Quantification of Quinolinic Acid Metabolism by Macrophages and Astrocytes

Author(s):  
Melvyn P. Heyes ◽  
Eugene O. Major ◽  
Kuniaki Sato ◽  
Sanford M. Markey
1984 ◽  
Vol 7 ◽  
pp. S247 ◽  
Author(s):  
R. Schwarcz ◽  
A. C. Foster

1987 ◽  
Vol 436 (1) ◽  
pp. 18-24 ◽  
Author(s):  
Carmela Speciale ◽  
Etsuo Okuno ◽  
Robert Schwarcz

1988 ◽  
Vol 99 (1) ◽  
pp. 213-218 ◽  
Author(s):  
Carmela Speciale ◽  
Robert Schwarcz

1949 ◽  
Vol 181 (2) ◽  
pp. 687-692
Author(s):  
L.M. Henderson ◽  
G.B. Ramasarma

1949 ◽  
Vol 181 (2) ◽  
pp. 677-685 ◽  
Author(s):  
L.M. Henderson

1949 ◽  
Vol 181 (2) ◽  
pp. 731-738 ◽  
Author(s):  
L.M. Henderson ◽  
G.B. Ramasarma ◽  
B. Connor Johnson

1949 ◽  
Vol 181 (2) ◽  
pp. 667-675 ◽  
Author(s):  
L.M. Henderson ◽  
Herbert M. Hirsch

1989 ◽  
Vol 490 (1) ◽  
pp. 103-109 ◽  
Author(s):  
Robert Schwarcz ◽  
Etsuo Okuno ◽  
Robert J. White

2003 ◽  
Vol 185 (16) ◽  
pp. 4844-4850 ◽  
Author(s):  
Silvia Garavaglia ◽  
Alessandro Galizzi ◽  
Menico Rizzi

ABSTRACT NADP is essential for biosynthetic pathways, energy, and signal transduction. In living organisms, NADP biosynthesis proceeds through the phosphorylation of NAD with a reaction catalyzed by NAD kinase. We expressed, purified, and characterized Bacillus subtilis NAD kinase. This enzyme represents a new member of the inorganic polyphosphate [poly(P)]/ATP NAD kinase subfamily, as it can use poly(P), ATP, or other nucleoside triphosphates as phosphoryl donors. NAD kinase showed marked positive cooperativity for the substrates ATP and poly(P) and was inhibited by its product, NADP, suggesting that the enzyme plays a major regulatory role in NADP biosynthesis. We discovered that quinolinic acid, a central metabolite in NAD(P) biosynthesis, behaved like a strong allosteric activator for the enzyme. Therefore, we propose that NAD kinase is a key enzyme for both NADP metabolism and quinolinic acid metabolism.


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