Direct Mg2+ Binding Activates Adenylate Kinase from Escherichia coli
نویسندگان
چکیده
منابع مشابه
Circular dichroism investigation of Escherichia coli adenylate kinase.
We examined by circular dichroism (CD) spectroscopy in far- and near-ultraviolet three different molecular forms of Escherichia coli adenylate kinase: the wild type protein, the enzyme carboxymethylated at a single cysteine residue (Cys-77), and the thermosensitive adenylate kinase. The thermosensitive enzyme differs from the wild type protein in that a serine is substituted for a proline resid...
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Polyphosphate kinase (PPK), responsible for the processive synthesis of inorganic polyphosphate (polyP) from ATP in Escherichia coli, can transfer in reverse the terminal phosphate residue of polyP to ADP to yield ATP. PolyP also serves as a donor in a polyP:AMP phosphotransferase (PAP) activity observed in extracts of Acinetobacter johnsonii and Myxococcus xanthus. We have found that overexpre...
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Introduction : The innate immune system as the first line of defense against the pathogens recognizes pathogen-associated molecular patterns (PAMPs) by Toll-Like Receptors (TLRs). Interaction of bacterial PAMPs by TLRs results in activation of innate and acquired immunity. FimH adhesin, a minor component of type 1 fimbriae encoded by Uropathogenic Escherichia coli (UPEC) is a PAMP of TLR4 tha...
متن کاملMembrane potential, adenylate levels and Mg2+ are interconnected via adenylate kinase equilibrium in plant cells.
Concentrations of adenylate species and free magnesium (Mg(2+)) within cells are mediated by the equilibrium governed by adenylate kinase (AK), the enzyme abundant in plants in chloroplast stroma and intermembrane spaces of chloroplasts and mitochondria. Ratios of free and Mg-bound adenylates (linked to the values of [Mg(2+)] established under AK equilibrium) can be rationalized in terms of the...
متن کاملNucleoside diphosphate kinase from Escherichia coli.
Nucleoside diphosphate (NDP) kinase from Escherichia coli was purified to homogeneity and was crystallized. Gel filtration analysis of the purified enzyme indicated that it forms a tetramer. The enzyme was phosphorylated with [gamma-32P]ATP, and the pH stability profile of the phosphoenzyme indicated that two different amino acid residues were phosphorylated. Both a histidine residue and serine...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2009
ISSN: 0021-9258
DOI: 10.1074/jbc.m803658200