4229-56-5

Basic information

• Product Name: 1,4-Dihydronicotinamide mononucleotide
• Synonyms: 1,4-Dihydronicotinamide mononucleotide
• CAS NO: 4229-56-5
• Molecular Formula: C₁₁H₁₇N₂O₈P
• Mol File: 4229-56-5.mol
• Article Data: 3

Chemical Properties

• Appearance: /
• CAS DataBase Reference: 1,4-Dihydronicotinamide mononucleotide(CAS DataBase Reference)
• NIST Chemistry Reference: 1,4-Dihydronicotinamide mononucleotide(4229-56-5)
• EPA Substance Registry System: 1,4-Dihydronicotinamide mononucleotide(4229-56-5)

Safety Data

• Hazardous Substances Data: 4229-56-5(Hazardous Substances Data)

Usage

Chemical compound

1,4-Dihydronicotinamide mononucleotide (DH-NMN) is a chemical compound that plays a role in the synthesis of NAD+.

Involvement in biological processes

DH-NMN is involved in various biological processes such as metabolism, DNA repair, and gene expression.

Precursor to NAD+

DH-NMN is a precursor to the coenzyme nicotinamide adenine dinucleotide (NAD+).

Therapeutic effects

DH-NMN is considered to have potential therapeutic effects related to aging, mitochondrial function, and various diseases.

Potential role in increasing NAD+ levels

DH-NMN has been studied for its potential role in increasing NAD+ levels and combating age-related decline.

Potential use in treating conditions

DH-NMN has been studied for its potential use in treating conditions such as obesity, diabetes, and neurodegenerative disorders.

Importance in cellular metabolism

DH-NMN is an important molecule in the field of cellular metabolism.

Attention for potential as a supplement or drug

DH-NMN has garnered attention for its potential as a supplement or drug in promoting healthy aging and treating age-related diseases.

Upstream product

• 58-68-4 NADH 
• 1094-61-7 nicotinamide mononucleotide 
• 75414-16-3 nicotinamide riboside 5'-monophosphate 

Relevant articles and documents

SYNTHETIC METHOD FOR NMN DERIVATIVE AND MEDICAL APPLICATIONS OF NMN AND ITS DERIVATIVE

It relates to use of nicotinamide mononucleotide, in particular, relates to use of nicotinamide mononucleotide for the preparation of a medicament for preventing or alleviating liver injury or liver fibrosis in a subject, and a method for preventing liver injury or liver fibrosis in a subject. It also relates to a method of producing dihydronicotinamide mononucleotide (NMNH) and uses of NMNH.

Human serine racemase is allosterically modulated by NADH and reduced nicotinamide derivatives

Serine racemase catalyzes both the synthesis and the degradation of D-serine, an obligatory co-Agonist of the glutamatergic NMDA receptors. It is allosterically controlled by adenosine triphosphate (ATP), which increases its activity around 7-fold through a cooperative binding mechanism. Serine racemase has been proposed as a drug target for the treatment of several neuropathologies but, so far, the search has been directed only toward the active site, with the identification of a few, low-Affinity inhibitors. Following the recent observation that nicotinamide adenine dinucleotide (reduced form) (NADH) inhibits serine racemase, here we show that the inhibition is partial, with an IC50 of 246 ± 63 μM, several-fold higher than NADH intracellular concentrations. At saturating concentrations of NADH, ATP binds with a 2-fold lower affinity and without co-operativity, suggesting ligand competition. NADH also reduces the weak activity of human serine racemase in the absence of ATP, indicating an additional ATP-independent inhibition mechanism. By dissecting the NADH molecule, we discovered that the inhibitory determinant is the Nsubstituted 1,4-dihydronicotinamide ring. Particularly, the NADH precursor 1,4-dihydronicotinamide mononucleotide exhibited a partial mixed-Type inhibition, with a KI of 18 ± 7 μM. Docking simulations suggested that all 1,4-dihydronicotinamide derivatives bind at the interdimeric interface, with the ring positioned in an unoccupied site next to the ATPbinding site. This newly recognized allosteric site might be exploited for the design of high-Affinity serine racemase effectors to finely modulate D-serine homeostasis.