PMID:11350937
| Citation |
Gutknecht, R, Beutler, R, Garcia-Alles, LF, Baumann, U and Erni, B (2001) The dihydroxyacetone kinase of Escherichia coli utilizes a phosphoprotein instead of ATP as phosphoryl donor. EMBO J. 20:2480-6 |
|---|---|
| Abstract |
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. |
| Links |
PubMed PMC125457 Online version:10.1093/emboj/20.10.2480 |
| Keywords |
Adenosine Triphosphate/metabolism; Amino Acid Sequence; Binding Sites; Escherichia coli/enzymology; Genes, Bacterial; Molecular Sequence Data; Mutagenesis; Operon; Phosphates/metabolism; Phosphoproteins/metabolism; Phosphorylation; Phosphotransferases/metabolism; Phosphotransferases (Alcohol Group Acceptor)/biosynthesis; Phosphotransferases (Alcohol Group Acceptor)/chemistry; Phosphotransferases (Alcohol Group Acceptor)/genetics; Phosphotransferases (Alcohol Group Acceptor)/metabolism; Protein Structure, Secondary; Sequence Homology, Amino Acid |
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