The Guanylyl Cyclase Core of an Atrial Natriuretic Peptide Receptor: Enzymatic Properties and Basis for Cooperativity
The enzymatic properties of a cloned atrial natriuretic peptide receptor are described. The renatured catalytic core had maximal activity with Mn2+, and all nucleoside triphosphates inhibited the enzyme competitively. The catalytic specificity of the enzyme was tested directly. The cyclase reaction...
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Veröffentlicht in: | Biochemical and biophysical research communications 1996-01, Vol.218 (3), p.670-673 |
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creator | Thorpe, David S. Niu, Shi Morkin, Eugene |
description | The enzymatic properties of a cloned atrial natriuretic peptide receptor are described. The renatured catalytic core had maximal activity with Mn2+, and all nucleoside triphosphates inhibited the enzyme competitively. The catalytic specificity of the enzyme was tested directly. The cyclase reaction was specific for guanine, producing cGMP and cyclic deoxyGMP. Surprisingly, deoxyguanylyl cyclase kinetics were classical, unlike the positive cooperativity seen for guanylyl cyclase activity, suggesting that the 2′ hydroxyl group of GTP is necessary for the allosteric mechanism. |
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The renatured catalytic core had maximal activity with Mn2+, and all nucleoside triphosphates inhibited the enzyme competitively. The catalytic specificity of the enzyme was tested directly. The cyclase reaction was specific for guanine, producing cGMP and cyclic deoxyGMP. 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subjects | Allosteric Regulation Cations, Divalent Deoxyribonucleotides - chemistry Deoxyribonucleotides - metabolism Guanosine Triphosphate - metabolism Guanylate Cyclase - antagonists & inhibitors Guanylate Cyclase - chemistry Guanylate Cyclase - metabolism Kinetics Nucleotides - chemistry Nucleotides - metabolism Receptors, Atrial Natriuretic Factor - chemistry Recombinant Proteins Signal Transduction Substrate Specificity |
title | The Guanylyl Cyclase Core of an Atrial Natriuretic Peptide Receptor: Enzymatic Properties and Basis for Cooperativity |
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