Structural and catalytic characteristics of Escherichia coli adenylate kinase.
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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Catalytic and allosteric properties of the normal and of a genetically altered glycerol kinase from Escherichia coli were examined. Normal glycerol kinase exhibited Michaelis-Menten kinetics for glycerol with an apparent K, of 10 PM. Gel filtration studies indicated that, at saturation, 3.7 moles of [Wlglycerol bound per mole of enzyme, and a dissociation constant of 10 pM was determined by ult...
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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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All known nucleoside monophosphate kinases contain an invariant sequence Asp-Gly-Phe(Tyr)-Pro-Arg. In order to understand better the structural and functional role of individual amino acid residues belonging to the above sequence, three mutants of Escherichia coli adenylate kinase (D84H, G85V, and F86L) were produced by site-directed mutagenesis. Circular dichroism spectra revealed that the sec...
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Adenylate kinase, the product of the adk locus in Escherichia coli K12, catalyzes the conversion of AMP and ATP to two molecules of ADP. The gene has been cloned by complementation of an adk temperature sensitive mutation. The DNA sequence of the complete coding region and of 5'- and 3'-untranslated regions were determined. The resulting protein sequence was found to contain several regions of ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1987
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)75829-3