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Citation
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HERO ID
1640618
Reference Type
Journal Article
Subtype
Review
Title
Guanylate cyclase and the .NO/cGMP signaling pathway
Author(s)
Denninger, JW; Marletta, MA
Year
1999
Is Peer Reviewed?
1
Journal
Biochimica et Biophysica Acta
ISSN:
0006-3002
EISSN:
1878-2434
Volume
1411
Issue
2-3
Page Numbers
334-350
Language
English
PMID
10320667
Abstract
Signal transduction with the diatomic radical nitric oxide (NO) is involved in a number of important physiological processes, including smooth muscle relaxation and neurotransmission. Soluble guanylate cyclase (sGC), a heterodimeric enzyme that converts guanosine triphosphate to cyclic guanosine monophosphate, is a critical component of this signaling pathway. sGC is a hemoprotein; it is through the specific interaction of NO with the sGC heme that sGC is activated. Over the last decade, much has been learned about the unique heme environment of sGC and its interaction with ligands like NO and carbon monoxide. This review will focus on the role of sGC in signaling, its relationship to the other nucleotide cyclases, and on what is known about sGC genetics, heme environment and catalysis. The latest understanding in regard to sGC will be incorporated to build a model of sGC structure, activation, catalytic mechanism and deactivation.
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