The Bacillus subtilis Gne (GneA, GalE) protein can catalyse UDP-glucose as well as UDP-N-acetylglucosamine 4-epimerisation
| Autor: | Claudio Scotti, Vladimir Lazarevic, Dimitri Karamata, Blazenka Soldo |
|---|---|
| Rok vydání: | 2003 |
| Předmět: |
Uridine Diphosphate Glucose
Recombinant Fusion Proteins Bacillus subtilis Catalysis Uridine Diphosphate Acetylglucosamine UDPglucose 4-Epimerase chemistry.chemical_compound Bacterial Proteins Biosynthesis Escherichia coli Genetics Histidine chemistry.chemical_classification Base Sequence biology Structural gene General Medicine biology.organism_classification carbohydrates (lipids) Uridine diphosphate Enzyme Biochemistry chemistry Mutation Uridine diphosphate glucose |
| Zdroj: | Gene. 319:65-69 |
| ISSN: | 0378-1119 |
| DOI: | 10.1016/s0378-1119(03)00793-5 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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