Publications

• Nicotinamide-adenine dinucleotide pyrophosphatase in the growing and aging mosquito.

  Anderson B.M., Lang C.A.

  1. The disappearance of pyridine nucleotides during incubation with mosquito homogenates proceeds through the hydrolysis of the pyrophosphate linkage of these compounds as demonstrated by the formation of NMN and AMP from NAD(+). This reaction was also demonstrated by the loss in the coenzyme func ... >> More

  1. The disappearance of pyridine nucleotides during incubation with mosquito homogenates proceeds through the hydrolysis of the pyrophosphate linkage of these compounds as demonstrated by the formation of NMN and AMP from NAD(+). This reaction was also demonstrated by the loss in the coenzyme functioning property of NAD(+) (yeast alcohol dehydrogenase reaction) without a concomitant loss in reactivity towards cyanide. Transglycosidase activity was not observed in the mosquito homogenates, and low concentrations of nicotinamide did not inhibit the NAD(+) splitting activity of these homogenates. These observations are all in accord with the presence in these homogenates of a NAD(+) pyrophosphatase rather than a NADase. 2. The NAD(+) pyrophosphatase is destroyed by boiling, is not heat-activated, and has a pH optimum at pH8.75. In addition to NAD(+), other dinucleotides such as NADP(+), the 3-acetylpyridine and thionicotinamide analogues of NAD(+) and the thionicotinamide analogue of NADP(+), function as substrates in the hydrolysis catalysed by the pyrophosphatase. 3. A decrease in the specific activity of NAD(+) pyrophosphatase was observed during larval development, and a barely detectable activity was found in the pupa and adult. 4. Enzyme activity per organism increased in the larva but decreased to a very low value in the pupa and adult. These results indicate that the decrease in specific activity was due to a decrease in enzyme concentration rather than an increase in amounts of protein. << Less

  Biochem J 101:392-396(1966) [PubMed] [EuropePMC]

  This publication is cited by 1 other entry.

• Cloning and characterization of the NADH pyrophosphatases from Caenorhabditis elegans and Saccharomyces cerevisiae, members of a Nudix hydrolase subfamily.

  Xu W., Dunn C.A., Bessman M.J.

  Two genes from Caenorhabditis elegans and Saccharomyces cerevisiae, coding for enzymes homologous to the Nudix hydrolase family of nucleotide pyrophosphatases, have been cloned and expressed in Escherichia coli. The purified enzymes are homodimers of 39.1 and 43. 5 kDa, respectively, are activated ... >> More

  Two genes from Caenorhabditis elegans and Saccharomyces cerevisiae, coding for enzymes homologous to the Nudix hydrolase family of nucleotide pyrophosphatases, have been cloned and expressed in Escherichia coli. The purified enzymes are homodimers of 39.1 and 43. 5 kDa, respectively, are activated by Mg(2+) and Mn(2+), and are 30 to 50 times more active on NADH than on NAD(+). They both have a conserved array of amino acids downstream of the Nudix box first seen in the orthologous enzyme from E. coli which designates them as members of an NADH pyrophosphatase subfamily of the Nudix hydrolases. << Less

  Biochem. Biophys. Res. Commun. 273:753-758(2000) [PubMed] [EuropePMC]

  This publication is cited by 1 other entry.

• A reduced pyridine nucleotide pyrophosphatase.

  JACOBSON K.B., KAPLAN N.O.

  J Biol Chem 226:427-437(1957) [PubMed] [EuropePMC]

  This publication is cited by 1 other entry.

• A heat-activated diphosphopyridine nucleotide pyrophosphatase from Proteus vulgaris.

  SWARTZ M.N., KAPLAN N.O., LAMBORG M.F.

  J Biol Chem 232:1051-1063(1958) [PubMed] [EuropePMC]

  This publication is cited by 1 other entry.

• Cloning, purification, and properties of a novel NADH pyrophosphatase. Evidence for a nucleotide pyrophosphatase catalytic domain in MutT-like enzymes.

  Frick D.N., Bessman M.J.

  An Escherichia coli open reading frame containing significant homology to the active site of the MutT enzyme codes for a novel dinucleotide pyrophosphatase. The motif shared by these two proteins and several others is conserved throughout nature and may designate a nucleotide-binding or pyrophosph ... >> More

  An Escherichia coli open reading frame containing significant homology to the active site of the MutT enzyme codes for a novel dinucleotide pyrophosphatase. The motif shared by these two proteins and several others is conserved throughout nature and may designate a nucleotide-binding or pyrophosphatase domain. The E. coli NADH pyrophosphatase has been cloned, overexpressed, and purified to near homogeneity. The protein contains 257 amino acids (M(r) = 29,774) and migrates on gel filtration columns as an apparent dimer. The enzyme catalyzes the hydrolysis of a broad range of dinucleotide pyrophosphates, but uniquely prefers the reduced form of NADH. The Vmax/Km for NADH (69 mumol min-1 mg-1 mM-1) is an order of magnitude higher than for any other dinucleotide pyrophosphate tested. In addition, the Km for NADH (0.1 mM) is 50-fold lower than the Km for NAD+. The hydrolysis of dinucleotide pyrophosphates requires divalent metal ions and yields two mononucleoside 5'-phosphates. The metals that most efficiently stimulate activity are Mg2+ and Mn2+. Although these metals support similar Vmax values at optimal metal concentration, the apparent Km for Mg2+ is 3.7 mM (at 1 mM NADH), whereas the apparent Km for Mn2+ at the same NADH concentration is 30 microM. << Less

  J. Biol. Chem. 270:1529-1534(1995) [PubMed] [EuropePMC]

  This publication is cited by 1 other entry.

• Purification and properties of NADP pyrophosphatase from Proteus vulgaris.

  Nakajima Y., Fukunaga N., Sasaki S., Usami S.

  Biochim Biophys Acta 293:242-255(1973) [PubMed] [EuropePMC]

  This publication is cited by 1 other entry.

• Analysis of Arabidopsis growth factor gene 1 (GFG1) encoding a nudix hydrolase during oxidative signaling.

  Jambunathan N., Mahalingam R.

  Maintenance of pyridine nucleotide homeostasis is vital for normal growth and development of plants and animals. We demonstrate that Arabidopsis Growth Factor Gene 1 (GFG1; At4g12720) encoding a nudix hydrolase, is an NADH pyrophosphatase and ADP-ribose pyrophosphatase. The affinity for NADH and A ... >> More

  Maintenance of pyridine nucleotide homeostasis is vital for normal growth and development of plants and animals. We demonstrate that Arabidopsis Growth Factor Gene 1 (GFG1; At4g12720) encoding a nudix hydrolase, is an NADH pyrophosphatase and ADP-ribose pyrophosphatase. The affinity for NADH and ADP-ribose indicates that this enzyme could serve as a connection between sensing cellular redox changes and downstream signaling. GFG1 transcript levels were rapidly and transiently induced during both biotic stresses imposed by avirulent pathogens and abiotic stresses like ozone and osmoticum. T-DNA knock out plants of GFG1 gene, gfg1-1, exhibit pleiotropic phenotypes such as reduced size, increased levels of reactive oxygen species and NADH, microscopic cell death, constitutive expression of pathogenesis-related genes and enhanced resistance to bacterial pathogens. The recombinant protein failed to complement the mutator deficiency in SBMutT-strain of Escherichia coli, suggesting this protein may not play a role in sanitizing the nucleotide pool. Based on rapid transcriptional changes in response to various stresses, substrate specificity of the enzyme, and analysis of the knock out mutant, we propose that GFG1 is a key gene linking cellular metabolism and oxidative signaling. << Less

  Planta 224:1-11(2006) [PubMed] [EuropePMC]

  This publication is cited by 1 other entry.

• Nucleotidases in plants. I. Partial purification and properties of the enzyme hydrolyzing flavine adenine dinucleotide from mung bean seedlings (Phaseolus radiatus).

  Kumar S.A., Rao N.A., Vaidyanathan C.S.

  Arch Biochem Biophys 111:646-652(1965) [PubMed] [EuropePMC]

  This publication is cited by 1 other entry.