{'fraction_non_alphanumeric': 0.020850040096230954, 'fraction_numerical': 0.0048115477145148355, 'mean_word_length': 5.466321243523316, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
Nucleotide regulation of soluble guanylate cyclase (1013.14)

The interaction of the enzyme soluble guanylate cyclase (sGC) with nitric oxide (NO) mediates numerous physiological and pathological processes. NO production regulates smooth muscle relaxation, myocardial function, perfusion and platelet aggregation. NO signaling engages the second messenger cyclic guanosine monophosphate (cGMP) synthesized by sGC. Due to the critical importance of cGMP in many cellular processes, sGC activity is tightly regulated by NO, ATP and GTP. The mechanistic details of sGC regulation by these molecules are not well understood. Nucleotides influence sGC activity via a poorly characterized allosteric site. The catalytic domain of sGC has two putative nucleotide binding sites. One of these sites lacks an aspartate residue that is essential for catalysis, and is denoted as the pseudosymmetric site. The role of pseudosymmetric site on nucleotide regulation was investigated by site‐point mutations at this site. Kinetic analysis of the pseudosymmetric site mutant at various NO states has shown that pseudosymmetric site is involved in nucleotide regulation of sGC, and the effect of nucleotides is also dependent on the NO binding state of the enzyme.