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

Biochemistry. 1988 Aug 9;27(16):5835-9. doi: 10.1021/bi00416a002.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding Sites
  • Biological Transport, Active
  • Cysteine / analogs & derivatives
  • Cysteine / metabolism
  • Escherichia coli / metabolism
  • Escherichia coli Proteins
  • Histidine / analogs & derivatives
  • Histidine / metabolism
  • Mannitol / metabolism*
  • Monosaccharide Transport Proteins
  • Phosphoenolpyruvate / metabolism
  • Phosphoenolpyruvate Sugar Phosphotransferase System / metabolism*
  • Phosphorylation

Substances

  • Escherichia coli Proteins
  • Monosaccharide Transport Proteins
  • S-phosphocysteine
  • Mannitol
  • Histidine
  • Phosphoenolpyruvate
  • Phosphoenolpyruvate Sugar Phosphotransferase System
  • mannitol PTS permease, E coli
  • Cysteine
  • phosphohistidine