| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH |
|
|
|
|||||||
|
|||||||||
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Papers In Press, published online ahead of print July 25, 2000
J. Biol. Chem, 10.1074/jbc.M001045200
Submitted on February 8, 2000
Accepted on July 25, 2000
Department of Biology, Johns Hopkins University, Baltimore, MD 21218
Corresponding Author: roseman{at}jhu.edu
Enzyme II permeases of the phosphoenolpyruvate:glycose phosphotransferase system (PTS) comprise one to five separately encoded polypeptides, but most contain similar domains (IIA, IIB, IIC). The phosphoryl group is transferred from one domain to another, with histidine as the phosphoryl acceptor in IIA and cysteine the acceptor in certain IIB domains. IIBChb is a phosphocarrier in the uptake/phosphorylation of the chitin disaccharide, (GlcNAc)2 , by Escherichia coli, and is unusual because it is separately encoded and soluble. Both the crystal and solution structures of a IIBChb mutant (Cys10Ser) have been reported. In the present studies, homogeneous phospho-IIBrChb was isolated, and the phosphoryl-Cys linkage established by 31P-NMR spectroscopy. Rate constants for the hydrolysis of phospho-IIBChb plotted versus pH gave the same shape peak reported for the model compound, butyl thiophosphate, but was shifted about 4 pH units. Evidence is presented for a stable complex between homogeneous Cys10SerIIBChb (which cannot be phosphorylated) and phospho-IIAChb, but not with IIAChb. The complex (a tetramer (Keyhani et al, J. Biol. Chem., accompanying manuscript)) contains equimolar quantities of the two proteins, and has been chemically cross-linked. It appears to be an analogue of the transition state complex in the reaction: phospho-IIAChb + IIBChb {double arrows} IIAChb + phospho-IIBChb. This is apparently the first report of the isolation of a transition state analogue in a protein-protein phosphotransfer reaction.
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
 |
|
  X. Li, L.-X. Wang, X. Wang, and S. Roseman The Chitin Catabolic Cascade in the Marine Bacterium Vibrio Cholerae: Characterization of a Unique Chitin Oligosaccharide Deacetylase Glycobiology, December 1, 2007; 17(12): 1377 - 1387. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 N. O. Keyhani, X.-B. Li, and S. Roseman Chitin Catabolism in the Marine Bacterium Vibrio furnissii. IDENTIFICATION AND MOLECULAR CLONING OF A CHITOPORIN J. Biol. Chem., October 13, 2000; 275(42): 33068 - 33076. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
J. K. Park, N. O. Keyhani, and S. Roseman Chitin Catabolism in the Marine Bacterium Vibrio furnissii. IDENTIFICATION, MOLECULAR CLONING, AND CHARACTERIZATION OF A N,N'-DIACETYLCHITOBIOSE PHOSPHORYLASE J. Biol. Chem., October 13, 2000; 275(42): 33077 - 33083. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
N. O. Keyhani, L.-X. Wang, Y. C. Lee, and S. Roseman The Chitin Disaccharide, N,N'-Diacetylchitobiose, Is Catabolized by Escherichia coli and Is Transported/Phosphorylated by the Phosphoenolpyruvate:Glycose Phosphotransferase System J. Biol. Chem., October 13, 2000; 275(42): 33084 - 33090. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
N. O. Keyhani, O. Boudker, and S. Roseman Isolation and Characterization of IIAChb, a Soluble Protein of the Enzyme II Complex Required for the Transport/Phosphorylation of N,N'-Diacetylchitobiose in Escherichia coli J. Biol. Chem., October 13, 2000; 275(42): 33091 - 33101. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
N. Keyhani, M. E. Rodgers, B. Demeler, J. C. Hansen, and S. Roseman Analytical Sedimentation of the IIAChb and IIBChb Proteins of the Escherichia coli N,N'-Diacetylchitobiose Phosphotransferase System. DEMONSTRATION OF A MODEL PHOSPHOTRANSFER TRANSITION STATE COMPLEX J. Biol. Chem., October 13, 2000; 275(42): 33110 - 33115. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |
