s-phosphocysteine and phosphohistidine

s-phosphocysteine has been researched along with phosphohistidine* in 1 studies

Other Studies

1 other study(ies) available for s-phosphocysteine and phosphohistidine

Article	Year
S-phosphocysteine and phosphohistidine are intermediates in the phosphoenolpyruvate-dependent mannitol transport catalyzed by Escherichia coli EIIMtl. Biochemistry, 1988, Aug-09, Volume: 27, Issue:16 During a cycle of mannitol transport and phosphorylation, the phosphoryl group originating on P-enolpyruvate is transferred, consecutively, to two sites on the Escherichia coli mannitol-specific carrier (EIIMtl) before being placed on mannitol [Pas et al. (1988) Biochemistry (in press)]. The peptides constituting the two EIIMtl phosphorylation sites have been isolated and identified after labeling with [32P]-P-enolpyruvate. The first site is localized in peptide Leu 541-Lys 560. The hydrolysis characteristics of the phosphorylated peptide indicate that a histidine residue is phosphorylated. The second site is located in peptide Ile 380-Met 393, which contains the activity-linked cysteine (384) [Pas & Robillard (1988) Biochemistry (in press)]. The hydrolysis characteristics of the phosphopeptide indicate that Cys 384 is the site of phosphorylation. Topics: Binding Sites; Biological Transport, Active; Cysteine; Escherichia coli; Escherichia coli Proteins; Histidine; Mannitol; Monosaccharide Transport Proteins; Phosphoenolpyruvate; Phosphoenolpyruvate Sugar Phosphotransferase System; Phosphorylation	1988

Article

Year

S-phosphocysteine and phosphohistidine are intermediates in the phosphoenolpyruvate-dependent mannitol transport catalyzed by Escherichia coli EIIMtl.

Biochemistry, 1988, Aug-09, Volume: 27, Issue:16

During a cycle of mannitol transport and phosphorylation, the phosphoryl group originating on P-enolpyruvate is transferred, consecutively, to two sites on the Escherichia coli mannitol-specific carrier (EIIMtl) before being placed on mannitol [Pas et al. (1988) Biochemistry (in press)]. The peptides constituting the two EIIMtl phosphorylation sites have been isolated and identified after labeling with [32P]-P-enolpyruvate. The first site is localized in peptide Leu 541-Lys 560. The hydrolysis characteristics of the phosphorylated peptide indicate that a histidine residue is phosphorylated. The second site is located in peptide Ile 380-Met 393, which contains the activity-linked cysteine (384) [Pas & Robillard (1988) Biochemistry (in press)]. The hydrolysis characteristics of the phosphopeptide indicate that Cys 384 is the site of phosphorylation.

Topics: Binding Sites; Biological Transport, Active; Cysteine; Escherichia coli; Escherichia coli Proteins; Histidine; Mannitol; Monosaccharide Transport Proteins; Phosphoenolpyruvate; Phosphoenolpyruvate Sugar Phosphotransferase System; Phosphorylation

1988