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S-phosphocysteine and phosphohistidine are intermediates in the phosphoenolpyruvate-dependent mannitol transport catalyzed by Escherichia coli EII/sup Mtl/

Journal Article · · Biochemistry; (United States)
OSTI ID:7002727

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 (EII/sup Mtl/) before being placed on mannitol. The peptides constituting the two EII/sup Mtl/ phosphorylation sites have been isolated and identified after labeling with (/sup 32/P)-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). The hydrolysis characteristics of the phosphopeptide indicate that Cys 384 is the site of phosphorylation.

Research Organization:
Univ. of Groningen (Netherlands)
OSTI ID:
7002727
Journal Information:
Biochemistry; (United States), Journal Name: Biochemistry; (United States) Vol. 27:16; ISSN BICHA
Country of Publication:
United States
Language:
English