Cargando…
Functional insight for β-glucuronidase in Escherichia coli and Staphylococcus sp. RLH1
Glycosyl hydrolases hydrolyze the glycosidic bond either in carbohydrates or between carbohydrate and non-carbohydrate moiety. The β-glucuronidase (beta D-glucuronoside glucuronosohydrolase; EC 3.2.1.31) enzyme belongs to the family-2 glycosyl hydrolase. The E. coli borne β-glucuronidase gene (uidA)...
Autores principales: | , , |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
Biomedical Informatics Publishing Group
2008
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2478733/ https://www.ncbi.nlm.nih.gov/pubmed/18685721 |
_version_ | 1782157625073336320 |
---|---|
author | Arul, Loganathan Benita, George Balasubramanian, Ponnusamy |
author_facet | Arul, Loganathan Benita, George Balasubramanian, Ponnusamy |
author_sort | Arul, Loganathan |
collection | PubMed |
description | Glycosyl hydrolases hydrolyze the glycosidic bond either in carbohydrates or between carbohydrate and non-carbohydrate moiety. The β-glucuronidase (beta D-glucuronoside glucuronosohydrolase; EC 3.2.1.31) enzyme belongs to the family-2 glycosyl hydrolase. The E. coli borne β-glucuronidase gene (uidA) was devised as a gene fusion marker in plant genetic transformation experiments. Recent plant transformation vectors contain a novel β-glucuronidase (gusA) derived from Staphylococcus sp. RLH1 for E. coli uidA. It is known to have a ten fold higher sensitivity compared to E. coli β-glucuronidase. The functional superiority of Staphylococcus (gusA) over E. coli (uidA) activity is not fully known. The comparison of secondary structural elements among them revealed an increased percentage of random coils in Staphylococcus β-glucuronidase. The 3D model of gusA shows catalytic site residues 396Glu, 508Glu and 471Tyr of gusA in loop regions. Accessible surface area (ASA) calculations on the 3D model showed increased ASA for active site residues in Staphylococcus β-glucuronidase. Increased random coil, the presence of catalytic residues in loops, greater solvent accessibility of active residues and increased charged residues in gusA of Staphylococcus might facilitate interaction with the solvent. This hypothesizes the enhanced catalytic activity of β-glucuronidase in Staphylococcus sp. RLH1 compared to that in E. coli. |
format | Text |
id | pubmed-2478733 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2008 |
publisher | Biomedical Informatics Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-24787332008-08-06 Functional insight for β-glucuronidase in Escherichia coli and Staphylococcus sp. RLH1 Arul, Loganathan Benita, George Balasubramanian, Ponnusamy Bioinformation Hypothesis Glycosyl hydrolases hydrolyze the glycosidic bond either in carbohydrates or between carbohydrate and non-carbohydrate moiety. The β-glucuronidase (beta D-glucuronoside glucuronosohydrolase; EC 3.2.1.31) enzyme belongs to the family-2 glycosyl hydrolase. The E. coli borne β-glucuronidase gene (uidA) was devised as a gene fusion marker in plant genetic transformation experiments. Recent plant transformation vectors contain a novel β-glucuronidase (gusA) derived from Staphylococcus sp. RLH1 for E. coli uidA. It is known to have a ten fold higher sensitivity compared to E. coli β-glucuronidase. The functional superiority of Staphylococcus (gusA) over E. coli (uidA) activity is not fully known. The comparison of secondary structural elements among them revealed an increased percentage of random coils in Staphylococcus β-glucuronidase. The 3D model of gusA shows catalytic site residues 396Glu, 508Glu and 471Tyr of gusA in loop regions. Accessible surface area (ASA) calculations on the 3D model showed increased ASA for active site residues in Staphylococcus β-glucuronidase. Increased random coil, the presence of catalytic residues in loops, greater solvent accessibility of active residues and increased charged residues in gusA of Staphylococcus might facilitate interaction with the solvent. This hypothesizes the enhanced catalytic activity of β-glucuronidase in Staphylococcus sp. RLH1 compared to that in E. coli. Biomedical Informatics Publishing Group 2008-05-22 /pmc/articles/PMC2478733/ /pubmed/18685721 Text en © 2008 Biomedical Informatics Publishing Group 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 Arul, Loganathan Benita, George Balasubramanian, Ponnusamy Functional insight for β-glucuronidase in Escherichia coli and Staphylococcus sp. RLH1 |
title | Functional insight for β-glucuronidase in Escherichia coli and Staphylococcus sp. RLH1 |
title_full | Functional insight for β-glucuronidase in Escherichia coli and Staphylococcus sp. RLH1 |
title_fullStr | Functional insight for β-glucuronidase in Escherichia coli and Staphylococcus sp. RLH1 |
title_full_unstemmed | Functional insight for β-glucuronidase in Escherichia coli and Staphylococcus sp. RLH1 |
title_short | Functional insight for β-glucuronidase in Escherichia coli and Staphylococcus sp. RLH1 |
title_sort | functional insight for β-glucuronidase in escherichia coli and staphylococcus sp. rlh1 |
topic | Hypothesis |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2478733/ https://www.ncbi.nlm.nih.gov/pubmed/18685721 |
work_keys_str_mv | AT arulloganathan functionalinsightforbglucuronidaseinescherichiacoliandstaphylococcussprlh1 AT benitageorge functionalinsightforbglucuronidaseinescherichiacoliandstaphylococcussprlh1 AT balasubramanianponnusamy functionalinsightforbglucuronidaseinescherichiacoliandstaphylococcussprlh1 |