ADP-ribosyl transferase and NAD glycohydrolase activities in rat liver mitochondria

O-ADP-Ribosylation in the NAD/NADase System: 2-Alkanols as Efficient Substrates.

“…However, in the equimolar mixture system of both 1-and 2-propanols (or butanols), the O-ribosylated compound from 1-propanol (or 1-butanol) was predominantly produced. 1 H-NMR signals due to the methyl protons of the alkoxide moieties in the mixed products 9 and 16 showed readily distinguishable chemical shifts with different splitting patterns [d 1.09 (d) and d 0.81 (t)]. Based on the integration of those two methyl signals, the formation ratio of 9 and 16 was estimated to be 1 : 4.…”

“…[1][2][3] ADP-ribosylation occurs, depending upon the chemicoenvironmental conditions, on the appropriate ring nitrogen atom of various nitrogen-containing heterocyclic compounds. 4) In general, the enzymatic reaction has been shown to be susceptible to the stereochemical and electronic environment of the substrate.…”

Inhibition of glutamate dehydrogenase and insulin secretion by KHG26377 does not involve ADP-ribosylation by SIRT4 or deacetylation by SIRT3

“…It is known that GDH is regulated by reversible ADP-ribosylation (13). Although many researchers have studied ADP-ribosylation of mitochondrial proteins (13)(14)(15)(16)(17), the identity of proteins involved remained unknown until Herrero-Yraola et al (13) showed that GDH is an actual target of this modification. SIRT4 is a mitochondrial enzyme that uses NAD + to ADP-ribosylate and downregulate GDH activity (18).…”

Unusual Enzymatic Hydrolysis of NAD by Solubilized Form of NAD+ Glycohydrolase.

“…There have been many reports [1][2][3][4][5][6][7][8][9] concerning substrates for the transferaselike activity of NADase, including synthetic low molecular compounds [2][3][4][5] and certain antibiotics components 6,7) as well as in vivo high molecular constituents. [8][9][10] NADase is a membrane-bound ecto-enzyme that is widely distributed in the organism, the richest source generally being the spleen, brain, and liver.…”

“…There have been many reports [1][2][3][4][5][6][7][8][9] concerning substrates for the transferaselike activity of NADase, including synthetic low molecular compounds [2][3][4][5] and certain antibiotics components 6,7) as well as in vivo high molecular constituents. [8][9][10] NADase is a membrane-bound ecto-enzyme that is widely distributed in the organism, the richest source generally being the spleen, brain, and liver.11) From the established viewpoint that the catalytic domain of the enzyme occurs in the extracellular region of the molecule, 12) it is of interest to examine whether enzyme activities of the parent particulate NADase (pNADase) are similarly observed with a solubilized extracellular portion (sNADase) of the pNADase.Thus, we undertook the solubilization of the porcine brain pNADase according to the method for bovine spleen NADase of Augustin et al,13) since no procedure has not been established for porcine brain NADase. The crude sNADase thus obtained, however, showed unexpected catalytic properties of a phosphatase-like function rather than the usual hydrolase activity.…”