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Int. J. Mol. Sci. 2009, 10(6), 2849-2859; doi:10.3390/ijms10062849
Article

Inactivation and Unfolding of the Hyperthermophilic Inorganic Pyrophosphatase from Thermus thermophilus by Sodium Dodecyl Sulfate

1,2, 3, 2, 2,* , 2,*  and 1,*
Received: 19 May 2009; in revised form: 31 May 2009 / Accepted: 17 June 2009 / Published: 23 June 2009
(This article belongs to the Section Biochemistry, Molecular Biology and Biophysics)
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Abstract: Inorganic pyrophosphatase (PPase, EC 3.6.1.1) is an essential constitutive enzyme for energy metabolism and clearance of excess pyrophosphate. In this research, we investigated the sodium dodecyl sulfate (SDS)-induced inactivation and unfolding of PPase from Thermus thermophilus (T-PPase), a hyperthermophilic enzyme. The results indicated that like many other mesophilic enzymes, T-PPase could be fully inactivated at a low SDS concentration of 2 mM. Using an enzyme activity assay, SDS was shown to act as a mixed type reversible inhibitor, suggesting T-PPase contained specific SDS binding sites. At high SDS concentrations, T-PPase was denatured via a two-state process without the accumulation of any intermediate, as revealed by far-UV CD and intrinsic fluorescence. A comparison of the inactivation and unfolding data suggested that the inhibition might be caused by the specific binding of the SDS molecules to the enzyme, while the unfolding might be caused by the cooperative non-specific binding of SDS to T-PPase. The possible molecular mechanisms underlying the mixed type inhibition by SDS was proposed to be caused by the local conformational changes or altered charge distributions.
Keywords: hyperthermophilic enzyme; inactivation; inorganic pyrophosphatase; mixed type reversible inhibition; protein folding; sodium dodecyl sulfate; Thermus thermophilus hyperthermophilic enzyme; inactivation; inorganic pyrophosphatase; mixed type reversible inhibition; protein folding; sodium dodecyl sulfate; Thermus thermophilus
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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MDPI and ACS Style

Mu, H.; Zhou, S.-M.; Xia, Y.; Zou, H.; Meng, F.; Yan, Y.-B. Inactivation and Unfolding of the Hyperthermophilic Inorganic Pyrophosphatase from Thermus thermophilus by Sodium Dodecyl Sulfate. Int. J. Mol. Sci. 2009, 10, 2849-2859.

AMA Style

Mu H, Zhou S-M, Xia Y, Zou H, Meng F, Yan Y-B. Inactivation and Unfolding of the Hyperthermophilic Inorganic Pyrophosphatase from Thermus thermophilus by Sodium Dodecyl Sulfate. International Journal of Molecular Sciences. 2009; 10(6):2849-2859.

Chicago/Turabian Style

Mu, Hang; Zhou, Sheng-Mei; Xia, Yong; Zou, Hechang; Meng, Fanguo; Yan, Yong-Bin. 2009. "Inactivation and Unfolding of the Hyperthermophilic Inorganic Pyrophosphatase from Thermus thermophilus by Sodium Dodecyl Sulfate." Int. J. Mol. Sci. 10, no. 6: 2849-2859.



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