The Transport/Phosphorylation ofN,N′-Diacetylchitobiose in Escherichia coli
Open Access
- 1 October 2000
- journal article
- Published by Elsevier
- Vol. 275 (42) , 33102-33109
- https://doi.org/10.1074/jbc.m001045200
Abstract
No abstract availableKeywords
This publication has 22 references indexed in Scilit:
- The Chitin Disaccharide,N,N′-Diacetylchitobiose, Is Catabolized byEscherichia coli and Is Transported/Phosphorylated by the Phosphoenolpyruvate:Glycose Phosphotransferase SystemJournal of Biological Chemistry, 2000
- Analytical Sedimentation of the IIAChb and IIBChb Proteins of the Escherichia coli N,N′-Diacetylchitobiose Phosphotransferase SystemPublished by Elsevier ,2000
- Isolation and Characterization of IIAChb, a Soluble Protein of the Enzyme II Complex Required for the Transport/Phosphorylation ofN,N′-Diacetylchitobiose in Escherichia coliPublished by Elsevier ,2000
- Glucose Transporter of Escherichia coli: NMR Characterization of the Phosphocysteine Form of the IIBGlc Domain and Its Binding Interface with the IIAGlc SubunitBiochemistry, 1997
- The structure of an energy-coupling protein from bacteria, IIBcellobiose, reveals similarity to eukaryotic protein tyrosine phosphatasesStructure, 1997
- Expression, Purification and Characterization of the Enzyme II Mannitol‐Specific Domain from Staphylococcus carnosus and Determination of the Active‐Site Cysteine ResidueEuropean Journal of Biochemistry, 1995
- Crystallization of Enzyme IIB of the Cellobiose-specific Phosphotransferase System of Escherichia coliJournal of Molecular Biology, 1994
- Enzyme IIB bcellobiose of the phosphoenol‐pyruvate‐dependent phosphotransferase system of Escherichia coli: Backbone assignment and secondary structure determined by three‐dimensional NMR spectroscopyProtein Science, 1994
- Enzyme IIMtl of the Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system: identification of the activity-linked cysteine on the mannitol carrierBiochemistry, 1988
- Acid and base catalysis in a non-enzymic transfer reaction A possible enzyme modelBiochimica et Biophysica Acta, 1957