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

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

Show Affiliations

1. Department of Biochemistry, Tarbiat Modares University, Tehran, Iran
2. Department of Biology, University of Zanjan, Zanjan, Iran
3. Department of Clinical Biochemistry, School of Medicine, Tehran University of Medical Sciences, Tehran, Iran
4. Department of Biophysics, Tarbiat Modares University, Tehran, Iran

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.

Related Docs

View other Related Docs

1. Unfolding of Chondroitinase Abc Ι Is Dependent on Thermodynamic Driving Force by Kinetically Rate Constant-Amplitude Compensation: A Stopped-Flow Fluorescence Study, Enzyme and Microbial Technology (2016)

2. Chondroitinase As a Therapeutic Enzyme: Prospects and Challenges, Enzyme and Microbial Technology (2024)

3. Establishment of Aromatic Pairs at the Surface of Chondroitinase Abc I: The Effect on Activity and Stability, Applied Biochemistry and Biotechnology (2018)

4. Role of His-His Interaction in Ser474-His475-Tyr476 Sequence of Chondroitinase Abc I in the Enzyme Activity and Stability, International Journal of Biological Macromolecules (2018)

5. Improvement of Activity and Stability of Chondroitinase Abc I by Introducing an Aromatic Cluster at the Surface of Protein, Enzyme and Microbial Technology (2017)

6. Optimization of Conformational Stability and Catalytic Efficiency in Chondroitinase Abc Ι by Protein Engineering Methods, Engineering in Life Sciences (2016)

7. Investigating the Role of Loop 131–140 in Activity and Thermal Stability of Chondroitinase Abc I, International Journal of Biological Macromolecules (2018)

8. Rigidifying Flexible Sites: An Approach to Improve Stability of Chondroitinase Abc I, International Journal of Biological Macromolecules (2017)

Experts (# of related papers)

View all Related Experts

Abolfazl Golestani (12)

Massoud Amanlou (2)

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 -

Science Communicator Platform

Authors

Authors Affiliations

Abstract