RGD Reference Report - Nucleotidyl cyclase activity of soluble guanylyl cyclase alpha1beta1. - Rat Genome Database

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Nucleotidyl cyclase activity of soluble guanylyl cyclase alpha1beta1.

Authors: Beste, KY  Burhenne, H  Kaever, V  Stasch, JP  Seifert, R 
Citation: Beste KY, etal., Biochemistry. 2012 Jan 10;51(1):194-204. doi: 10.1021/bi201259y. Epub 2011 Dec 13.
RGD ID: 10401947
Pubmed: PMID:22122229   (View Abstract at PubMed)
DOI: DOI:10.1021/bi201259y   (Journal Full-text)

Soluble guanylyl cyclase (sGC) regulates several important physiological processes by converting GTP into the second-messenger cGMP. sGC has several structural and functional properties in common with adenylyl cyclases (ACs). Recently, we reported that membranous ACs and sGC are potently inhibited by 2',3'-O-(2,4,6-trinitrophenyl)-substituted purine and pyrimidine nucleoside 5'-triphosphates. Using a highly sensitive high-performance liquid chromatography-tandem mass spectrometry method, we report that highly purified recombinant sGC of rat possesses nucleotidyl cyclase activity. As opposed to GTP, ITP, XTP and ATP, the pyrimidine nucleotides UTP and CTP were found to be sGC substrates in the presence of Mn(2+). When Mg(2+) is used, sGC generates cGMP, cAMP, cIMP, and cXMP. In conclusion, soluble "guanylyl" cyclase possesses much broader substrate specificity than previously assumed. Our data have important implications for cyclic nucleotide-mediated signal transduction.

Gene Ontology Annotations    Click to see Annotation Detail View

Molecular Function

Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Gucy1a1Ratadenylate cyclase activity contributes_toIDA  RGD 
Gucy1b1Ratadenylate cyclase activity contributes_toIDA  RGD 
Gucy1a1Ratcytidylate cyclase activity contributes_toIDA  RGD 
Gucy1b1Ratcytidylate cyclase activity contributes_toIDA  RGD 

Objects Annotated

Genes (Rattus norvegicus)
Gucy1a1  (guanylate cyclase 1 soluble subunit alpha 1)
Gucy1b1  (guanylate cyclase 1 soluble subunit beta 1)

Additional Information