NAD(+)-glycohydrolase from Streptococcus pyogenes shows cyclic ADP-ribose forming activity.
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+.
Karasawa
T
T
Department of Bacteriology, School of Medicine, Kanazawa University, Japan.
Takasawa
S
S
Yamakawa
K
K
Yonekura
H
H
Okamoto
H
H
Nakamura
S
S
D000246:Adenosine Diphosphate Ribose / Q000031:analogs & derivatives* / Q000096:biosynthesis; D036563:Cyclic ADP-Ribose; D009244:NAD+ Nucleosidase / Q000302:isolation & purification / Q000494:pharmacology*; D013297:Streptococcus pyogenes / Q000201:enzymology*
D036563:Cyclic ADP-Ribose; D000246:Adenosine Diphosphate Ribose; D009244:NAD+ Nucleosidase