanase at 24&amp;#176C and pH = 7.0 via Application of the Clausius-Clapeyron Equation

Characterization of 3-phosphoglycerate kinase from Corynebacterium glutamicum and its impact on amino acid production

Current awareness on yeast

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Volume Change of the Random Coil to Folded Conformational Transition of <i>Thermomyces</i> <i>lanuginosus</i> Xylanase at 24&#176C and pH = 7.0 via Application of the Clausius-Clapeyron Equation

Volume Change of the Random Coil to Folded Conformational Transition of <i>Thermomyces</i> <i>lanuginosus</i> Xylanase at 24&#176C and pH = 7.0 via Application of the Clausius-Clapeyron Equation