Acting on acid anhydrides;
In phosphorus-containing anhydrides
This enzyme, described from plants, animals, and bacteria, can act on both reduced and oxidized forms of its substrate, although enzymes from different organisms have different preferences. Also acts on other dinucleotides, including NADP(H), FAD(H2), and the thionicotinamide analogues of NAD+ and NADP+.
EC 184.108.40.206 created 1972
|Nicotinate and nicotinamide metabolism|
Kornberg, A. and Pricer, W.E.
J Biol Chem 182:763-778 (1950)
JACOBSON KB, KAPLAN NO.
A reduced pyridine nucleotide pyrophosphatase.
J Biol Chem 226:427-37 (1957)
SWARTZ MN, KAPLAN NO, LAMBORG MF.
A heat-activated diphosphopyridine nucleotide pyrophosphatase from Proteus vulgaris.
J Biol Chem 232:1051-63 (1958)
Kumar SA, Rao NA, Vaidyanathan CS.
Nucleotidases in plants. I. Partial purification and properties of the enzyme hydrolyzing flavine adenine dinucleotide from mung bean seedlings (Phaseolus radiatus).
Anderson BM, Lang CA.
Nicotinamide-adenine dinucleotide pyrophosphatase in the growing and aging mosquito.
Nakajima Y, Fukunaga N, Sasaki S, Usami S.
Purification and properties of NADP pyrophosphatase from Proteus vulgaris.
Frick DN, Bessman MJ
Cloning, purification, and properties of a novel NADH pyrophosphatase. Evidence for a nucleotide pyrophosphatase catalytic domain in MutT-like enzymes.
Xu W, Dunn CA, Bessman MJ
Cloning and characterization of the NADH pyrophosphatases from Caenorhabditis elegans and Saccharomyces cerevisiae, members of a Nudix hydrolase subfamily.
Jambunathan N, Mahalingam R
Analysis of Arabidopsis growth factor gene 1 (GFG1) encoding a nudix hydrolase during oxidative signaling.
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