Title : Acidic residues at the active sites of CD38 and ADP-ribosyl cyclase determine nicotinic acid adenine dinucleotide phosphate (NAADP) synthesis and hydrolysis activities.

Pub. Date : 2006 Sep 29

PMID : 16861223






5 Functional Relationships(s)
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1 Acidic residues at the active sites of CD38 and ADP-ribosyl cyclase determine nicotinic acid adenine dinucleotide phosphate (NAADP) synthesis and hydrolysis activities. NAADP CD38 molecule Homo sapiens
2 Acidic residues at the active sites of CD38 and ADP-ribosyl cyclase determine nicotinic acid adenine dinucleotide phosphate (NAADP) synthesis and hydrolysis activities. NAADP CD38 molecule Homo sapiens
3 Here we show that CD38 can, in fact, hydrolyze NAADP to ADP-ribose 2"-phosphate. NAADP CD38 molecule Homo sapiens
4 Synthesis of NAADP catalyzed by CD38 is known to have strong preference for acidic pH, suggesting that Glu(146) and Asp(155) are also critical determinants. NAADP CD38 molecule Homo sapiens
5 Likewise, using similar approaches, Glu(98) of the cyclase, which is equivalent to Glu(146) in CD38, was found to be responsible for controlling the pH dependence of NAADP synthesis by the cyclase. NAADP CD38 molecule Homo sapiens