Abstract
The phosphoenolpyruvate:sugar phosphotransferase system of bacteria plays an important role in the concomitant uptake and phosphorylation of numerous sugars. The first protein in the pathway of phosphotransfer of the phosphoenolpyruvate:sugar phosphotransferase system is Enzyme I. It has been shown that a stable N-terminal domain can be produced by treatment of the purified protein with various proteolytic enzymes. We show here that the region from glutamate-252 to leucine-264 is accessible to proteolysis resulting in N-terminal cores ranging from M(r) 27521 to 28799.
MeSH terms
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Amino Acid Sequence
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Chymotrypsin / metabolism
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Escherichia coli / enzymology*
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Mass Spectrometry
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Models, Molecular
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Molecular Sequence Data
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Peptide Fragments / chemistry*
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Phosphoenolpyruvate Sugar Phosphotransferase System / chemistry*
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Phosphoenolpyruvate Sugar Phosphotransferase System / metabolism
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Phosphotransferases (Nitrogenous Group Acceptor) / chemistry*
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Phosphotransferases (Nitrogenous Group Acceptor) / metabolism
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Protein Conformation
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Sequence Analysis
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Serine Endopeptidases / metabolism
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Trypsin / metabolism
Substances
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Peptide Fragments
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Phosphoenolpyruvate Sugar Phosphotransferase System
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Phosphotransferases (Nitrogenous Group Acceptor)
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phosphoenolpyruvate-protein phosphotransferase
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Serine Endopeptidases
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Chymotrypsin
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glutamyl endopeptidase
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Trypsin