NAD(+)-glycohydrolase from Streptococcus pyogenes shows cyclic ADP-ribose forming activity

FEMS Microbiol Lett. 1995 Aug 1;130(2-3):201-4. doi: 10.1111/j.1574-6968.1995.tb07720.x.

Abstract

NAD(+)-glycohydrolase from Streptococcus pyogenes was purified by successive chromatography on CM Sepharose CL-6B, Sephacryl S-200 HR and hydroxyapatite. The purified enzyme possessed synthesis and hydrolysis activities of cyclic ADP-ribose (cADPR), a newly found second messenger for Ca2+ mobilisation, along with cleavage activity of the ribose-nicotinamide bond in NAD+.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Diphosphate Ribose / analogs & derivatives*
  • Adenosine Diphosphate Ribose / biosynthesis
  • Cyclic ADP-Ribose
  • NAD+ Nucleosidase / isolation & purification
  • NAD+ Nucleosidase / pharmacology*
  • Streptococcus pyogenes / enzymology*

Substances

  • Cyclic ADP-Ribose
  • Adenosine Diphosphate Ribose
  • NAD+ Nucleosidase