Dav id Karow et al. (2002) West Coast Worm Meeting "Guanylate Cyclase Beta 2 Subunit: A Novel NO-insensitive, Heme-bound Cyclase?"

Dav id Karow, Chinmay Majmudar, Ron Ellis, Michael Marletta, Jennifer Chang

[West Coast Worm Meeting, 2002]

Soluble guanylate cyclases (sGCs) catalyze the conversion of GTP to cGMP. In mammals, the most well-studied sGC is a heme-containing, heterodimer, composed of alpha 1 and beta 1 subunits. Nitric oxide (NO) binds to the heme, which is ligated to the beta 1 subunit, and stimulates the activity of the enzyme 400fold. A beta 1 homologue, beta 2, has been cloned from rat and human kidney cDNA libraries and appears to be expressed in the kidney collecting duct cells. However, the heme binding status, sensitivity to NO, and intracellular localization are not well-characterized. We would like to elucidate the structure and function of this protein.