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The dihydroxyacetone kinase of Escherichia coli utilizes a phosphoprotein instead of ATP as phosphoryl donor
Author(s) -
Gutknecht Regula,
Beutler Rudolf,
GarciaAlles Luis F.,
Baumann Ulrich,
Erni Bernhard
Publication year - 2001
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/20.10.2480
Subject(s) - pep group translocation , biology , biochemistry , dihydroxyacetone , escherichia coli , phosphorylation , kinase , phosphoprotein , transferase , groes , enzyme , phosphoenolpyruvate carboxykinase , gene , groel , glycerol
The dihydroxyacetone kinase (DhaK) of Escherichia coli consists of three soluble protein subunits. DhaK (YcgT; 39.5 kDa) and DhaL (YcgS; 22.6 kDa) are similar to the N‐ and C‐terminal halves of the ATP‐dependent DhaK ubiquitous in bacteria, animals and plants. The homodimeric DhaM (YcgC; 51.6 kDa) consists of three domains. The N‐terminal dimerization domain has the same fold as the IIA domain (PDB code 1PDO) of the mannose transporter of the bacterial phosphoenolpyruvate:sugar phosphotransferase system (PTS). The middle domain is similar to HPr and the C‐terminus is similar to the N‐terminal domain of enzyme I (EI) of the PTS. DhaM is phosphorylated three times by phosphoenolpyruvate in an EI‐ and HPr‐dependent reaction. DhaK and DhaL are not phosphorylated. The IIA domain of DhaM, instead of ATP, is the phosphoryl donor to dihydroxyacetone (Dha). Unlike the carbohydrate‐specific transporters of the PTS, DhaK, DhaL and DhaM have no transport activity.