The dihydroxyacetone kinase of Escherichia coli utilizes a phosphoprotein instead of ATP as phosphoryl donor

Autor:	Ulrich Baumann, Rudolf Beutler, Bernhard Erni, Regula Gutknecht, Luis F. Garcia-Alles
Přispěvatelé:	University of Bern
Rok vydání:	2001
Předmět:	[SDV.BIO]Life Sciences [q-bio]/Biotechnology MESH: Sequence Homology Amino Acid MESH: Protein Structure Secondary Mannose MESH: Phosphotransferases MESH: Amino Acid Sequence medicine.disease_cause Protein Structure Secondary chemistry.chemical_compound Adenosine Triphosphate MESH: Adenosine Triphosphate Protein phosphorylation Phosphorylation MESH: Mutagenesis 0303 health sciences MESH: Escherichia coli General Neuroscience PEP group translocation 3. Good health Phosphotransferases (Alcohol Group Acceptor) Biochemistry MESH: Phosphates MESH: Genes Bacterial Phosphoenolpyruvate carboxykinase MESH: Operon Protein subunit Molecular Sequence Data Dihydroxyacetone macromolecular substances Biology MESH: Phosphoproteins Article General Biochemistry Genetics and Molecular Biology Phosphates 03 medical and health sciences Operon Escherichia coli medicine [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology Amino Acid Sequence Molecular Biology 030304 developmental biology MESH: Molecular Sequence Data Binding Sites MESH: Phosphorylation Sequence Homology Amino Acid General Immunology and Microbiology 030306 microbiology Phosphotransferases Phosphoproteins MESH: Phosphotransferases (Alcohol Group Acceptor) MESH: Binding Sites chemistry Genes Bacterial Mutagenesis Phosphoprotein bacteria
Zdroj:	EMBO Journal EMBO Journal, EMBO Press, 2001, 20 (10), pp.2480-2486. ⟨10.1093/emboj/20.10.2480⟩
ISSN:	1460-2075 0261-4189
DOI:	10.1093/emboj/20.10.2480
Popis:	International audience; 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.
Databáze:	OpenAIRE
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