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BioMed Research International
Volume 2014, Article ID 934351, 14 pages
http://dx.doi.org/10.1155/2014/934351
Research Article

Molecular Cloning and Biochemical Characterization of a Recombinant Sterol 3-O-Glucosyltransferase from Gymnema sylvestre R.Br. Catalyzing Biosynthesis of Steryl Glucosides

1Metabolic and Structural Biology Department, CSIR-Central Institute of Medicinal and Aromatic Plants (CSIR-CIMAP), P.O. CIMAP, Lucknow, Uttar Pradesh 226015, India
2Centre of Innovative and Applied Bioprocessing, (A National Institute under Department of Biotechnology Gov. of India) C-127, Phase-8, Industrial Area, S.A.S. Nagar, Mohali, Punjab 160071, India
3Department of Biotechnology, Uttar Pradesh Technical University, Lucknow, Uttar Pradesh 226021, India

Received 26 February 2014; Revised 9 June 2014; Accepted 23 June 2014; Published 27 August 2014

Academic Editor: Dinesh A. Nagegowda

Copyright © 2014 Pragya Tiwari et al. 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.

Supplementary Material

Supplementary Figure 1: Deduced disorderliness state of the protein, secondary structures and presence of transmembrance helices in the GsSGT protein.

Supplementary Figure 2: Analysis of the nucleotide (UDPG) binding PSPG conserved domain in G. sylvestre UDP: sterol glucosyltransferase. The HCGWNS motif within the PSPG box is essential for enzymatic activity and found to be 100% conserved in the protein sequence of GsSGT.

Supplementary Figure 3: Pie chart representation of the percentage of each amino acid present in secondary structure of GsSGT protein.

Supplementary Figure 4: Protein secondary structure analysis showing 28.48% alpha helix, 20.00% extended strands and 51.52% random coil.

  1. Supplementary Figures