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Identification of the sequence motif of glycoside hydrolase 13 family members
A bioinformatics analysis of sequences of enzymes of the glycoside hydrolase (GH) 13 family members such as α-amylase, cyclodextrin glycosyltransferase (CGTase), branching enzyme and cyclomaltodextrinase has been carried out in order to find out the sequence motifs that govern the reactions specific...
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Formato: | Texto |
Lenguaje: | English |
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Biomedical Informatics
2011
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3082856/ https://www.ncbi.nlm.nih.gov/pubmed/21544166 |
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author | Kumar, Vikash |
author_facet | Kumar, Vikash |
author_sort | Kumar, Vikash |
collection | PubMed |
description | A bioinformatics analysis of sequences of enzymes of the glycoside hydrolase (GH) 13 family members such as α-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 α -amylase sequence motif have low sequence conservation than rest of the motifs of the GH13 family members. |
format | Text |
id | pubmed-3082856 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | Biomedical Informatics |
record_format | MEDLINE/PubMed |
spelling | pubmed-30828562011-05-04 Identification of the sequence motif of glycoside hydrolase 13 family members Kumar, Vikash Bioinformation Hypothesis A bioinformatics analysis of sequences of enzymes of the glycoside hydrolase (GH) 13 family members such as α-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 α -amylase sequence motif have low sequence conservation than rest of the motifs of the GH13 family members. Biomedical Informatics 2011-03-26 /pmc/articles/PMC3082856/ /pubmed/21544166 Text en © 2011 Biomedical Informatics 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. |
spellingShingle | Hypothesis Kumar, Vikash Identification of the sequence motif of glycoside hydrolase 13 family members |
title | Identification of the sequence motif of glycoside hydrolase 13 family members |
title_full | Identification of the sequence motif of glycoside hydrolase 13 family members |
title_fullStr | Identification of the sequence motif of glycoside hydrolase 13 family members |
title_full_unstemmed | Identification of the sequence motif of glycoside hydrolase 13 family members |
title_short | Identification of the sequence motif of glycoside hydrolase 13 family members |
title_sort | identification of the sequence motif of glycoside hydrolase 13 family members |
topic | Hypothesis |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3082856/ https://www.ncbi.nlm.nih.gov/pubmed/21544166 |
work_keys_str_mv | AT kumarvikash identificationofthesequencemotifofglycosidehydrolase13familymembers |