Substrate selection by class III adenylyl cyclases and guanylyl cyclases

IUBMB Life. 2005 Dec;57(12):797-803. doi: 10.1080/15216540500415636.

Abstract

The second messengers cAMP and cGMP are of central importance in signal transduction pathways. To assure pathway specificity adenylyl and guanylyl cyclases are highly selective for their substrates, ATP and GTP, respectively. The universal class III cyclases are equipped with a variety of purine-binding modes, which have been identified by structure determination and mutagenesis. Most selection mechanisms rely on a pair of residues which form hydrogen bonds to N1 and the N(6)-amino or O(6)-keto group of adenine and guanine, respectively. Furthermore, selection is supported by hydrogen bonds involving the peptide backbone and by constraints imposed by hydrophobic side-chains.

Publication types

  • Review

MeSH terms

  • Adenosine Triphosphate / metabolism
  • Adenylyl Cyclases / chemistry
  • Adenylyl Cyclases / metabolism*
  • Animals
  • Bacteria
  • Eukaryota
  • Guanosine Triphosphate / metabolism
  • Guanylate Cyclase / chemistry
  • Guanylate Cyclase / metabolism*
  • Hydrogen Bonding
  • Isoenzymes / chemistry
  • Isoenzymes / metabolism
  • Mammals
  • Protein Binding
  • Purines / metabolism*
  • Signal Transduction / genetics*
  • Substrate Specificity

Substances

  • Isoenzymes
  • Purines
  • Guanosine Triphosphate
  • Adenosine Triphosphate
  • Adenylyl Cyclases
  • adenylate cyclase 3
  • Guanylate Cyclase