The adenine nucleotide binding site on yeast hexokinase PII. Affinity labeling of Lys-111 by pyridoxal 5‘-diphospho-5‘-adenosine.
نویسندگان
چکیده
منابع مشابه
Affinity labeling of nucleotide-binding sites on kinases and dehydrogenases by pyridoxal 5'-diphospho-5'-adenosine.
A new adenine nucleotide analog, [3H]pyridoxal 5'-diphospho-5'-adenosine (PLP-AMP), has been synthesized. The effectiveness of PLP-AMP as an affinity probe has been tested using a number of nucleotide-binding enzymes. In comparison to reaction with pyridoxal 5'-phosphate, PLP-AMP binds more tightly and exhibits greater specificity of labeling for most enzymes tested. PLP-AMP is a very potent in...
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We have labeled the nucleoside triphosphate-binding domain of Escherichia coli rho factor with the ATP affinity analog [3H]pyridoxal 5'-diphospho-5'-adenosine (PLP-AMP). PLP-AMP completely inactivates the RNA-dependent ATPase activity of rho upon incorporation of 3 mol of reagent/mol of hexameric rho protein. Although the potency of PLP-AMP is enhanced when an RNA substrate such as poly(C) is p...
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We have labeled the adenosine triphosphate binding site of Escherichia coli DNA gyrase with the ATP affinity analog, [3H]pyridoxal 5’-diphospho-5’-adenosine (PLP-AMP). PLP-AMP strongly inhibits the ATPase and DNA supercoiling activities of DNA gyrase, with 50% inhibition occurring at 7.5 pM inhibitor. ATP and ADP compete with PLP-AMP for binding and protect the enzyme against inhibition. The la...
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A new adenosine analogue adenosine 5'-(2-bromoethyl)-phosphate has been synthesized. The reactive moiety, a bromoalkyl group, has the ability to react with the nucleophilic side chains of several amino acids. This compound reacts with NAD-dependent isocitrate dehydrogenase from pig heart, causing inactivation. Addition of the allosteric regulator ADP to the reaction mixture protects the enzyme ...
متن کاملAffinity labeling of the adenosine 5'-monophosphate binding site of rabbit muscle glycogen phosphorylase b with an adenosine 5'-monophosphate-cobalt(3) complex.
A new affinity labeling method is presented which may be used for enzyme-catalyzing reactions in the presence of magnesium. This method uses the substrate-cobalt(III) analog of the substrate-magnesium complex as a covalent label of the active site. The specific case of rabbit muscle glycogen phosphorylase b, which has been covalently labeled with a AMP-Co(II1) derivative at the allosteric site,...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1988
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)68583-7