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The Bacillus subtilis Gne (GneA, GalE) protein can catalyse UDP-glucose as well as UDP-N-acetylglucosamine 4-epimerisation.
Mutations in the Bacillus subtilis gene that affect the activity of the uridine diphosphate (UDP)-N-acetylglucosamine (GlcNAc) 4-epimerase (EC 22.214.171.124) were shown to map to galE, the structural gene of the UDP-glucose (Glc) 4-epimerase (EC 126.96.36.199). 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.
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
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