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| The EMBO Journal
(2001) 20, 2480–2486, doi:10.1093/emboj/20.10.2480 |
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| The dihydroxyacetone kinase of Escherichia coli utilizes a phosphoprotein instead of ATP as phosphoryl donor |
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| Regula Gutknecht, Rudolf Beutler, Luis F. Garcia-Alles, Ulrich Baumann and Bernhard Erni |
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Departement für Chemie und Biochemie, Universität Bern, Freiestrasse 3, CH-3012 Bern, Switzerland To whom correspondence should be addressed Bernhard Erni, erni@ibc.unibe.ch Received 18 December 2000; Revised 20 March 2001; Accepted 22 March 2001. |
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| Abstract |
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| 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. |
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| Keywords: dihydroxyacetone kinase, phosphohistidine, protein phosphorylation, PTS |
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