β-Nicotinamide mononucleotide
β-Nicotinamide mononucleotide structure
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Common Name | β-Nicotinamide mononucleotide | ||
|---|---|---|---|---|
| CAS Number | 1094-61-7 | Molecular Weight | 334.219 | |
| Density | N/A | Boiling Point | N/A | |
| Molecular Formula | C11H15N2O8P | Melting Point | N/A | |
| MSDS | Chinese USA | Flash Point | N/A | |
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Lipopolysaccharide Regulation of Intestinal Tight Junction Permeability Is Mediated by TLR4 Signal Transduction Pathway Activation of FAK and MyD88.
J. Immunol. 195 , 4999-5010, (2015) Gut-derived bacterial LPS plays an essential role in inducing intestinal and systemic inflammatory responses and have been implicated as a pathogenic factor in necrotizing enterocolitis and inflammatory bowel disease. The defective intestinal tight junction b... |
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A possibility of nutriceuticals as an anti-aging intervention: activation of sirtuins by promoting mammalian NAD biosynthesis.
Pharmacol. Res. 62(1) , 42-7, (2010) Aging science has recently drawn much attention, and discussions on the possibility of anti-aging medicine have multiplied. One potential target for the development of anti-aging drugs is the SIR2 (silent information regulator 2) family of NAD-dependent deace... |
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The high-resolution crystal structure of periplasmic Haemophilus influenzae NAD nucleotidase reveals a novel enzymatic function of human CD73 related to NAD metabolism.
Biochem. J. 441(1) , 131-41, (2012) Haemophilus influenzae is a major pathogen of the respiratory tract in humans that has developed the capability to exploit host NAD(P) for its nicotinamide dinucleotide requirement. This strategy is organized around a periplasmic enzyme termed NadN (NAD nucle... |
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Nicotinamide phosphoribosyltransferase/visfatin does not catalyze nicotinamide mononucleotide formation in blood plasma.
PLoS ONE 6(8) , e22781, (2011) Nicotinamide (Nam) phosphoribosyltransferase (NAMPT) is the rate-limiting enzyme in mammalian NAD synthesis, catalyzing nicotinamide mononucleotide (NMN) formation from Nam and 5-phosphoribosyl 1-pyrophosphate (PRPP). NAMPT has also been described as an adipo... |
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Nicotinamide mononucleotide protects against pro-inflammatory cytokine-mediated impairment of mouse islet function.
Diabetologia 54(12) , 3083-92, (2011) Nicotinamide phosphoribosyltransferase (NAMPT), the rate-limiting enzyme for NAD(+) biosynthesis, exists as intracellular NAMPT (iNAMPT) and extracellular NAMPT (eNAMPT). eNAMPT, secreted from adipose tissue, promotes insulin secretion. Administration of nico... |
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Detection and pharmacological modulation of nicotinamide mononucleotide (NMN) in vitro and in vivo.
Biochem. Pharmacol. 77(10) , 1612-20, (2009) The emerging key role of NAD-consuming enzymes in cell biology has renewed the interest in NAD resynthesis through the rescue pathways. The first step of the nicotinamide-dependent NAD-rescue pathway is operated by nicotinamide phosphoribosyl transferase (NaP... |
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Effects of long-acting somatostatin analogues on adrenal growth and phosphoribosyl pyrophosphate formation in experimental diabetes.
Int. J. Exp. Pathol. 93(1) , 56-69, (2012) Adrenal growth and increased adrenal function occur in experimental diabetes. Previously, we have shown that phosphoribosyl pyrophosphate (PRPP) and PRPP synthetase increased rapidly between 3 and 7 days after induction of diabetes with streptozotocin (STZ), ... |
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Enzymatic biofuel cells utilizing a biomimetic cofactor.
Chem. Commun. (Camb.) 48(13) , 1898-900, (2012) The performance of immobilized enzyme systems is often limited by cofactor diffusion and regeneration. Here, we demonstrate an engineered enzyme capable of utilizing the minimal cofactor nicotinamide mononucleotide (NMN(+)) to address these limitations. Signi... |
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CD73 protein as a source of extracellular precursors for sustained NAD+ biosynthesis in FK866-treated tumor cells.
J. Biol. Chem. 288(36) , 25938-49, (2013) NAD(+) is mainly synthesized in human cells via the "salvage" pathways starting from nicotinamide, nicotinic acid, or nicotinamide riboside (NR). The inhibition with FK866 of the enzyme nicotinamide phosphoribosyltransferase (NAMPT), catalyzing the first reac... |
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ArsAB, a novel enzyme from Sporomusa ovata activates phenolic bases for adenosylcobamide biosynthesis.
Mol. Microbiol. 81(4) , 952-67, (2011) In the homoacetogenic bacterium Sporomusa ovata, phenol and p-cresol are converted into α-ribotides, which are incorporated into biologically active cobamides (Cbas) whose lower ligand bases do not form axial co-ordination bonds with the cobalt ion of the cor... |