NDLI: Functional insight for beta-glucuronidase in Escherichia coli and Staphylococcus sp. RLH1.

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Functional insight for beta-glucuronidase in Escherichia coli and Staphylococcus sp. RLH1.

Content Provider	Europe PMC
Author	Arul, Loganathan Benita, George Balasubramanian, Ponnusamy
Copyright Year	2007
Abstract	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 novelβ-glucuronidase (gusA) derived from Staphylococcus sp. RLH1 for E. coli uidA. It is known to have a ten fold higher sensitivity compared toE. coli β-glucuronidase. The functional superiority of Staphylococcus (gusA) over E. coli (uidA) activity is not fully known. The comparison ofsecondary structural elements among them revealed an increased percentage of random coils in Staphylococcus β-glucuronidase. The 3D model of gusAshows catalytic site residues 396Glu, 508Glu and 471Tyr of gusA in loop regions. Accessible surface area (ASA) calculations on the 3D model showedincreased 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 thesolvent. This hypothesizes the enhanced catalytic activity of β-glucuronidase in Staphylococcus sp. RLH1 compared to that in E. coli.
Journal	Bioinformation
Volume Number	2
PubMed Central reference number	PMC2478733
Issue Number	8
PubMed reference number	18685721
e-ISSN	09732063
DOI	10.6026/97320630002339
Language	English
Publisher	Biomedical Informatics Publishing Group
Publisher Date	2008-05-22
Access Restriction	Open
Rights 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. © 2008 Biomedical Informatics Publishing Group
Subject Keyword	β-glucuronidase structure-function relationships uidA GUSPlus catalytic activity
Content Type	Text
Resource Type	Article
Subject	Agricultural and Biological Sciences

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