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- W2009784881 abstract "Partially purified hepatic soluble guanylate cyclase (EC 4.6.1.2) was rapidly inactivated by molecular oxygen and by low concentrations of SH oxidants at pH 7.4, a process which was prevented and reversed by dithiothreitol. Cystamine and 5,5′-dithiobis(2-nitrobenzoic acid) inhibited enzymatic activity in a time- and temperature-dependent manner. Various disulfides, SH oxidants, and thiol alkylating agents inhibited both basal guanylate cyclase activity and activity stimulated by nitric oxide, S-nitrosocysteine, and nitrosylhemoglobin. These observations indicate that guanylate cyclase possesses one or more SH groups at its catalytic site. Preincubation of guanylate cyclase with excess MgGTP or with enzyme activators markedly protected the enzyme against inhibition by various thiol reactive agents. These findings suggest that the SH groups at the catalytic site interact also with enzyme activators. 2,3-Dimercaprol, which possesses vicinal dithiols, but not dithiothreitol markedly inhibited guanylate cyclase activity at concentrations equal to or exceeding those of MgGTP. Thus, two closely juxtaposed SH groups may be located at the catalytic site. The presence of cysteine or hematin in preincubates of guanylate cyclase, to which nitric oxide was also added, was mandatory in order to enable the activated form of the enzyme to be recovered by gel filtration. Guanylate cyclase activated by S-nitrosocysteine or nitrosyl-hemoglobin was recovered in the maximally activated state, and this was prevented by preincubation of enzyme with SH oxidants or excess MgGTP. These data imply that cysteine, hematin, and their nitrosyl derivatives bind to SH groups at the catalytic site of guanylate cyclase." @default.
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- W2009784881 date "1981-04-01" @default.
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- W2009784881 title "Evidence that regulation of hepatic guanylate cyclase activity involves interactions between catalytic site SH groups and both substrate and activator" @default.
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- W2009784881 doi "https://doi.org/10.1016/0003-9861(81)90125-9" @default.
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