Cargando…

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...

Descripción completa

Detalles Bibliográficos
Autor principal: Kumar, Vikash
Formato: Texto
Lenguaje:English
Publicado: Biomedical Informatics 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3082856/
https://www.ncbi.nlm.nih.gov/pubmed/21544166
_version_ 1782202340463345664
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