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1 NMN appeared to have stronger effects on liver fat catab
2 NMN deamidase, a bacterial enzyme, shares NMN-consuming
3 NMN is a rate-limiting precursor for recycling to the es
4 NMN is a substrate of both ectoenzymes CD38 and CD73, wi
5 NMN synthesis by NAMPT is powerfully inhibited by both N
7 ntral domain has a weak adenylyltransferase (NMN-AT; EC 2.7.7.1) activity that converts NMN directly
10 Inhibition is observed with reduced beta-NMN and alpha-NADH, but neither is as effective as beta-
12 to be a bifunctional enzyme possessing both NMN adenylytransferase (NMNAT; EC ) and ribosylnicotinam
13 strate specificity of the enzyme toward both NMN and NaMN and reveal the structural mechanism for ade
14 nique dual substrate specificity toward both NMN and NaMN, thus flexible in participating in both de
19 table isotope-labelled compounds, we confirm NMN is metabolized extracellularly to NR that is then ta
20 (NMN-AT; EC 2.7.7.1) activity that converts NMN directly to NAD but is physiologically irrelevant.
21 (NMN) in zebrafish and mice, which decreases NMN levels by converting it to NaMN, protects against ax
24 D38 impairs, the conversion of extracellular NMN to NR as a precursor for intracellular NAD(+) biosyn
25 an cells require conversion of extracellular NMN to NR for cellular uptake and NAD(+) synthesis, expl
26 reated cells supplemented with extracellular NMN was strongly reduced in tumor cells, upon pharmacolo
31 In route 1, nicotinamide is removed from NMN in the periplasm and enters the cell as the free bas
32 2, described here, phosphate is removed from NMN in the periplasm by acid phosphatase (AphA), and the
33 validation of the predicted route (NaMN --> NMN --> NAD) in F. tularensis including mathematical mod
34 y in pnuC* transporter mutants, which import NMN intact and can therefore grow on lower levels of NMN
39 cterial nicotinamide adenine mononucleotide (NMN) in zebrafish and mice, which decreases NMN levels b
41 le synthesis of nicotinamide mononucleotide (NMN) and inorganic pyrophosphate (PP i) from nicotinamid
42 ccumulations of nicotinamide mononucleotide (NMN) and nicotinamide riboside (NR) in the amidated salv
43 (+) precursors, nicotinamide mononucleotide (NMN) and NR, can reverse the FK866-induced cell death, t
46 D(+) precursor, nicotinamide mononucleotide (NMN) can reverse some of the negative consequences of hi
47 N) and mediates nicotinamide mononucleotide (NMN) catabolism, thereby contributing to both NmR salvag
51 cleoside of the nicotinamide mononucleotide (NMN) leaving group are oriented solely via atomic intera
52 tion of NaMN to nicotinamide mononucleotide (NMN) occurs before the adenylylation reaction, which con
53 ursors, such as nicotinamide mononucleotide (NMN) or nicotinamide riboside (NR), protects against met
54 zymatic product nicotinamide mononucleotide (NMN), was not blocked by the Nampt enzyme inhibitor FK86
58 the condensation of pyridine mononucleotide (NMN or NaMN) with the AMP moiety of ATP to form NAD (or
62 was downregulated and so the accumulation of NMN and NR was best explained by reduced flux through th
64 ve ATPase activity, allows the production of NMN at product:substrate ratios thermodynamically forbid
65 further study to confirm the suitability of NMN for use in reversing metabolic dysfunction linked to
66 strates and NAD(+), and the IC(50) values of NMN and AMP, examined the effects of MgCl(2) and PEG(800
69 overexpressed NMNATs, NMN deamidase reduces NMN accumulation in injured mouse sciatic nerves and pre
71 NMN deamidase, a bacterial enzyme, shares NMN-consuming activity with NMNAT2, but not NAD-synthesi
72 l by maintaining low levels of its substrate NMN rather than generating NAD; however, this is still d
74 complex of CD38 with one of its substrates, NMN, showed that the nicotinamide moiety was in close co
78 14); (ii) comprise the interface between the NMN-binding domain (domain Ia) and the nucleotidyltransf
80 Together with the crystal structure of the NMN.PPi.Mg2.enzyme complex, the reaction coordinate is d
81 itors with oxacarbenium mimics replacing the NMN-ribosyl group of NAD(+) show 200-620-fold increased
85 e catalytic domain is flanked by an upstream NMN-binding module and by downstream OB-fold, zinc finge
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