Moraxella catarrhalis Lgt2, a galactosyltransferase with broad acceptor substrate specificity

No Thumbnail Available
File version
Author(s)
Faglin, Isabelle
Wilson, Jennifer C
Tiralongo, Joe
Peak, Ian R
Griffith University Author(s)
Primary Supervisor
Other Supervisors
Editor(s)
Date
2010
Size
File type(s)
Location
License
Abstract

The genetic basis of lipo-oligosaccharide (LOS) biosynthesis for the bacterium Moraxella catarrhalis has been elucidated and functions suggested for each of the glycosyltransferases. In this study we have expressed and characterised one of these enzymes, the putative galactosyltransferase Lgt2B/C. The lgt2B/C gene was amplified from M. catarrhalis, expressed in Escherichia coli, and Lgt2B/C was purified. Analysis of its glycosyltransferase catalytic activity ascertained the pH and temperature optima. The donor specificity and acceptor specificity were examined and they showed that Lgt2B/C is a galactosyltransferase with relatively broad acceptor specificity with optimal activity in the presence of exogenous Mg2+.

Journal Title

Carbohydrate Research

Conference Title
Book Title
Edition
Volume

345

Issue

15

Thesis Type
Degree Program
School
Publisher link
Patent number
Funder(s)
Grant identifier(s)
Rights Statement
Rights Statement
Item Access Status
Note
Access the data
Related item(s)
Subject

Medicinal and biomolecular chemistry

Organic chemistry

Organic chemistry not elsewhere classified

Biochemistry and cell biology

Persistent link to this record
Citation
Collections