Format

Send to

Choose Destination
J Biochem. 1999 Mar;125(3):449-53.

Purification and characterization of ADP-ribosyl cyclase from Euglena gracilis.

Author information

1
Department of Applied Biological Chemistry, Osaka Prefecture University, Sakai, Osaka, 599-8531, Japan.

Abstract

ADP-ribosyl cyclase, which catalyzes the conversion from NAD+ to cyclic adenosine diphosphoribose (cADPR), is proposed to participate in cell cycle regulation in Euglena gracilis. This enzyme, which was found as a membrane-bound protein, was purified almost the homogeneity after solubilization with deoxycholate, and found to be a monomeric protein with a molecular mass of 40 kDa. Its Km value for NAD+ was estimated to be 0.4 mM, and cADPR, a product of the enzyme, inhibited the enzyme competitively with respect to NAD+ whereas another product, nicotinamide, showed noncompetitive (mixed-type) inhibition. In contrast to mammalian CD38 and BST-1, Euglena ADP-ribosyl cyclase lacked cADPR hydrolase activity.

[Indexed for MEDLINE]
Free full text

Supplemental Content

Full text links

Icon for Silverchair Information Systems Icon for J-STAGE, Japan Science and Technology Information Aggregator, Electronic
Loading ...
Support Center