Conversion of a guanylyl cyclase to an adenylyl cyclase

Research output: Contribution to journalArticlepeer-review

16 Scopus citations


Guanylyl cyclases catalyze the formation of cGMP from GTP, but display extensive identity at the catalytic domain primary amino acid level with the adenylyl cyclases. The recent solving of the crystal structures of soluble forms of adenylyl cyclase has resulted in predictions of those amino acids important for substrate specificity. Modeling of a membrane-bound homodimeric guanylyl cyclase predicted the comparable amino acids that would interact with the guanine ring. Based on these structural data, the replacement of three key residues in the heterodimeric form of soluble guanylyl cyclase has led to a complete conversion in substrate specificity. Furthermore, the mutant enzyme remained fully sensitive to sodium nitroprusside, a nitric oxide donor.

Original languageEnglish (US)
Pages (from-to)545-550
Number of pages6
JournalMethods: A Companion to Methods in Enzymology
Issue number4
StatePublished - Dec 1999
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)


Dive into the research topics of 'Conversion of a guanylyl cyclase to an adenylyl cyclase'. Together they form a unique fingerprint.

Cite this