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J Biol Chem, Vol. 274, Issue 4, 2525-2531, January 22, 1999

Identification and Characterization of a Novel  Subunit of Soluble Guanylyl Cyclase That Is Active in the Absence of a Second Subunit and Is Relatively Insensitive to Nitric Oxide

Alan Nighorn, Kathryn A. Byrnes, and David B. Morton^§

From the  Arizona Research Labs, Division of Neurobiology, The University of Arizona, Tucson, Arizona 85721 and the ^§ Department of Biological Structure and Function, Oregon Health Sciences University, School of Dentistry, Portland, Oregon 97201-3097

Previously characterized soluble guanylyl cyclases form - heterodimers that can be activated by the gaseous messenger, nitric oxide. In mammals, four subunits have been cloned, named 1, 2, 1, and 2. We have identified a novel soluble guanylyl cyclase isoform from the nervous system of the insect Manduca sexta that we have named M. sexta guanylyl cyclase 3 (MsGC-3). It is most closely related to the mammalian  subunits but has several features that distinguish it from previously identified soluble cyclases. Most importantly, MsGC-3 does not need to form heterodimers to form an active enzyme because guanylyl cyclase activity can be measured when it is expressed alone in COS-7 cells. Moreover, this activity is only weakly enhanced in the presence of the nitric oxide donor, sodium nitroprusside. Several of the amino acids in rat 1 subunits, previously identified as being important in heme binding or necessary for nitric oxide activation, are substituted with nonsimilar amino acids in MsGC-3. There are also an additional 315 amino acids C-terminal to the catalytic domain of MsGC-3 that have no sequence similarity to any known protein. Northern blot analysis shows that MsGC-3 is primarily expressed in the nervous system of Manduca.

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