Abstract
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.
Highlights
Saccharomyces cerevisiae and Kluveromycetes lactis have several common features in galactose metabolism
The above studies may be applied to Human Gal10p, where it can help in gaining useful insight into Galactosemia disease
Gal10p is an UDP-Glucose 4-epimerase enzyme which participates in Leloir pathway of D- Galactose metabolism
Summary
Saccharomyces cerevisiae and Kluveromycetes lactis have several common features in galactose metabolism. Galactose can be taken by the cells by different permeation systems regulated by three enzymatic reactions which are essential for the metabolism of galactose as shown in Supplementary material [3,4]. It splits in to mutarotase and UDP galactose 4-epimerase activities [5]. Crystal structure analysis has revealed that the galactose 4-epimerase domain, encoded by the N-terminus domain of the protein, is separated from the C-terminal mutarotase domain by a simple Type II turn [6]. Loss of Gal10p activity prevents cell growth when galactose is the sole carbon source [7]. The Saccharomyces cerevisiae epimerase encoded by the GAL10 gene is about twice the size of either the bacterial or human protein but has nearly similar size as Gal10p of K.lactis [5]
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
