For Libraries For Publication Open Access Downloads About Us Contact Us
Paper Titles
Effects of Low-Voltage Pulsed Magnetic Field and Pouring Temperature on Solidified Structure of Al-4.5%Cu Alloy
p.2139
First-Principles Study on Structure and Stability of YAP Crystal
p.2144
Scttering of SH-Waves by Interface Semicircular Debonded Cylindrical Lining and Linear Cracks Originating at Edge of Lining
p.2149
Mechanical Properties of Carbon Cathodes during Aluminium Electrolysis
p.2155
Prediction of the Tertiary Structure of α-Glycosidase from Aspergillus niger by Homology Modeling
p.2160
Critical Life Prediction of Ship-Borne Helicopter Metallic Dynamic Components Based on Corrosion Damage
p.2164
Fractals and Catastrophe Analysis of Fatigue Crack Propagation for Sample by Plastic Deformation
p.2169
The Cycle Measurement of Sulfur Blank Value with the CS-444 Infrared Ray Carbon Sulfur Analyzer
p.2173
Study on Surface Stress Measurement of Laser Cladding Fe-Based Alloy Coating Based on Rayleigh Wave Signal Analysis
p.2177

Prediction of the Tertiary Structure of α-Glycosidase from Aspergillus niger by Homology Modeling

Article Preview

Abstract:

α-Glucosidases play critical role both in primary metabolism and in glycoconjugate biosynthesis and processing. In this paper, the reasonable three-dimensional molecular model of AglA was generated by homology modeling. This modeled protein is divided into five major structural domains, and the catalytic domain is classical (β/α) 8 barrel with the active site pocket positioned at its C-terminal side. With analyses of conserved residues and overlay of homology structures, the residues Tyr 662, Tyr527, Glu521, His238 and Tyr235 was predicted as the main substrate binding sites, and residues Asp490, Glu493 and Asp660 were deduced to be the acid/base catalytic residues.

You might also be interested in these eBooks
New Materials, Applications and Processes View Preview

Info:

Periodical:

Advanced Materials Research (Volumes 399-401)

Pages:

2160-2163

DOI:

https://doi.org/10.4028/www.scientific.net/AMR.399-401.2160

Citation:

Cite this paper

Online since:

November 2011

Authors:

Fa Xiang Wang, Qin Yun Wang, Yong Le Liu, Jian Yu

Keywords:

Active Site, Aspergillus niger, Homology Modeling, Tertiary Structure, α-Glucosidase

Export:

RIS, BibTeX

Price:

Permissions CCC:

Request Permissions

Permissions PLS:

Request Permissions

Сopyright:

© 2012 Trans Tech Publications Ltd. All Rights Reserved

Share:

Citation:

References

[1] B. Henrissat: Biochem. J. Vol. 280 (1991), p.309

Google Scholar

[2] B. Henrissat and A. Bairoch: Biochem. J. Vol. 316 (1996), p.695

Google Scholar

[3] A. L. Lovering, S. S. Lee, Y.W. Kim, S. G. Withers and N. C. J. Strynadka: J. Biol. Chem. Vol. 280 (2005), p.2105

Google Scholar

[4] K. Watanabe, Y. Hata, H. Kizaki, Y. Katsube and Y. Suzuki: J. Mol. Biol. Vol. 269 (1997), p.142

Google Scholar

[5] H.A. Ernst, L.L. Leggio, M. Willemoe, G. Leonard, P. Blum and S. Larsen: J. Mol. Biol. Vol. 358 (2006), p.1106

Google Scholar

[6] S. Lyann, Q.C. Roberto, E.S. Erwin, L.N. Buford and R.R. David: J. Mol. Biol. Vol. 375 (2008), p.782

Google Scholar

[7] A. Sali and T.L. Blundell: J. Mol. Biol. Vol. 234(1993), p.779

Google Scholar

[8] K.Arnold, L. Bordoli, J. Kopp and T. Schwede: Bioinformatics Vol.22 (2006), p.195

Google Scholar

[9] R.A. Laskowski, M.W. MacArthur, D.S. Moss and J.M. Thornton: J. App. Cryst. Vol.26 (1993), p.283

Google Scholar

[10] Wiederstein and M.J. Sippl: Nucleic Acids Res. Vol. 35 (2007), p.W407

Google Scholar

[11] S. Lyann, Q.C. Roberto, E.S. Erwin, L.N. Buford and R.R. David: J. Mol. Biol. Vol. 375 (2008), p.782

Google Scholar

[11] J. Dundas, Z. Ouyang, J. Tseng, A. Binkowski, Y. Turpaz and J. Liang: Nucleic Acid Res. Vol.34 (2006), p.W116

DOI: 10.1093/nar/gkl282

Google Scholar

© 2025 Trans Tech Publications Ltd. All rights are reserved, including those for text and data mining, AI training, and similar technologies. For open access content, terms of the Creative Commons licensing CC-BY are applied.
Scientific.Net is a registered trademark of Trans Tech Publications Ltd.