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Title

Identification of the sequence motif of glycoside hydrolase 13 family members 

Authors

Vikash Kumar*

Affiliation

Department of Biosciences and Bioengineering, Indian Institute of Technology Bombay, Powai, Mumbai 400076, India
 

Email

kvikash01@rediffmail.com; *Corresponding author

Article Type

Hypothesis

 

Date

Received December 17, 2010; Accepted February 07, 2011; Published March 26, 2011

 

Abstract

A bioinformatics analysis of sequences of enzymes of the glycoside hydrolase (GH) 13 family members such as a-amylase, cyclodextrin glycosyltransferase (CGTase), branching enzyme and cyclomaltodextrinase has been carried out in order to find out the sequence motifs that govern the reactions specificities of these enzymes by using hidden Markov model (HMM) profile. This analysis suggests the existence of such sequence motifs and residues of these motifs constituting the 1 to +3 catalytic subsites of the enzyme. Hence, by introducing mutations in the residues of these four subsites, one can change the reaction specificities of the enzymes. In general it has been observed that a -amylase sequence motif have low sequence conservation than rest of the motifs of the GH13 family members.
 

Keywords

a-Amylases; Glycoside hydrolase family 13; Sequence motif; Reaction specificity; Substrate specificity; HMM profile.

 

Citation

Kumar. Bioinformation 6(2): 61-63 (2011)

Edited by

P Kangueane

 

ISSN

0973-2063

 

Publisher

Biomedical Informatics

 

Copyright

Publisher

 

Copyright Transfer Agreement

The authors of published articles in Bioinformation automatically transfer the copyright to the publisher upon formal acceptance. However, the authors reserve right to use the information contained in the article for non commercial purposes.

 

License

This is an open-access article, which permits unrestricted use, distribution, and reproduction in any medium, for non-commercial purposes, provided the original author and source are credited.