The Bacillus subtilis Gne (GneA, GalE) protein can catalyse UDP-glucose as well as UDP-N-acetylglucosamine 4-epimerisation.

Details

Serval ID
serval:BIB_29636
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
The Bacillus subtilis Gne (GneA, GalE) protein can catalyse UDP-glucose as well as UDP-N-acetylglucosamine 4-epimerisation.
Journal
Gene
Author(s)
Soldo B., Scotti C., Karamata D., Lazarevic V.
ISSN
0378-1119[print], 0378-1119[linking]
Publication state
Published
Issued date
2003
Volume
319
Pages
65-69
Language
english
Abstract
Mutations in the Bacillus subtilis gene that affect the activity of the uridine diphosphate (UDP)-N-acetylglucosamine (GlcNAc) 4-epimerase (EC 5.1.3.7) were shown to map to galE, the structural gene of the UDP-glucose (Glc) 4-epimerase (EC 5.1.3.2). This genetic evidence that the same enzyme can catalyse the epimerisation of hexoses as well as of their N-acetylated forms is confirmed by in vitro assays with purified enzyme. It appears that in B. subtilis, Gne (GneA, GalE) is involved in two distinct and essential functions, i.e., cell detoxification under certain growth conditions and the biosynthesis of anionic cell wall polymers. We discuss the evidence that such enzymes capable of utilizing both UDP-hexoses and UDP-N-acetylhexosamines are present in other organisms.
Keywords
Acetylglucosamine/metabolism, Bacillus subtilis/enzymology, Bacillus subtilis/genetics, Bacterial Proteins/genetics, Bacterial Proteins/metabolism, Base Sequence, Catalysis, Escherichia coli/genetics, Histidine/genetics, Mutation, Recombinant Fusion Proteins/genetics, Recombinant Fusion Proteins/isolation & purification, UDPglucose 4-Epimerase/genetics, UDPglucose 4-Epimerase/metabolism, Uridine Diphosphate/metabolism, Uridine Diphosphate Glucose/metabolism
Pubmed
Web of science
Create date
19/11/2007 12:27
Last modification date
20/08/2019 13:09
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