Title

Authors

Ashwani Sharma¹ & Pushkar Malakar^{1, *}

Affiliation

¹Department of Bioscience & Bioengineering, Indian Institute of Technology, Bombay, Powai, Mumbai-400076, Maharashtra, India 

Email

pushkarbt@iitb.ac.in

+91-22-25764215

Article Type

Prediction model

Date

Received May 27, 2010; Accepted October 20, 2010; Published November 27, 2010
 

The Gal10p (UDP-Galactose 4-epimerase) protein is known for regulation of D-galactose metabolism. It catalyzes the inter-conversion between UDPgalactose and UDP-glucose. Knowledge of protein structure, neighboring interacting partners as well as functional residues of the Gal10p is crucial for carry out its function. These problems are still uncovered in case of the Epimerase enzyme. Structure of Epimerase enzyme has already been determined in S.cerevisiae and E.coli, however, no structural information for this protein is available for K.lactis. We used the homology modeling approach to model the structure of Gal10p in K.lactis. Furthermore, functional residues were predicted for modeled Gal10 protein and the strength of interaction between Gal10p and other Gal proteins was carried out by protein –protein interaction studies. The interaction studies revealed that the affinity of Gal10p for other Gal proteins vary in different organisms. Sequence and structure comparison of Epimerase enzyme showed that the orthologs in K.lactis and S.cervisiae are more similar to each other as compared to the ortholog in E.coli .The studies carried by us will help in better understanding of the galactose metabolism. The above studies may be applied to Human Gal10p, where it can help in gaining useful insight into Galactosemia disease. 

Keywords

GAL protein, Gal10p, D-galactose metabolism, functional site prediction servers, RMSD, protein-protein interaction.

Citation

Malakar & Sharma. Bioinformation, 5(6): 266-270, 2010

Edited by

P. Kangueane

ISSN

0973-2063

Publisher

Biomedical Informatics

License

This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.