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DNA-Tethered RNA Polymerase for Programmable In vitro Transcription and Molecular Computation

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Published on: December 29, 2021

A processive carbohydrate polymerase that mediates bifunctional catalysis using a single active site.

John F May¹, Matthew R Levengood, Rebecca A Splain

¹Department of Biochemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706-1544, United States.

|January 6, 2012

Summary

This summary is machine-generated.

Glycosyltransferases can synthesize complex carbohydrate polymers with specific sequences. Bifunctional enzymes like GlfT2 use a single active site to create multiple glycosidic linkages, revealing enzyme versatility.

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Area of Science:

Biochemistry
Glycobiology
Enzymology

Background:

Glycosyltransferases typically form one type of glycosidic linkage per enzyme.
Some glycosyltransferases are bifunctional, creating polysaccharides with multiple linkage types.
The active site configuration of bifunctional glycosyltransferases remains unclear.

Purpose of the Study:

To investigate the active site mechanism of the bifunctional galactosyltransferase GlfT2.
To determine if GlfT2 utilizes one or two active sites for dual regioselectivity.
To understand how bifunctional glycosyltransferases generate complex polysaccharide sequences.

Main Methods:

Enzyme characterization of GlfT2.
Structural modeling of related bifunctional glycosyltransferases (hyaluronan synthase, cellulose synthase).

Main Results:

GlfT2 mediates mycobacterial galactan polymerization using a single active site.
This active site exhibits dual regioselectivity, forming alternating linkages.
Structural modeling suggests similar single-active-site mechanisms for hyaluronan and cellulose synthases.

Conclusions:

Bifunctional glycosyltransferases can possess a single active site with dual catalytic activity.
This single active site mechanism enables the synthesis of specific, complex polysaccharide sequences.
A single active site generating multiple glycosidic bonds is a hallmark of processive carbohydrate polymer elongation.