Description
Soluble guanylate cyclase is a heterodimeric enzyme, composed of α and β subunits, that synthesizes cGMP from GTP. The enzyme is activated by the binding of nitric oxide or carbon monoxide to the heme group of the enzyme. Chronic hypoxia upregulates soluble guanylate expression in rat lung. The α1 subunit contains 690-
717 amino acids and has a molecular mass of 77-
82 kDa. The cloned β1 subunit of guanylate cyclase from human, bovine, and rat sources contains 619 amino acids and has a molecular mass of approximately 70,000.
References
[1] JAMES R. STONE Michael A M. Soluble Guanylate Cyclase from Bovine Lung: Activation with Nitric Oxide and Carbon Monoxide and Spectral Characterization of the Ferrous and Ferric States[J]. Biochemistry Biochemistry, 1994, 33 18: 5636-5640. DOI:
10.1021/bi00184a036[2] D LI R A J N Zhou. Soluble guanylate cyclase gene expression and localization in rat lung after exposure to hypoxia.[J]. American Journal of Physiology, 1999, 277 4: L841-7. DOI:
10.1152/ajplung.1999.277.4.l841[3] GALICIA GIUILI. Molecular cloning of the cDNAs coding for the two subunits of soluble guanylyl cyclase from human brain[J]. FEBS Letters, 1992, 304 1: Pages 83-88. DOI:
10.1016/0014-5793(92)80594-7[4] M. NAKANE. Molecular cloning and expression of cDNAs coding for soluble guanylate cyclase from rat lung.[J]. The Journal of Biological Chemistry, 1990, 184 1: 16841-16845. DOI:
10.1016/s0021-9258(17)44837-x[5] MYUNG HO LEE Robert M B. Supplementation of the phosphatidyl-L-serine requirement of protein kinase C with nonactivating phospholipids[J]. Biochemistry Biochemistry, 1992, 31 22: 5176-5182. DOI:
10.1021/bi00137a013[6] DORIS KOESLING . The primary structure of the 70 kDa subunit of bovine soluble guanylate cyclase[J]. FEBS Letters, 1988, 239 1: Pages 29-34. DOI:
10.1016/0014-5793(88)80539-8[7] MASAKI NAKANE . Molecular cloning of a cDNA coding for 70 kilodalton subunit of soluble guanylate cyclase from rat lung[J]. Biochemical and biophysical research communications, 1988, 157 3: Pages 1139-1147. DOI:
10.1016/s0006-291x(88)80992-6