Critical Role of a Loop at C-Terminal Domain on the Conformational Stability and Catalytic Efficiency of Chondroitinase Abc I

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Critical Role of a Loop at C-Terminal Domain on the Conformational Stability and Catalytic Efficiency of Chondroitinase Abc I Publisher Pubmed

Shirdel SA¹ ; Khalifeh K² ; Golestani A³ ; Ranjbar B⁴ ; Khajeh K¹

Source: Molecular Biotechnology Published:2015

Abstract

We used a combination of protein engineering and spectroscopic methods to investigate the effect of a long length loop on the conformational stability and activity of chondroitinase ABC I. This study involves manipulation of interactions around Asp689 as a key residue in the central region of the loop containing residues 681–695 located at C-terminal domain of the enzyme. According to the equilibrium unfolding experiments and considering thermodynamic m value and ΔG(H2O), we found that the folded state of H700N, L701T, and H700N/L701T are more compact relative to the folded state of wild-type protein and they become stabilized upon mutation. However, the compactness and stability of other variants are less than those of wild-type protein. According to enzyme activity measurements, we found that the catalytic efficiency of structurally stabilized variants is decreased, while that of destabilized mutants is improved. © 2015, Springer Science+Business Media New York.

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Style	Citing Format
MLA	Shirdel SA, et al.. "Critical Role of a Loop at C-Terminal Domain on the Conformational Stability and Catalytic Efficiency of Chondroitinase Abc I." Molecular Biotechnology, vol. 57, no. 8, 2015, pp. 727-734.
APA	Shirdel SA, Khalifeh K, Golestani A, Ranjbar B, Khajeh K (2015). Critical Role of a Loop at C-Terminal Domain on the Conformational Stability and Catalytic Efficiency of Chondroitinase Abc I. Molecular Biotechnology, 57(8), 727-734.
Chicago	Shirdel SA, Khalifeh K, Golestani A, Ranjbar B, Khajeh K. "Critical Role of a Loop at C-Terminal Domain on the Conformational Stability and Catalytic Efficiency of Chondroitinase Abc I." Molecular Biotechnology 57, no. 8 (2015): 727-734.
Harvard	Shirdel SA et al. (2015) 'Critical Role of a Loop at C-Terminal Domain on the Conformational Stability and Catalytic Efficiency of Chondroitinase Abc I', Molecular Biotechnology, 57(8), pp. 727-734.
Vancouver	Shirdel SA, Khalifeh K, Golestani A, Ranjbar B, Khajeh K. Critical Role of a Loop at C-Terminal Domain on the Conformational Stability and Catalytic Efficiency of Chondroitinase Abc I. Molecular Biotechnology. 2015;57(8):727-734.
BibTex	@article{ author = {Shirdel SA and Khalifeh K and Golestani A and Ranjbar B and Khajeh K}, title = {Critical Role of a Loop at C-Terminal Domain on the Conformational Stability and Catalytic Efficiency of Chondroitinase Abc I}, journal = {Molecular Biotechnology}, volume = {57}, number = {8}, pages = {727-734}, year = {2015} }
RIS	TY - JOUR AU - Shirdel SA AU - Khalifeh K AU - Golestani A AU - Ranjbar B AU - Khajeh K TI - Critical Role of a Loop at C-Terminal Domain on the Conformational Stability and Catalytic Efficiency of Chondroitinase Abc I JO - Molecular Biotechnology VL - 57 IS - 8 SP - 727 EP - 734 PY - 2015 ER -

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