A Novel Preparation of Nicotinamide Mononucleotide

Liu, Rihe; Visscher, J.

doi:10.1080/15257779408011891

Cited by 10 publications

(7 citation statements)

References 5 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…All chemicals were purchased from Sigma-Aldrich unless otherwise stated. Accurate concentrations of cofactor fragments and analogues were measured by UV/vis spectrophotometry using the following extinction coefficients: 6220 M -1 cm -1 at 340 nm for NADPH and NADH; 18000 M -1 cm -1 at 260 nm for NADP + and NAD + ; 15400 M -1 cm -1 at 259 nm for AMP, ADP, and ATP; 4200 M -1 cm -1 at 266 nm for β-NMN; 13700 M -1 cm -1 at 253 nm for GDP and GTP; 15400 M -1 cm -1 at 260 nm for 2‘P-AMP and 2‘P-ADP-ribose. , …”

Section: Methodsmentioning

confidence: 99%

Probing Hot Spots at Protein−Ligand Binding Sites: A Fragment-Based Approach Using Biophysical Methods

et al. 2006

View full text Add to dashboard Cite

Mapping interactions at protein-ligand binding sites is an important aspect of understanding many biological reactions and a key part of drug design. In this paper, we have used a fragment-based approach to probe "hot spots" at the cofactor-binding site of a model dehydrogenase, Escherichia coli ketopantoate reductase. Our strategy involved the breaking down of NADPH (Kd = 300 nM) into smaller fragments and the biophysical characterization of their binding using WaterLOGSY NMR spectroscopy, isothermal titration calorimetry (ITC), and inhibition studies. The weak binding affinities of fragments were measured by direct ITC titrations under low c value conditions. The 2'-phosphate and the reduced nicotinamide groups were found to contribute a large part of the binding energy. A combination of ITC and site-directed mutagenesis enabled us to locate the fragments at separate hot spots on opposite ends of the cofactor-binding site. This study has identified structural determinants for cofactor recognition that represent a blueprint for future inhibitor design.

show abstract

Section: Methodsmentioning

confidence: 99%

Probing Hot Spots at Protein−Ligand Binding Sites: A Fragment-Based Approach Using Biophysical Methods

et al. 2006

View full text Add to dashboard Cite

show abstract

“…A key intermediate in the synthesis of all of the NAD analogues was imidazole-activated nicotinamide mononucleotide ( 8 ), obtained from nicotinamide riboside (NR) 5′-monophosphate ( 7 ). The latter can be either synthesized de novo by a multistep procedure, prepared enzymatically, or obtained by hydrolysis of commercially available NAD in the presence of aqueous ZrCl 4 . We chose the last of these methods, as it appeared the most time- and cost-efficient for gram-scale synthesis.…”

mentioning

confidence: 99%

“…The latter can be either synthesized de novo by a multistep procedure, 14 prepared enzymatically, 15 or obtained by hydrolysis of commercially available NAD in the presence of aqueous ZrCl 4 . 16 We chose the last of these methods, as it appeared the most time-and cost-efficient for gram-scale synthesis. The resulting mixture of AMP and nicotinamide mononucleotide was separated by ion-exchange chromatography (IEC) using DEAE Sephadex A25 to give compound 7 as a triethylammonium salt in 30% yield (Scheme 1A).…”

mentioning

confidence: 99%

Nicotinamide-Containing Di- and Trinucleotides as Chemical Tools for Studies of NAD-Capped RNAs

et al. 2018

View full text Add to dashboard Cite

We report the chemical synthesis of a set of nicotinamide adenine dinucleotide (NAD) cap analogues containing chemical modifications that reduce their susceptibility to NAD-RNA-degrading enzymes. These analogues can be incorporated into transcripts in a similar way as NAD. Biochemical characterization of RNAs carrying these caps with DXO, NudC, and Nudt12 enzymes led to the identification of compounds that can be instrumental in unraveling so far unaddressed biological aspects of NAD-RNAs.

show abstract

“…NMN-phosphorimidazolide (Im-NMN) was synthesized as described with some modifications. Starting from NMN, Im-NMN-2′-3′-carbonate was prepared using a 10× excess of CDI in dry DMF. Hydrolysis of this intermediate with 0.2 M TEAB furnished Im-NMN in 63% yield and high purity (Figures S1 and S2 in Supporting Information).…”

mentioning

confidence: 99%

Synthesis of 5′-NAD-Capped RNA

et al. 2016

View full text Add to dashboard Cite

In prokaryotic organisms, certain regulatory RNAs have recently been found to be linked to the ubiquitous redox cofactor nicotinamide adenine dinucleotide (NAD) at their 5'-ends. Biochemical and structural investigations of this new caplike RNA modification require synthetic access to pure NAD-RNA. Here we report a chemoenzymatic approach to generate 5'-NAD-capped RNA in high yields and purity under mild conditions. This approach uses unprotected 5'-monophosphate RNA synthesized either chemically or enzymatically, 5',5'-pyrophosphate bond formation by phosphorimidazolide chemistry, and an enzymatic cleanup step. Thus, 5'-NAD-modified RNA can be synthesized independent of length, structure, and nucleotide sequence.

show abstract

A Novel Preparation of Nicotinamide Mononucleotide

Abstract: Nicotinamide mononucleotide is conveniently prepared from nicotinamide adenine dinucleotide by specific hydrolysis of the pyrophosphate bond using the Zr4+ ion as catalyst.

Cited by 10 publications

References 5 publications

Probing Hot Spots at Protein−Ligand Binding Sites: A Fragment-Based Approach Using Biophysical Methods

Probing Hot Spots at Protein−Ligand Binding Sites: A Fragment-Based Approach Using Biophysical Methods

Nicotinamide-Containing Di- and Trinucleotides as Chemical Tools for Studies of NAD-Capped RNAs

Synthesis of 5′-NAD-Capped RNA

Contact Info

Product

Resources

About